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><channel><title>Natural Sciences Bibliography &#187; Escherichia</title> <atom:link href="http://scien.net/category/enzyme/escherichia/feed" rel="self" type="application/rss+xml" /><link>http://scien.net</link> <description>190,000 References and 135,000 Tags</description> <lastBuildDate>Sat, 18 May 2013 07:38:21 +0000</lastBuildDate> <language>en-US</language> <sy:updatePeriod>hourly</sy:updatePeriod> <sy:updateFrequency>1</sy:updateFrequency> <generator>http://wordpress.org/?v=3.5.1</generator> <item><title>Genetic analysis of Escherichia coli from porcine postweaning diarrhoea</title><link>http://scien.net/enzyme/escherichia/genetic-analysis-of-escherichia-coli-from-porcine-postweaning-diarrhoea</link> <comments>http://scien.net/enzyme/escherichia/genetic-analysis-of-escherichia-coli-from-porcine-postweaning-diarrhoea#comments</comments> <pubDate>Sat, 18 May 2013 07:09:18 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Escherichia]]></category> <category><![CDATA[unweaned]]></category><guid
isPermaLink="false">http://scien.net/enzyme/escherichia/genetic-analysis-of-escherichia-coli-from-porcine-postweaning-diarrhoea</guid> <description><![CDATA[Hampson, D. J.; Woodward, J. M.; Connaughton, I. D., 1993: Genetic analysis of Escherichia coli from porcine postweaning diarrhoea. Epidemiology &#038; Infection. 110(3): 575-581 A total of 79 Australian isolates of beta-haemolytic Escherichia coli from cases of porcine postweaning diarrhoea (Pwd), and 18 isolates of serotype 0149:k91:k88 (F4) from unweaned pigs from Australia, Indonesia and [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/escherichia/genetic-analysis-of-escherichia-coli-from-porcine-postweaning-diarrhoea/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Functional assignment of Erwinia herbicola Eho10 carotenoid genes expressed in Escherichia coli</title><link>http://scien.net/enzyme/escherichia/functional-assignment-of-erwinia-herbicola-eho10-carotenoid-genes-expressed-in-escherichia-coli</link> <comments>http://scien.net/enzyme/escherichia/functional-assignment-of-erwinia-herbicola-eho10-carotenoid-genes-expressed-in-escherichia-coli#comments</comments> <pubDate>Sat, 18 May 2013 07:02:01 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Escherichia]]></category> <category><![CDATA[diglucoside]]></category> <category><![CDATA[geranylgeranyl]]></category> <category><![CDATA[herbicola]]></category> <category><![CDATA[nonphotosynthetic]]></category> <category><![CDATA[phytoene]]></category><guid
isPermaLink="false">http://scien.net/enzyme/escherichia/functional-assignment-of-erwinia-herbicola-eho10-carotenoid-genes-expressed-in-escherichia-coli</guid> <description><![CDATA[Hundle, B.; Alberti, M.; Nievelstein, V.; Beyer, P.; Kleinig, H.; Armstrong, G. A.; Burke, D. H.; Hearst, J. E., 1994: Functional assignment of Erwinia herbicola Eho10 carotenoid genes expressed in Escherichia coli. Molecular &#038; General Genetics. 245(4): 406-416 Erwinia herbicola is a nonphotosynthetic bacterium that is yellow pigmented due to the presence of carotenoids. When [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/escherichia/functional-assignment-of-erwinia-herbicola-eho10-carotenoid-genes-expressed-in-escherichia-coli/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Functional analysis of a leucine aminopeptidase from Solanum tuberosum L</title><link>http://scien.net/enzyme/escherichia/functional-analysis-of-a-leucine-aminopeptidase-from-solanum-tuberosum-l</link> <comments>http://scien.net/enzyme/escherichia/functional-analysis-of-a-leucine-aminopeptidase-from-solanum-tuberosum-l#comments</comments> <pubDate>Sat, 18 May 2013 07:01:40 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Escherichia]]></category> <category><![CDATA[bestatin]]></category> <category><![CDATA[homohexameric]]></category> <category><![CDATA[parallelled]]></category><guid
isPermaLink="false">http://scien.net/enzyme/escherichia/functional-analysis-of-a-leucine-aminopeptidase-from-solanum-tuberosum-l</guid> <description><![CDATA[Herbers, K; Prat, S; Willmitzer, L., 1994: Functional analysis of a leucine aminopeptidase from Solanum tuberosum L. Planta 94(2): 230-240 A protein encoded by a potato cDNA homologous to a leucine aminopeptidase (Lap) from bovine lens (Hildmann et al. 1992) was expressed in Escherichia coli cells and biochemically characterized by hydrolysis of leucine &#8211; Activity [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/escherichia/functional-analysis-of-a-leucine-aminopeptidase-from-solanum-tuberosum-l/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Fitness, flux and phantoms in temporally variable environments</title><link>http://scien.net/enzyme/escherichia/fitness-flux-and-phantoms-in-temporally-variable-environments</link> <comments>http://scien.net/enzyme/escherichia/fitness-flux-and-phantoms-in-temporally-variable-environments#comments</comments> <pubDate>Sat, 18 May 2013 06:47:58 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Escherichia]]></category> <category><![CDATA[skepticism]]></category><guid
isPermaLink="false">http://scien.net/enzyme/escherichia/fitness-flux-and-phantoms-in-temporally-variable-environments</guid> <description><![CDATA[Dean, A. M., 1994: Fitness, flux and phantoms in temporally variable environments. Genetics 136(4): 1481-1495 The evolutionary problem of selection in temporally variable environments is addressed by investigating a metabolic model describing the approach to steady state of a flux emanating from a simple linear pathway of unsaturated enzymes catalyzing reversible monomolecular reactions. Analysis confirms [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/escherichia/fitness-flux-and-phantoms-in-temporally-variable-environments/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Fibrobacter succinogenes S85 possesses at least nine distinct glucanase genes</title><link>http://scien.net/enzyme/escherichia/fibrobacter-succinogenes-s85-possesses-at-least-nine-distinct-glucanase-genes</link> <comments>http://scien.net/enzyme/escherichia/fibrobacter-succinogenes-s85-possesses-at-least-nine-distinct-glucanase-genes#comments</comments> <pubDate>Sat, 18 May 2013 06:43:44 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Escherichia]]></category> <category><![CDATA[dashii]]></category> <category><![CDATA[dextrinase]]></category> <category><![CDATA[fibrobacter]]></category> <category><![CDATA[laminarin]]></category> <category><![CDATA[lichenan]]></category> <category><![CDATA[lichenase]]></category> <category><![CDATA[succinogenes]]></category> <category><![CDATA[zymogram]]></category><guid
isPermaLink="false">http://scien.net/enzyme/escherichia/fibrobacter-succinogenes-s85-possesses-at-least-nine-distinct-glucanase-genes</guid> <description><![CDATA[Malburg, Laercio M.Jr.; Forsberg, Cecil W., 1993: Fibrobacter succinogenes S85 possesses at least nine distinct glucanase genes. Canadian Journal Of Microbiology. 39(9): 882-891 The construction of genomic libraries of Fibrobacter succinogenes S85 in lambda-Dash, lambda-DashII, and pUC19, and the screening of recombinant clones for carboxymethylcellulose hydrolysis yielded 38 glucanase clones. These clones along with a [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/escherichia/fibrobacter-succinogenes-s85-possesses-at-least-nine-distinct-glucanase-genes/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Fibrobacter succinogenes S85 has multiple xylanase genes</title><link>http://scien.net/enzyme/escherichia/fibrobacter-succinogenes-s85-has-multiple-xylanase-genes</link> <comments>http://scien.net/enzyme/escherichia/fibrobacter-succinogenes-s85-has-multiple-xylanase-genes#comments</comments> <pubDate>Sat, 18 May 2013 06:43:44 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Escherichia]]></category> <category><![CDATA[cellobiosidase]]></category> <category><![CDATA[cotained]]></category> <category><![CDATA[endoxylanase]]></category> <category><![CDATA[fibrobacter]]></category> <category><![CDATA[succinogenes]]></category> <category><![CDATA[xylanases]]></category> <category><![CDATA[xylobiose]]></category> <category><![CDATA[xylooligosaccharides]]></category> <category><![CDATA[zymograms]]></category><guid
isPermaLink="false">http://scien.net/enzyme/escherichia/fibrobacter-succinogenes-s85-has-multiple-xylanase-genes</guid> <description><![CDATA[Malburg, L. M.Jr.; Smith, D. C.; Schellhorn, H. E.; Forsberg, C. W., 1993: Fibrobacter succinogenes S85 has multiple xylanase genes. Journal Of Applied Bacteriology. 75(6): 564-573 Four distinct Dna fragments encoding xylanase activities, pBX1.2, pXC30.2, pX14 and Lx31, were cloned from plasmid and lambda libraries constructed using genomic Dna from Fibrobacter succinogenes S8 pBX1.2 cotained [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/escherichia/fibrobacter-succinogenes-s85-has-multiple-xylanase-genes/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Expression of the betaine aldehyde dehydrogenase gene in barley in response to osmotic stress and abscisic acid</title><link>http://scien.net/enzyme/escherichia/expression-of-the-betaine-aldehyde-dehydrogenase-gene-in-barley-in-response-to-osmotic-stress-and-abscisic-acid</link> <comments>http://scien.net/enzyme/escherichia/expression-of-the-betaine-aldehyde-dehydrogenase-gene-in-barley-in-response-to-osmotic-stress-and-abscisic-acid#comments</comments> <pubDate>Sat, 18 May 2013 06:31:44 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Escherichia]]></category> <category><![CDATA[badh]]></category> <category><![CDATA[osmoprotectant]]></category><guid
isPermaLink="false">http://scien.net/enzyme/escherichia/expression-of-the-betaine-aldehyde-dehydrogenase-gene-in-barley-in-response-to-osmotic-stress-and-abscisic-acid</guid> <description><![CDATA[Ishitani, M; Nakamura, T; Han, Sy; Takabe, T., 1995: Expression of the betaine aldehyde dehydrogenase gene in barley in response to osmotic stress and abscisic acid. Plant molecular biology 27(2): 307-315 When subjected to salt stress or drought, some vascular plants such as barley respond with an increased accumulation of the osmoprotectant glycine betaine (betaine), [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/escherichia/expression-of-the-betaine-aldehyde-dehydrogenase-gene-in-barley-in-response-to-osmotic-stress-and-abscisic-acid/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Expression of a plant sesquiterpene cyclase gene in Escherichia coli</title><link>http://scien.net/enzyme/escherichia/expression-of-a-plant-sesquiterpene-cyclase-gene-in-escherichia-coli</link> <comments>http://scien.net/enzyme/escherichia/expression-of-a-plant-sesquiterpene-cyclase-gene-in-escherichia-coli#comments</comments> <pubDate>Sat, 18 May 2013 06:30:06 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Escherichia]]></category> <category><![CDATA[argentation]]></category> <category><![CDATA[aristolochene]]></category> <category><![CDATA[nonchallenged]]></category><guid
isPermaLink="false">http://scien.net/enzyme/escherichia/expression-of-a-plant-sesquiterpene-cyclase-gene-in-escherichia-coli</guid> <description><![CDATA[Back, K; Yin, S; Chappell, J., 1994: Expression of a plant sesquiterpene cyclase gene in Escherichia coli. Archives of biochemistry and biophysics 315(2): 527-532 5-Epi-aristolochene synthase is a sesquiterpene cyclase activity found in pathogen-challenged tobacco cells, but not in nonchallenged tissues, and appears to be encoded by a complex gene family. As a prerequisite to [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/escherichia/expression-of-a-plant-sesquiterpene-cyclase-gene-in-escherichia-coli/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Expression of Semliki Forest virus nsP1-specific methyltransferase in insect cells and in Escherichia coli</title><link>http://scien.net/enzyme/escherichia/expression-of-semliki-forest-virus-nsp1-specific-methyltransferase-in-insect-cells-and-in-escherichia-coli</link> <comments>http://scien.net/enzyme/escherichia/expression-of-semliki-forest-virus-nsp1-specific-methyltransferase-in-insect-cells-and-in-escherichia-coli#comments</comments> <pubDate>Sat, 18 May 2013 06:29:47 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Escherichia]]></category> <category><![CDATA[acnpv]]></category> <category><![CDATA[dgtp]]></category> <category><![CDATA[gpppa]]></category> <category><![CDATA[gpppg]]></category> <category><![CDATA[semliki]]></category><guid
isPermaLink="false">http://scien.net/enzyme/escherichia/expression-of-semliki-forest-virus-nsp1-specific-methyltransferase-in-insect-cells-and-in-escherichia-coli</guid> <description><![CDATA[&#8220;Laakkonen, Pirjo; Hyvonen, Marko; Peranen, Johan; Kaariainen, Leevi, 1994: Expression of Semliki Forest virus nsP1-specific methyltransferase in insect cells and in Escherichia coli. Journal Of Virology. 68(11): 7418-7425 We have expressed the Semliki Forest virus (Sfv)-specific nonstructural protein nsP1 both in insect cells and in Escherichia coli in the absence of other viral proteins. A [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/escherichia/expression-of-semliki-forest-virus-nsp1-specific-methyltransferase-in-insect-cells-and-in-escherichia-coli/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Expression in Escherichia coli and partial characterization of two tyrosine/dopa decarboxylases from opium poppy</title><link>http://scien.net/enzyme/escherichia/expression-in-escherichia-coli-and-partial-characterization-of-two-tyrosinedopa-decarboxylases-from-opium-poppy</link> <comments>http://scien.net/enzyme/escherichia/expression-in-escherichia-coli-and-partial-characterization-of-two-tyrosinedopa-decarboxylases-from-opium-poppy#comments</comments> <pubDate>Sat, 18 May 2013 06:29:33 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Escherichia]]></category> <category><![CDATA[decarboxylases]]></category> <category><![CDATA[somniferum]]></category> <category><![CDATA[tyrosinedopa]]></category><guid
isPermaLink="false">http://scien.net/enzyme/escherichia/expression-in-escherichia-coli-and-partial-characterization-of-two-tyrosinedopa-decarboxylases-from-opium-poppy</guid> <description><![CDATA[Facchini, Peter J.; De Luca, Vincenzo, 1995: Expression in Escherichia coli and partial characterization of two tyrosine/dopa decarboxylases from opium poppy. Phytochemistry (oxford). 38(5): 1119-1126 Two tyrosine/dopa decarboxylases (Tydc1 and Tydc2) from opium poppy (Papaver somniferum) were heterologously expressed in Escherichia coli and partially characterized. Tydc1 and Tydc2 are representative members of the two major [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/escherichia/expression-in-escherichia-coli-and-partial-characterization-of-two-tyrosinedopa-decarboxylases-from-opium-poppy/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Expression and identification of the strA-strB gene pair from streptomycin-resistant Erwinia amylovora</title><link>http://scien.net/enzyme/escherichia/expression-and-identification-of-the-stra-strb-gene-pair-from-streptomycin-resistant-erwinia-amylovora</link> <comments>http://scien.net/enzyme/escherichia/expression-and-identification-of-the-stra-strb-gene-pair-from-streptomycin-resistant-erwinia-amylovora#comments</comments> <pubDate>Sat, 18 May 2013 06:29:16 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Escherichia]]></category> <category><![CDATA[dalgarno]]></category> <category><![CDATA[lacl]]></category> <category><![CDATA[stra]]></category> <category><![CDATA[strb]]></category><guid
isPermaLink="false">http://scien.net/enzyme/escherichia/expression-and-identification-of-the-stra-strb-gene-pair-from-streptomycin-resistant-erwinia-amylovora</guid> <description><![CDATA[&#8220;Chiou, C.S.; Jones, A. L., 1995: Expression and identification of the strA-strB gene pair from streptomycin-resistant Erwinia amylovora. Gene (amsterdam). 152(1): 47-51 Deletions in either of the genes in the strA-strB gene pair of Erwinia amylovora plasmid pEa34 resulted in a dramatic decrease in streptomycin resistance (Sm-R), but Sm-R was restored to high levels by [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/escherichia/expression-and-identification-of-the-stra-strb-gene-pair-from-streptomycin-resistant-erwinia-amylovora/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Ethanol from lignocellulosic wastes with utilization of recombinant bacteria</title><link>http://scien.net/enzyme/escherichia/ethanol-from-lignocellulosic-wastes-with-utilization-of-recombinant-bacteria</link> <comments>http://scien.net/enzyme/escherichia/ethanol-from-lignocellulosic-wastes-with-utilization-of-recombinant-bacteria#comments</comments> <pubDate>Sat, 18 May 2013 06:11:49 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Escherichia]]></category> <category><![CDATA[bioenergy]]></category> <category><![CDATA[cellotriose]]></category> <category><![CDATA[gainesville]]></category> <category><![CDATA[ingram]]></category> <category><![CDATA[katzen]]></category> <category><![CDATA[lonnie]]></category> <category><![CDATA[oxytoca]]></category> <category><![CDATA[prehydrolysis]]></category> <category><![CDATA[raphael]]></category> <category><![CDATA[saccharification]]></category><guid
isPermaLink="false">http://scien.net/enzyme/escherichia/ethanol-from-lignocellulosic-wastes-with-utilization-of-recombinant-bacteria</guid> <description><![CDATA[Katzen, Raphael; Fowler, David E., 1994: Ethanol from lignocellulosic wastes with utilization of recombinant bacteria. Applied Biochemistry &#038; Biotechnology. 45-46(0): 697-707 This article presents the advanced technology that has been developed by BioEnergy International of Gainesville, Florida, utilizing novel recombinant strains of bacteria developed by Lonnie Ingram of the University of Florida. The first commercial [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/escherichia/ethanol-from-lignocellulosic-wastes-with-utilization-of-recombinant-bacteria/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Erwinia chrysanthemi hrp genes and their involvement in soft rot pathogenesis and elicitation of the hypersensitive response</title><link>http://scien.net/enzyme/escherichia/erwinia-chrysanthemi-hrp-genes-and-their-involvement-in-soft-rot-pathogenesis-and-elicitation-of-the-hypersensitive-response</link> <comments>http://scien.net/enzyme/escherichia/erwinia-chrysanthemi-hrp-genes-and-their-involvement-in-soft-rot-pathogenesis-and-elicitation-of-the-hypersensitive-response#comments</comments> <pubDate>Sat, 18 May 2013 06:06:46 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Escherichia]]></category> <category><![CDATA[cosmids]]></category> <category><![CDATA[macerates]]></category> <category><![CDATA[macerating]]></category> <category><![CDATA[pectate]]></category> <category><![CDATA[pelabce]]></category><guid
isPermaLink="false">http://scien.net/enzyme/escherichia/erwinia-chrysanthemi-hrp-genes-and-their-involvement-in-soft-rot-pathogenesis-and-elicitation-of-the-hypersensitive-response</guid> <description><![CDATA[Bauer, David W.; Bogdanove, Adam J.; Beer, Steven V.; Collmer, Alan, 1994: Erwinia chrysanthemi hrp genes and their involvement in soft rot pathogenesis and elicitation of the hypersensitive response. Molecular Plant-Microbe Interactions. 7(5): 573-581 Unlike the bacterial pathogens that typically cause the hypersensitive response (Hr) in plants, Erwinia chrysanthemi has a wide host range, rapidly [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/escherichia/erwinia-chrysanthemi-hrp-genes-and-their-involvement-in-soft-rot-pathogenesis-and-elicitation-of-the-hypersensitive-response/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Effects of high levels of selenite and Escherichia coli on enrichment of Salmonella and detection of Salmonella by polymyxin-cloth enzyme immunoassay</title><link>http://scien.net/enzyme/escherichia/effects-of-high-levels-of-selenite-and-escherichia-coli-on-enrichment-of-salmonella-and-detection-of-salmonella-by-polymyxin-cloth-enzyme-immunoassay</link> <comments>http://scien.net/enzyme/escherichia/effects-of-high-levels-of-selenite-and-escherichia-coli-on-enrichment-of-salmonella-and-detection-of-salmonella-by-polymyxin-cloth-enzyme-immunoassay#comments</comments> <pubDate>Fri, 17 May 2013 03:22:05 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Escherichia]]></category><guid
isPermaLink="false">http://scien.net/enzyme/escherichia/effects-of-high-levels-of-selenite-and-escherichia-coli-on-enrichment-of-salmonella-and-detection-of-salmonella-by-polymyxin-cloth-enzyme-immunoassay</guid> <description><![CDATA[Chen, Hong; Hayashi, Satoko; Yamazaki, Hiroshi, 1995: Effects of high levels of selenite and Escherichia coli on enrichment of Salmonella and detection of Salmonella by polymyxin-cloth enzyme immunoassay. International Journal Of Food Microbiology. 25(2): 119-129 The effect of various concentrations of selenite on the recovery of Salmonella typhimurium and Escherichia coli was examined in a [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/escherichia/effects-of-high-levels-of-selenite-and-escherichia-coli-on-enrichment-of-salmonella-and-detection-of-salmonella-by-polymyxin-cloth-enzyme-immunoassay/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Effects of concanavalin A and pokeweed lectins on microvillar membrane proteins during the organ culture of rabbit intestinal mucosa</title><link>http://scien.net/enzyme/escherichia/effects-of-concanavalin-a-and-pokeweed-lectins-on-microvillar-membrane-proteins-during-the-organ-culture-of-rabbit-intestinal-mucosa</link> <comments>http://scien.net/enzyme/escherichia/effects-of-concanavalin-a-and-pokeweed-lectins-on-microvillar-membrane-proteins-during-the-organ-culture-of-rabbit-intestinal-mucosa#comments</comments> <pubDate>Fri, 17 May 2013 03:14:45 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Escherichia]]></category> <category><![CDATA[epec]]></category> <category><![CDATA[microvillar]]></category> <category><![CDATA[vesiculation]]></category><guid
isPermaLink="false">http://scien.net/enzyme/escherichia/effects-of-concanavalin-a-and-pokeweed-lectins-on-microvillar-membrane-proteins-during-the-organ-culture-of-rabbit-intestinal-mucosa</guid> <description><![CDATA[Embaye, H.; Whybrew, L.; Odedra, R. M.; Hart, C. A.; Fletcher, J. N.; Saunders, J. R.; Batt, R. M., 1995: Effects of concanavalin A and pokeweed lectins on microvillar membrane proteins during the organ culture of rabbit intestinal mucosa. Research In Veterinary Science. 59(1): 50-55 The effects of pokeweed lectin (Pwl) and concanavalin A (Con [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/escherichia/effects-of-concanavalin-a-and-pokeweed-lectins-on-microvillar-membrane-proteins-during-the-organ-culture-of-rabbit-intestinal-mucosa/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Direct isolation of functional genes encoding cellulases from the microbial consortia in a thermophilic, anaerobic digester maintained on lignocellulose</title><link>http://scien.net/enzyme/escherichia/direct-isolation-of-functional-genes-encoding-cellulases-from-the-microbial-consortia-in-a-thermophilic-anaerobic-digester-maintained-on-lignocellulose</link> <comments>http://scien.net/enzyme/escherichia/direct-isolation-of-functional-genes-encoding-cellulases-from-the-microbial-consortia-in-a-thermophilic-anaerobic-digester-maintained-on-lignocellulose#comments</comments> <pubDate>Fri, 17 May 2013 02:12:32 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Escherichia]]></category> <category><![CDATA[celb]]></category> <category><![CDATA[cellobiopyranoside]]></category> <category><![CDATA[cellulosa]]></category> <category><![CDATA[digesters]]></category> <category><![CDATA[feedstocks]]></category> <category><![CDATA[lignocellulose]]></category> <category><![CDATA[methylumbelliferyl]]></category> <category><![CDATA[thermocellum]]></category> <category><![CDATA[xylosidase]]></category><guid
isPermaLink="false">http://scien.net/enzyme/escherichia/direct-isolation-of-functional-genes-encoding-cellulases-from-the-microbial-consortia-in-a-thermophilic-anaerobic-digester-maintained-on-lignocellulose</guid> <description><![CDATA[&#8220;Healy, Fg; Ray, Rm; Aldrich, Hc; Wilkie, Ac; Ingram, Lo; Shanmugam, Kt, 1995: Direct isolation of functional genes encoding cellulases from the microbial consortia in a thermophilic, anaerobic digester maintained on lignocellulose. Applied microbiology and biotechnology 43(4): 667-674 Gene libraries (&#8220;&#8221;zoolibraries&#8221;") were constructed in Escherichia coli using Dna isolated from the mixed liquor of thermophilic, [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/escherichia/direct-isolation-of-functional-genes-encoding-cellulases-from-the-microbial-consortia-in-a-thermophilic-anaerobic-digester-maintained-on-lignocellulose/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Dihydrolipoamide dehydrogenase in the Trypanosoma subgenus, Trypanozoon</title><link>http://scien.net/enzyme/escherichia/dihydrolipoamide-dehydrogenase-in-the-trypanosoma-subgenus-trypanozoon</link> <comments>http://scien.net/enzyme/escherichia/dihydrolipoamide-dehydrogenase-in-the-trypanosoma-subgenus-trypanozoon#comments</comments> <pubDate>Fri, 17 May 2013 02:11:12 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Escherichia]]></category> <category><![CDATA[dihydrolipoamide]]></category> <category><![CDATA[gambiense]]></category> <category><![CDATA[procyclic]]></category> <category><![CDATA[rhodesiense]]></category> <category><![CDATA[salivarian]]></category> <category><![CDATA[stercorarian]]></category> <category><![CDATA[trypanozoon]]></category><guid
isPermaLink="false">http://scien.net/enzyme/escherichia/dihydrolipoamide-dehydrogenase-in-the-trypanosoma-subgenus-trypanozoon</guid> <description><![CDATA[Else, Anthony J.; Clarke, James F.; Willis, Anthony; Jackman, Simon A.; Hough, David W.; Danson, Michael J., 1994: Dihydrolipoamide dehydrogenase in the Trypanosoma subgenus, Trypanozoon. Molecular &#038; Biochemical Parasitology. 64(2): 233-239 The enzyme dihydrolipoamide dehydrogenase has been discovered and characterized in four salivarian trypanosomes of the subgenus trypanozoon: Trypanosoma brucei brucei, T. b. gambiense, T. [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/escherichia/dihydrolipoamide-dehydrogenase-in-the-trypanosoma-subgenus-trypanozoon/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Development of gusA reporter gene constructs for cereal transformation: availability of plant transformation vectors from the CAMBIA Molecular Genetic Resource Service</title><link>http://scien.net/enzyme/escherichia/development-of-gusa-reporter-gene-constructs-for-cereal-transformation-availability-of-plant-transformation-vectors-from-the-cambia-molecular-genetic-resource-service</link> <comments>http://scien.net/enzyme/escherichia/development-of-gusa-reporter-gene-constructs-for-cereal-transformation-availability-of-plant-transformation-vectors-from-the-cambia-molecular-genetic-resource-service#comments</comments> <pubDate>Wed, 15 May 2013 03:23:37 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Escherichia]]></category> <category><![CDATA[cambia]]></category> <category><![CDATA[gusa]]></category><guid
isPermaLink="false">http://scien.net/enzyme/escherichia/development-of-gusa-reporter-gene-constructs-for-cereal-transformation-availability-of-plant-transformation-vectors-from-the-cambia-molecular-genetic-resource-service</guid> <description><![CDATA[McElroy, D.; Chamberlain, D. A.; Moon, E.; Wilson, K. J., 1995: Development of gusA reporter gene constructs for cereal transformation: availability of plant transformation vectors from the CAMBIA Molecular Genetic Resource Service. Molecular Breeding 1(1): 27-37 The use of reporter genes to characterise sequence elements that act to regulate gene expression in transgenic plants has [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/escherichia/development-of-gusa-reporter-gene-constructs-for-cereal-transformation-availability-of-plant-transformation-vectors-from-the-cambia-molecular-genetic-resource-service/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Controlled expression and structural organization of a Lactococcus lactis bacteriophage lysin encoded by two overlapping genes</title><link>http://scien.net/enzyme/escherichia/controlled-expression-and-structural-organization-of-a-lactococcus-lactis-bacteriophage-lysin-encoded-by-two-overlapping-genes</link> <comments>http://scien.net/enzyme/escherichia/controlled-expression-and-structural-organization-of-a-lactococcus-lactis-bacteriophage-lysin-encoded-by-two-overlapping-genes#comments</comments> <pubDate>Wed, 15 May 2013 02:48:31 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Escherichia]]></category> <category><![CDATA[holin]]></category> <category><![CDATA[lactococci]]></category> <category><![CDATA[lysin]]></category> <category><![CDATA[lysozymes]]></category> <category><![CDATA[methionines]]></category><guid
isPermaLink="false">http://scien.net/enzyme/escherichia/controlled-expression-and-structural-organization-of-a-lactococcus-lactis-bacteriophage-lysin-encoded-by-two-overlapping-genes</guid> <description><![CDATA[Sherman, Claire A.; Jury, Karen L.; Gasson, Michael J., 1994: Controlled expression and structural organization of a Lactococcus lactis bacteriophage lysin encoded by two overlapping genes. Applied &#038; Environmental Microbiology. 60(9): 3063-3073 The phi-Ml3 bacteriophage lysin is specific for lactococci and could be used to promote enzyme release during cheese manufacture. The level of lysin [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/escherichia/controlled-expression-and-structural-organization-of-a-lactococcus-lactis-bacteriophage-lysin-encoded-by-two-overlapping-genes/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Comparative complement selection in bacteria enables screening for lead compounds targeted to a purine salvage enzyme of parasites</title><link>http://scien.net/enzyme/escherichia/comparative-complement-selection-in-bacteria-enables-screening-for-lead-compounds-targeted-to-a-purine-salvage-enzyme-of-parasites</link> <comments>http://scien.net/enzyme/escherichia/comparative-complement-selection-in-bacteria-enables-screening-for-lead-compounds-targeted-to-a-purine-salvage-enzyme-of-parasites#comments</comments> <pubDate>Wed, 15 May 2013 02:24:49 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Escherichia]]></category> <category><![CDATA[hprts]]></category> <category><![CDATA[semidefined]]></category> <category><![CDATA[tritrichomonas]]></category><guid
isPermaLink="false">http://scien.net/enzyme/escherichia/comparative-complement-selection-in-bacteria-enables-screening-for-lead-compounds-targeted-to-a-purine-salvage-enzyme-of-parasites</guid> <description><![CDATA[Eakin, Ann E.; Nieves Alicea, Rene; Tosado Acevedo, Rafael; Chin, Marian S.; Wang, Ching C.; Craig, Sydney P.IIi, 1995: Comparative complement selection in bacteria enables screening for lead compounds targeted to a purine salvage enzyme of parasites. Antimicrobial Agents &#038; Chemotherapy. 39(3): 620-625 Expression plasmids encoding the hypoxanthine phosphoribosyltransferases (HPRTs) of Plasmodium falciparum, Schistosoma mansoni, [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/escherichia/comparative-complement-selection-in-bacteria-enables-screening-for-lead-compounds-targeted-to-a-purine-salvage-enzyme-of-parasites/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Cloning, expression, and characterization of cDNAs encoding Arabidopsis thaliana squalene synthase</title><link>http://scien.net/enzyme/escherichia/cloning-expression-and-characterization-of-cdnas-encoding-arabidopsis-thaliana-squalene-synthase</link> <comments>http://scien.net/enzyme/escherichia/cloning-expression-and-characterization-of-cdnas-encoding-arabidopsis-thaliana-squalene-synthase#comments</comments> <pubDate>Wed, 15 May 2013 02:15:02 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Escherichia]]></category> <category><![CDATA[dehydrosqualene]]></category> <category><![CDATA[phytoene]]></category><guid
isPermaLink="false">http://scien.net/enzyme/escherichia/cloning-expression-and-characterization-of-cdnas-encoding-arabidopsis-thaliana-squalene-synthase</guid> <description><![CDATA[Nakashima, T; Inoue, T; Oka, A; Nishino, T; Osumi, T; Hata, S., 1995: Cloning, expression, and characterization of cDNAs encoding Arabidopsis thaliana squalene synthase. Proceedings of the National Academy of Sciences of the United States of America, 92(6): 2328-2332 We have isolated and characterized two overlapping cDNA clones for Arabidopsis thaliana squalene synthase. Their nucleotide [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/escherichia/cloning-expression-and-characterization-of-cdnas-encoding-arabidopsis-thaliana-squalene-synthase/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Cloning of the genes for degradation of the herbicides EPTC (S-ethyl dipropylthiocarbamate) and atrazine from Rhodococcus sp. strain TE1</title><link>http://scien.net/enzyme/escherichia/cloning-of-the-genes-for-degradation-of-the-herbicides-eptc-s-ethyl-dipropylthiocarbamate-and-atrazine-from-rhodococcus-sp-strain-te1</link> <comments>http://scien.net/enzyme/escherichia/cloning-of-the-genes-for-degradation-of-the-herbicides-eptc-s-ethyl-dipropylthiocarbamate-and-atrazine-from-rhodococcus-sp-strain-te1#comments</comments> <pubDate>Wed, 15 May 2013 02:14:37 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Escherichia]]></category> <category><![CDATA[dealkylation]]></category> <category><![CDATA[dipropylthiocarbamate]]></category> <category><![CDATA[electroporated]]></category> <category><![CDATA[epta]]></category> <category><![CDATA[isopropylamino]]></category> <category><![CDATA[kpni]]></category><guid
isPermaLink="false">http://scien.net/enzyme/escherichia/cloning-of-the-genes-for-degradation-of-the-herbicides-eptc-s-ethyl-dipropylthiocarbamate-and-atrazine-from-rhodococcus-sp-strain-te1</guid> <description><![CDATA[Shao, Z. Q.; Behki, R., 1995: Cloning of the genes for degradation of the herbicides EPTC (S-ethyl dipropylthiocarbamate) and atrazine from Rhodococcus sp. strain TE1. Applied and Environmental Microbiology 61(5): 2061-2065 The degradation of the herbicides Eptc (S-ethyl dipropylthiocarbamate) and atrazine (2-chloro-4-ethyl-amino-6-isopropylamino-1,3,5-triazine) is associated with an indigenous plasmid in Rhodococcus sp. strain Te Plasmid Dna [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/escherichia/cloning-of-the-genes-for-degradation-of-the-herbicides-eptc-s-ethyl-dipropylthiocarbamate-and-atrazine-from-rhodococcus-sp-strain-te1/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Cloning and regulation of flavonol 3-sulfotransferase in cell-suspension cultures of Flaveria bidentis</title><link>http://scien.net/enzyme/escherichia/cloning-and-regulation-of-flavonol-3-sulfotransferase-in-cell-suspension-cultures-of-flaveria-bidentis</link> <comments>http://scien.net/enzyme/escherichia/cloning-and-regulation-of-flavonol-3-sulfotransferase-in-cell-suspension-cultures-of-flaveria-bidentis#comments</comments> <pubDate>Wed, 15 May 2013 02:12:52 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Escherichia]]></category> <category><![CDATA[bidentis]]></category> <category><![CDATA[flaveria]]></category> <category><![CDATA[polysulfates]]></category> <category><![CDATA[rhamnetin]]></category> <category><![CDATA[sulfotransferases]]></category> <category><![CDATA[trisulfate]]></category><guid
isPermaLink="false">http://scien.net/enzyme/escherichia/cloning-and-regulation-of-flavonol-3-sulfotransferase-in-cell-suspension-cultures-of-flaveria-bidentis</guid> <description><![CDATA[Ananvoranich, S; Varin, L; Gulick, P; Ibrahim, R., 1994: Cloning and regulation of flavonol 3-sulfotransferase in cell-suspension cultures of Flaveria bidentis. Plant physiology 106(2): 485-491 Flaveria spp. accumulate flavonol sulfate esters whose biosynthesis is catalyzed by a number of position-specific flavonol sulfotransferases. Although the accumulation of sulfated flavonols appears to be tissue specific and developmentally [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/escherichia/cloning-and-regulation-of-flavonol-3-sulfotransferase-in-cell-suspension-cultures-of-flaveria-bidentis/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Cloning and nucleotide sequence analysis of the Lactobacillus delbrueckii ssp. lactis DSM7290 cysteine aminopeptidase gene pepC</title><link>http://scien.net/enzyme/escherichia/cloning-and-nucleotide-sequence-analysis-of-the-lactobacillus-delbrueckii-ssp-lactis-dsm7290-cysteine-aminopeptidase-gene-pepc</link> <comments>http://scien.net/enzyme/escherichia/cloning-and-nucleotide-sequence-analysis-of-the-lactobacillus-delbrueckii-ssp-lactis-dsm7290-cysteine-aminopeptidase-gene-pepc#comments</comments> <pubDate>Wed, 15 May 2013 02:12:41 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Escherichia]]></category> <category><![CDATA[icus]]></category> <category><![CDATA[naphthylamide]]></category> <category><![CDATA[pepc]]></category><guid
isPermaLink="false">http://scien.net/enzyme/escherichia/cloning-and-nucleotide-sequence-analysis-of-the-lactobacillus-delbrueckii-ssp-lactis-dsm7290-cysteine-aminopeptidase-gene-pepc</guid> <description><![CDATA[Klein, J. R.; Henrich, B.; Plapp, R., 1994: Cloning and nucleotide sequence analysis of the Lactobacillus delbrueckii ssp. lactis DSM7290 cysteine aminopeptidase gene pepC. FEMS Microbiology Letters 124(3): 291-300 A genomic library of Lactobacillus delbrueckii ssp. lactis Dsm7290 in the low copy number vector pLG339, was screened for the presence of peptidase genes. Using the [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/escherichia/cloning-and-nucleotide-sequence-analysis-of-the-lactobacillus-delbrueckii-ssp-lactis-dsm7290-cysteine-aminopeptidase-gene-pepc/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Cloning and heterologous expression of the Candida albicans gene PMI 1 encoding phosphomannose isomerase</title><link>http://scien.net/enzyme/escherichia/cloning-and-heterologous-expression-of-the-candida-albicans-gene-pmi-1-encoding-phosphomannose-isomerase</link> <comments>http://scien.net/enzyme/escherichia/cloning-and-heterologous-expression-of-the-candida-albicans-gene-pmi-1-encoding-phosphomannose-isomerase#comments</comments> <pubDate>Wed, 15 May 2013 02:12:30 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Escherichia]]></category> <category><![CDATA[phosphomannose]]></category><guid
isPermaLink="false">http://scien.net/enzyme/escherichia/cloning-and-heterologous-expression-of-the-candida-albicans-gene-pmi-1-encoding-phosphomannose-isomerase</guid> <description><![CDATA[Smith, David J.; Proudfoot, Amanda E. I.; Detiani, Mariastella; Wells, Timothy N. C.; Payton, Mark A., 1995: Cloning and heterologous expression of the Candida albicans gene PMI 1 encoding phosphomannose isomerase. Yeast. 11(4): 301-310 Using a Dna fragment derived from the Saccharomyces cerevisiae phosphomannose isomerase (Pmi) structural gene as a probe against a random ordered [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/escherichia/cloning-and-heterologous-expression-of-the-candida-albicans-gene-pmi-1-encoding-phosphomannose-isomerase/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Cloning and expression of the soybean DapA gene encoding dihydrodipicolinate synthase</title><link>http://scien.net/enzyme/escherichia/cloning-and-expression-of-the-soybean-dapa-gene-encoding-dihydrodipicolinate-synthase</link> <comments>http://scien.net/enzyme/escherichia/cloning-and-expression-of-the-soybean-dapa-gene-encoding-dihydrodipicolinate-synthase#comments</comments> <pubDate>Wed, 15 May 2013 02:12:16 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Escherichia]]></category> <category><![CDATA[auxotroph]]></category> <category><![CDATA[dapa]]></category> <category><![CDATA[dihydrodipicolinate]]></category><guid
isPermaLink="false">http://scien.net/enzyme/escherichia/cloning-and-expression-of-the-soybean-dapa-gene-encoding-dihydrodipicolinate-synthase</guid> <description><![CDATA[Silk, Gw; Matthews, Bf; Somers, Da; Gengenbach, Bg, 1994: Cloning and expression of the soybean DapA gene encoding dihydrodipicolinate synthase. Plant molecular biology 26(3): 989-993 The rate-limiting step in the pathway for lysine synthesis in plants is catalyzed by the enzyme dihydrodipicolinate synthase (Ds). We have cloned the portion of the soybean (Glycine max cv. [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/escherichia/cloning-and-expression-of-the-soybean-dapa-gene-encoding-dihydrodipicolinate-synthase/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Cloning and characterization of a cDNA from Aspergillus parasiticus encoding an O-methyltransferase involved in aflatoxin biosynthesis</title><link>http://scien.net/enzyme/escherichia/cloning-and-characterization-of-a-cdna-from-aspergillus-parasiticus-encoding-an-o-methyltransferase-involved-in-aflatoxin-biosynthesis</link> <comments>http://scien.net/enzyme/escherichia/cloning-and-characterization-of-a-cdna-from-aspergillus-parasiticus-encoding-an-o-methyltransferase-involved-in-aflatoxin-biosynthesis#comments</comments> <pubDate>Wed, 15 May 2013 02:10:47 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Escherichia]]></category> <category><![CDATA[dihydrosterigmatocystin]]></category> <category><![CDATA[methylsterigmatocystin]]></category> <category><![CDATA[srrc]]></category> <category><![CDATA[sterigmatocystin]]></category><guid
isPermaLink="false">http://scien.net/enzyme/escherichia/cloning-and-characterization-of-a-cdna-from-aspergillus-parasiticus-encoding-an-o-methyltransferase-involved-in-aflatoxin-biosynthesis</guid> <description><![CDATA[Yu, J; Cary, Jw; Bhantnagar, D; Cleveland, Te; Keller, Np; Chu, Fs, 1993: Cloning and characterization of a cDNA from Aspergillus parasiticus encoding an O-methyltransferase involved in aflatoxin biosynthesis. Applied and environmental microbiology 59(11): 3564-3571 Aflatoxins are polyketide-derived secondary metabolites produced by the fungi Aspergillus flavus and Aspergillus parasiticus. Among the catalytic steps in the [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/escherichia/cloning-and-characterization-of-a-cdna-from-aspergillus-parasiticus-encoding-an-o-methyltransferase-involved-in-aflatoxin-biosynthesis/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Chloroplast-encoded protein as a subunit of acetyl-CoA carboxylase in pea plant</title><link>http://scien.net/enzyme/escherichia/chloroplast-encoded-protein-as-a-subunit-of-acetyl-coa-carboxylase-in-pea-plant</link> <comments>http://scien.net/enzyme/escherichia/chloroplast-encoded-protein-as-a-subunit-of-acetyl-coa-carboxylase-in-pea-plant#comments</comments> <pubDate>Wed, 15 May 2013 01:56:59 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Escherichia]]></category> <category><![CDATA[accd]]></category><guid
isPermaLink="false">http://scien.net/enzyme/escherichia/chloroplast-encoded-protein-as-a-subunit-of-acetyl-coa-carboxylase-in-pea-plant</guid> <description><![CDATA[Sasaki, Y; Hakamada, K; Suama, Y; Nagano, Y; Furusawa, I; Matsuno, R., 1993: Chloroplast-encoded protein as a subunit of acetyl-CoA carboxylase in pea plant. Journal of biological chemistry, 268(33): 25118-25123 The gene product of an open reading frame of the chloroplast genome, accD, that has sequence similarity with a subunit of acetyl-CoA carboxylase from Escherichia [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/escherichia/chloroplast-encoded-protein-as-a-subunit-of-acetyl-coa-carboxylase-in-pea-plant/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Characterization of the Candida albicans TRP1 gene and construction of a homozygous trp1 mutant by sequential co-transformation</title><link>http://scien.net/enzyme/escherichia/characterization-of-the-candida-albicans-trp1-gene-and-construction-of-a-homozygous-trp1-mutant-by-sequential-co-transformation</link> <comments>http://scien.net/enzyme/escherichia/characterization-of-the-candida-albicans-trp1-gene-and-construction-of-a-homozygous-trp1-mutant-by-sequential-co-transformation#comments</comments> <pubDate>Wed, 15 May 2013 01:35:45 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Escherichia]]></category> <category><![CDATA[auxotroph]]></category> <category><![CDATA[phosphoribosylanthrani]]></category> <category><![CDATA[prai]]></category> <category><![CDATA[trpc]]></category> <category><![CDATA[unifunctional]]></category><guid
isPermaLink="false">http://scien.net/enzyme/escherichia/characterization-of-the-candida-albicans-trp1-gene-and-construction-of-a-homozygous-trp1-mutant-by-sequential-co-transformation</guid> <description><![CDATA[Ostrander, Darin B.; Gorman, Jessica A., 1994: Characterization of the Candida albicans TRP1 gene and construction of a homozygous trp1 mutant by sequential co-transformation. Gene (amsterdam). 148(2): 179-185 The Candida albicans Trp1 gene has been isolated by complementation of an Escherichia coli trpC mutant. Sequence analysis has revealed a single Orf (open reading frame) of [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/escherichia/characterization-of-the-candida-albicans-trp1-gene-and-construction-of-a-homozygous-trp1-mutant-by-sequential-co-transformation/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Characterization of a Rickettsia rickettsii DNA fragment analogous to the firA-ORF17-lpxA region of Escherichia coli</title><link>http://scien.net/enzyme/escherichia/characterization-of-a-rickettsia-rickettsii-dna-fragment-analogous-to-the-fira-orf17-lpxa-region-of-escherichia-coli</link> <comments>http://scien.net/enzyme/escherichia/characterization-of-a-rickettsia-rickettsii-dna-fragment-analogous-to-the-fira-orf17-lpxa-region-of-escherichia-coli#comments</comments> <pubDate>Wed, 15 May 2013 01:21:25 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Escherichia]]></category> <category><![CDATA[fira]]></category> <category><![CDATA[lpxa]]></category> <category><![CDATA[rickettsii]]></category><guid
isPermaLink="false">http://scien.net/enzyme/escherichia/characterization-of-a-rickettsia-rickettsii-dna-fragment-analogous-to-the-fira-orf17-lpxa-region-of-escherichia-coli</guid> <description><![CDATA[Shaw, Edward I.; Wood, David O., 1994: Characterization of a Rickettsia rickettsii DNA fragment analogous to the firA-ORF17-lpxA region of Escherichia coli. Gene (amsterdam). 140(1): 109-113 The firA and lpxA genes, as well as an Orf coding for a putative 16-kDa protein of unknown function, have been identified and characterized in the obligate intracellular bacterium, [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/escherichia/characterization-of-a-rickettsia-rickettsii-dna-fragment-analogous-to-the-fira-orf17-lpxa-region-of-escherichia-coli/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Characterization of a Flavobacterium glutathione S-transferase gene involved in reductive dechlorination</title><link>http://scien.net/enzyme/escherichia/characterization-of-a-flavobacterium-glutathione-s-transferase-gene-involved-in-reductive-dechlorination</link> <comments>http://scien.net/enzyme/escherichia/characterization-of-a-flavobacterium-glutathione-s-transferase-gene-involved-in-reductive-dechlorination#comments</comments> <pubDate>Wed, 15 May 2013 01:21:07 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Escherichia]]></category> <category><![CDATA[dechlorinating]]></category> <category><![CDATA[dehalogenase]]></category> <category><![CDATA[dichlorohydroquinone]]></category> <category><![CDATA[formylmethionyl]]></category> <category><![CDATA[methylobacterium]]></category> <category><![CDATA[pcpc]]></category> <category><![CDATA[tetrachloro]]></category> <category><![CDATA[trichlorohydroquinone]]></category><guid
isPermaLink="false">http://scien.net/enzyme/escherichia/characterization-of-a-flavobacterium-glutathione-s-transferase-gene-involved-in-reductive-dechlorination</guid> <description><![CDATA[Orser, Cindy S.; Dutton, James; Lange, Cleston; Jablonski, Peter; Xun, Luying; Hargis, Mike, 1993: Characterization of a Flavobacterium glutathione S-transferase gene involved in reductive dechlorination. Journal Of Bacteriology. 175(9): 2640-2644 The gene pcpC, encoding tetrachloro&#8211; (TeCH) reductive dehalogenase, was cloned from Flavobacterium sp. strain Atcc 39723 and sequenced. The gene was identified by hybridization with [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/escherichia/characterization-of-a-flavobacterium-glutathione-s-transferase-gene-involved-in-reductive-dechlorination/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Characterization of Serpulina hyodysenteriae isolates of serotypes 8 and 9 from Quebec by restriction endonuclease fingerprinting and ribotyping</title><link>http://scien.net/enzyme/escherichia/characterization-of-serpulina-hyodysenteriae-isolates-of-serotypes-8-and-9-from-quebec-by-restriction-endonuclease-fingerprinting-and-ribotyping</link> <comments>http://scien.net/enzyme/escherichia/characterization-of-serpulina-hyodysenteriae-isolates-of-serotypes-8-and-9-from-quebec-by-restriction-endonuclease-fingerprinting-and-ribotyping#comments</comments> <pubDate>Wed, 15 May 2013 01:20:24 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Escherichia]]></category> <category><![CDATA[bglii]]></category> <category><![CDATA[hyodysenteriae]]></category> <category><![CDATA[ribotype]]></category> <category><![CDATA[ribotyping]]></category> <category><![CDATA[rrnb]]></category> <category><![CDATA[serpulina]]></category><guid
isPermaLink="false">http://scien.net/enzyme/escherichia/characterization-of-serpulina-hyodysenteriae-isolates-of-serotypes-8-and-9-from-quebec-by-restriction-endonuclease-fingerprinting-and-ribotyping</guid> <description><![CDATA[Harel, Josee; Belanger, Myriam; Forget, Celine; Jacques, Mario, 1994: Characterization of Serpulina hyodysenteriae isolates of serotypes 8 and 9 from Quebec by restriction endonuclease fingerprinting and ribotyping. Canadian Journal Of Veterinary Research. 58(4): 302-305 This study was undertaken to assess the discriminatory value of restriction endonuclease fingerprinting (Ref) analysis and ribotyping of 21 Serpulina hyodysenteriae [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/escherichia/characterization-of-serpulina-hyodysenteriae-isolates-of-serotypes-8-and-9-from-quebec-by-restriction-endonuclease-fingerprinting-and-ribotyping/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>CDNA cloning, overexpression in Escherichia coli, purification and characterization of sheep liver cytosolic serine hydroxymethyltransferase</title><link>http://scien.net/enzyme/escherichia/cdna-cloning-overexpression-in-escherichia-coli-purification-and-characterization-of-sheep-liver-cytosolic-serine-hydroxymethyltransferase</link> <comments>http://scien.net/enzyme/escherichia/cdna-cloning-overexpression-in-escherichia-coli-purification-and-characterization-of-sheep-liver-cytosolic-serine-hydroxymethyltransferase#comments</comments> <pubDate>Tue, 14 May 2013 02:30:26 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Escherichia]]></category> <category><![CDATA[aldimine]]></category> <category><![CDATA[hydroxymethyltransferas]]></category> <category><![CDATA[shmt]]></category> <category><![CDATA[tetrahydrofolate]]></category><guid
isPermaLink="false">http://scien.net/enzyme/escherichia/cdna-cloning-overexpression-in-escherichia-coli-purification-and-characterization-of-sheep-liver-cytosolic-serine-hydroxymethyltransferase</guid> <description><![CDATA[Jagath Reddy, Junutula; Ganesan, Kaliannan; Savithri, Handanahal S.; Datta, Asis; Rao, Naropantul Appaji, 1995: CDNA cloning, overexpression in Escherichia coli, purification and characterization of sheep liver cytosolic serine hydroxymethyltransferase. European Journal Of Biochemistry. 230(2): 533-537 A sheep liver cDNA clone for the cytosolic serine hydroxymethyltransferase (Shmt) was isolated and its nucleotide sequence determined. The full-length [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/escherichia/cdna-cloning-overexpression-in-escherichia-coli-purification-and-characterization-of-sheep-liver-cytosolic-serine-hydroxymethyltransferase/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Apramycin-resistant Escherichia coli isolated from pigs and a stockman</title><link>http://scien.net/enzyme/escherichia/apramycin-resistant-escherichia-coli-isolated-from-pigs-and-a-stockman</link> <comments>http://scien.net/enzyme/escherichia/apramycin-resistant-escherichia-coli-isolated-from-pigs-and-a-stockman#comments</comments> <pubDate>Tue, 14 May 2013 01:51:24 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Escherichia]]></category> <category><![CDATA[apramycin]]></category> <category><![CDATA[netilmicin]]></category> <category><![CDATA[preweaner]]></category> <category><![CDATA[serotypable]]></category> <category><![CDATA[stockman]]></category> <category><![CDATA[stockmans]]></category><guid
isPermaLink="false">http://scien.net/enzyme/escherichia/apramycin-resistant-escherichia-coli-isolated-from-pigs-and-a-stockman</guid> <description><![CDATA[Hunter, J. E. B.; Bennett, M.; Hart, C. A.; Shelley, J. C.; Walton, J. R., 1994: Apramycin-resistant Escherichia coli isolated from pigs and a stockman. Epidemiology &#038; Infection. 112(3): 473-480 Escherichia coli serotype O147:K89:K88a,c was found to be associated with outbreaks of diarrhoea in preweaner pigs of up to 4 weeks of age on a [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/escherichia/apramycin-resistant-escherichia-coli-isolated-from-pigs-and-a-stockman/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Analysis of Tox5 gene expression in Gibberella pulicaris strains with different trichothecene production phenotypes</title><link>http://scien.net/enzyme/escherichia/analysis-of-tox5-gene-expression-in-gibberella-pulicaris-strains-with-different-trichothecene-production-phenotypes</link> <comments>http://scien.net/enzyme/escherichia/analysis-of-tox5-gene-expression-in-gibberella-pulicaris-strains-with-different-trichothecene-production-phenotypes#comments</comments> <pubDate>Tue, 14 May 2013 01:36:05 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Escherichia]]></category> <category><![CDATA[cosegregation]]></category> <category><![CDATA[pulicaris]]></category> <category><![CDATA[trichodiene]]></category> <category><![CDATA[trichothecene]]></category> <category><![CDATA[trichothecenes]]></category><guid
isPermaLink="false">http://scien.net/enzyme/escherichia/analysis-of-tox5-gene-expression-in-gibberella-pulicaris-strains-with-different-trichothecene-production-phenotypes</guid> <description><![CDATA[Hohn, Tm; Desjardins, Ae; Mccormick, Sp, 1993: Analysis of Tox5 gene expression in Gibberella pulicaris strains with different trichothecene production phenotypes. Applied and environmental microbiology 59(8) The Tox5 gene encodes trichodiene synthase, the first unique enzyme in the trichothecene biosynthetic pathway. In Gibberella pulicaris R-6380, the level of Tox5 mRNA was found to increase 47-fold [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/escherichia/analysis-of-tox5-gene-expression-in-gibberella-pulicaris-strains-with-different-trichothecene-production-phenotypes/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>A glutathione S-transferase involved in vacuolar transfer encoded by the maize gene Bronze-2</title><link>http://scien.net/enzyme/escherichia/a-glutathione-s-transferase-involved-in-vacuolar-transfer-encoded-by-the-maize-gene-bronze-2</link> <comments>http://scien.net/enzyme/escherichia/a-glutathione-s-transferase-involved-in-vacuolar-transfer-encoded-by-the-maize-gene-bronze-2#comments</comments> <pubDate>Mon, 13 May 2013 02:32:55 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Escherichia]]></category> <category><![CDATA[glutathionation]]></category> <category><![CDATA[sequesters]]></category><guid
isPermaLink="false">http://scien.net/enzyme/escherichia/a-glutathione-s-transferase-involved-in-vacuolar-transfer-encoded-by-the-maize-gene-bronze-2</guid> <description><![CDATA[Marrs, Kathleen A.; Alfenito, Mark R.; Lloyd, Alan M.; Walbot, Virginia, 1995: A glutathione S-transferase involved in vacuolar transfer encoded by the maize gene Bronze-2. Nature (london). 375(6530): 397-400 Glutathione S-transferases (GSTs) are enzymes that detoxify heterocyclic compounds (xenobiotics) by covalently linking glutathione to the substrate, forming a glutathione S conjugate. A glutathione pump in [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/escherichia/a-glutathione-s-transferase-involved-in-vacuolar-transfer-encoded-by-the-maize-gene-bronze-2/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>A conditional negative selection for Arabidopsis expressing a bacterial cytosine deaminase gene</title><link>http://scien.net/enzyme/escherichia/a-conditional-negative-selection-for-arabidopsis-expressing-a-bacterial-cytosine-deaminase-gene</link> <comments>http://scien.net/enzyme/escherichia/a-conditional-negative-selection-for-arabidopsis-expressing-a-bacterial-cytosine-deaminase-gene#comments</comments> <pubDate>Mon, 13 May 2013 02:28:24 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Escherichia]]></category> <category><![CDATA[bialaphos]]></category> <category><![CDATA[nopaline]]></category> <category><![CDATA[pnos]]></category><guid
isPermaLink="false">http://scien.net/enzyme/escherichia/a-conditional-negative-selection-for-arabidopsis-expressing-a-bacterial-cytosine-deaminase-gene</guid> <description><![CDATA[Kobayashi, Tetsuto; Hisajima, Shigeru; Stougaard, Jens; Ichikawa, Hiroaki, 1995: A conditional negative selection for Arabidopsis expressing a bacterial cytosine deaminase gene. Japanese Journal Of Genetics. 70(3): 409-422 The enzyme activity for cytosine deaminase, which converts cytosine to uracil in bacteria, is usually undetected in higher plants and animals. The enzyme also catalyzes conversion of non-toxic [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/escherichia/a-conditional-negative-selection-for-arabidopsis-expressing-a-bacterial-cytosine-deaminase-gene/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Visualization and ablation of phenylethanolamine N-methyltransferase producing cells in transgenic mice</title><link>http://scien.net/enzyme/escherichia/visualization-and-ablation-of-phenylethanolamine-n-methyltransferase-producing-cells-in-transgenic-mice</link> <comments>http://scien.net/enzyme/escherichia/visualization-and-ablation-of-phenylethanolamine-n-methyltransferase-producing-cells-in-transgenic-mice#comments</comments> <pubDate>Mon, 13 May 2013 02:06:29 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Escherichia]]></category> <category><![CDATA[hpnmt]]></category> <category><![CDATA[myelencephalon]]></category> <category><![CDATA[phenylethanolamine]]></category> <category><![CDATA[pnmt]]></category><guid
isPermaLink="false">http://scien.net/enzyme/escherichia/visualization-and-ablation-of-phenylethanolamine-n-methyltransferase-producing-cells-in-transgenic-mice</guid> <description><![CDATA[Quaife, Carol J.; Hoyle, Gary W.; Froelick, Glenda J.; Findley, Seth D.; Baetge, E. Edward; Behringer, Richard R.; Hammang, Joseph P.; Brinster, Ralph L.; Palmiter, Richard D., 1994: Visualization and ablation of phenylethanolamine N-methyltransferase producing cells in transgenic mice. Transgenic Research. 3(6): 388-400 We cloned and sequenced the mouse phenylethanolamine N-methyltransferase (Pnmt) gene which encodes [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/escherichia/visualization-and-ablation-of-phenylethanolamine-n-methyltransferase-producing-cells-in-transgenic-mice/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Two genes for carbohydrate catabolism are divergently transcribed from a region of DNA containing the hexC locus in Pseudomonas aeruginosa PAO1</title><link>http://scien.net/enzyme/escherichia/two-genes-for-carbohydrate-catabolism-are-divergently-transcribed-from-a-region-of-dna-containing-the-hexc-locus-in-pseudomonas-aeruginosa-pao1</link> <comments>http://scien.net/enzyme/escherichia/two-genes-for-carbohydrate-catabolism-are-divergently-transcribed-from-a-region-of-dna-containing-the-hexc-locus-in-pseudomonas-aeruginosa-pao1#comments</comments> <pubDate>Mon, 13 May 2013 01:37:58 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Escherichia]]></category> <category><![CDATA[hexc]]></category> <category><![CDATA[mobilis]]></category> <category><![CDATA[ninefold]]></category> <category><![CDATA[polydeoxyadenosine]]></category> <category><![CDATA[zymomonas]]></category><guid
isPermaLink="false">http://scien.net/enzyme/escherichia/two-genes-for-carbohydrate-catabolism-are-divergently-transcribed-from-a-region-of-dna-containing-the-hexc-locus-in-pseudomonas-aeruginosa-pao1</guid> <description><![CDATA[&#8220;Temple, Louise; Sage, Andrew; Christie, Gail E.; Phibbs, Paul V.Jr, 1994: Two genes for carbohydrate catabolism are divergently transcribed from a region of DNA containing the hexC locus in Pseudomonas aeruginosa PAO1. Journal Of Bacteriology. 176(15): 4700-4709 The hexC locus of Pseudomonas aeruginosa Pao1 was localized to a 247-bp segment of chromosomal Dna on the [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/escherichia/two-genes-for-carbohydrate-catabolism-are-divergently-transcribed-from-a-region-of-dna-containing-the-hexc-locus-in-pseudomonas-aeruginosa-pao1/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Transfer of genes from Pseudomonas saccharophila to construct xylose-utilizing strains of Alcaligenes eutrophus</title><link>http://scien.net/enzyme/escherichia/transfer-of-genes-from-pseudomonas-saccharophila-to-construct-xylose-utilizing-strains-of-alcaligenes-eutrophus</link> <comments>http://scien.net/enzyme/escherichia/transfer-of-genes-from-pseudomonas-saccharophila-to-construct-xylose-utilizing-strains-of-alcaligenes-eutrophus#comments</comments> <pubDate>Mon, 13 May 2013 01:15:44 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Escherichia]]></category> <category><![CDATA[doudoroff]]></category> <category><![CDATA[entner]]></category> <category><![CDATA[eutrophus]]></category> <category><![CDATA[saccharophila]]></category> <category><![CDATA[transconjugant]]></category> <category><![CDATA[transconjugants]]></category> <category><![CDATA[xylulokinase]]></category><guid
isPermaLink="false">http://scien.net/enzyme/escherichia/transfer-of-genes-from-pseudomonas-saccharophila-to-construct-xylose-utilizing-strains-of-alcaligenes-eutrophus</guid> <description><![CDATA[Buccholz, Baerbel; Nordsiek, Gabriele; Meister, Martina; Bowien, Botho, 1994: Transfer of genes from Pseudomonas saccharophila to construct xylose-utilizing strains of Alcaligenes eutrophus. Current Microbiology. 29(3): 157-162 About 1500 hybrid broad-host-range plasmids from a genomic library of Pseudomonas saccharophila were individually transferred by conjugation from Escherichia coli to Alcaligenes eutrophus. Direct selection for pentose-utilizing transconjugants yielded [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/escherichia/transfer-of-genes-from-pseudomonas-saccharophila-to-construct-xylose-utilizing-strains-of-alcaligenes-eutrophus/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> </channel> </rss>