Escherichia is a rod-shaped genus of bacteria from the family Enterobacteriaceae. This genus of bacteria is Gram-negative, does not form spores, and is facultatively anaerobic, which means that this bacteria makes adenosine triphosphate (ATP) by aerobic respiration if oxygen is present in the environment, but can also switch to fermentation. Escherichia is commonly founding the gastrointestinal tracts of warm-blooded animals, and these species of bacteria typically provide a portion of vitamin K (microbially derived) to their host. A good number of Escherichia species are pathogenic, which means that it can cause disease to its host. The genus Escherichia is named after Theodor Escherich, a German-Austriant pediatrician and professor who discovered the Escherichia coli or E. coli.
There are many enzymes found in the Escherichia genus, including the pyruvate formate lyase (PFL), which helps regulate anaerobic glucose metabolism—a process that is important in a facultatively anaerobic organism. Pyruvate formate lyase uses radical non-redox chemistry in order to catalyze the reversible conversion of pyruvate and coenzyme-A (CoA) into acetyl coenzyme-A and formate. Restriction endonuclease is an enzyme involved with restriction modification system and naturally found in Escherichia coli. This enzyme contains 402 amino acids, which gve the substance a molecular mass of 45.2 kDa.
Fumarate hydratase is an enzyme that catalyzes the reversible hydration of fumarate to L-malate, and this enzyme is typically found in Escherichia coli fumC, because of its thermolabile dimeric nature. The glycoside hydrolase family 2 is a group of enzymes have a conserved glutamic acid residue, which is often found in Escherichia coli lacZ. These enzymes hydrolyse the glycosidic bond between two or more carbohydrate molecules, as well as between a carbohydrate molecule and a non-carbohydrate molecule.
This category contains scientific information on Escherichia, a genus of bacteria that contains a wide variety of enzymes.
Moews, P. C.; Knox, J. R., 1979: Predicted secondary structures of 4 penicillin beta lactamases ec 184.108.40.206 and a comparison with 2 lysozymes. International Journal of Peptide and Protein Research 13(4): 385-393 The secondary structures of 4.beta.-lactamases (Bacillus cereus, B. licheniformis, Staphylococcus aureus and Escherichia coli R-Tem) were predicted by the statistical method of Chou [...]
Szeberenyi, J.; Roy, M. K.; Apirion, D., 1983: Precursor nucleotides at the 5 end are not required for processing by rnase e at the 3 end of 5s ribosomal rna. European Journal of Biochemistry 136(2): 321-326 7-S Rna, a single-site substrate for the processing enzyme RNase E of Escherichia coli, consists of p5 rRNA (the [...]
Shakulov R.S., 1986: Precise mapping of the gpp gene involved in guanosine tetraphosphate synthesis and deletion of the ilvc gpp region of escherichia coli chromosome. Genetika: 2775-2783 Using the set of transducing.lambda. phages the gpp gene, responsible for pppGpp to ppGpp conversion, was localized between rep and trxA genes on 85 min of the Escherichia [...]
Kilburn D.G., 1988: Precise excision of the cellulose binding domains from two cellulomonas fimi cellulases by a homologous protease and the effect of catalysis. Journal Of Biological Chemistry1: 10401-10407 An endo-.beta.-1,4-glucanase (Cen A) and an exo-.beta.-1,4-glucanase (Cex) were prepared from Escherichia coli expressing recombinant Dna of the cellulolytic bacterium Cellulomas fimi. Purification was facilitated by [...]
Kotze J.M., 1987: Potential applications of random dna probes and restriction fragment length polymorphisms in the taxonomy of the fusaria. Phytopathology: 669-672 A range of Fusarium species was screened for Dna restriction fragment length polymorphisms in ethidium-stained agarose gels and by hybridization to random probes generated from total Dna of an isolate of Fusarium oxysporum [...]
Knappe, J.; Neugebauer, F. A.; Blaschkowski, H. P.; Gaenzler, M., 1984: Post translational activation introduces a free radical into pyruvate formate lyase ec 220.127.116.11. Proceedings of the National Academy of Sciences of the United States of America 81(5): 1332-1335 Pyruvate formate-lyase (formate acetyltransferase: Ec 18.104.22.168) of Escherichia coli cells is post-tanslationally interconverted between inactive and [...]
“Paulson J.C., 1988: Post golgi apparatus localization and regional expression of rat intestinal sialyltransferase detected by immunoelectron microscopy with polypeptide epitope purified antibody. Journal Of Biological Chemistry3: 6302-6309 During studies on the Golgi apparatus immunolocalization of.beta.-galactoside.alpha.2,6-sialyltransferase in intestinal cells, immunostaining of a number of post-Golgi apparatus structures including mucus droplets and plasma membrane were observed. [...]
Bridger W.A., 1987: Positional oxygen isotope exchange as a probe for the mechanism of catalysis by escherichia coli succinyl coenzyme a synthetase. Biochemistry: 4483-4487 Succinyl-CoA synthetase of Escherichia coli has an.alpha.2.beta.2 subunit structure. The enzyme shows strict half-sites reactivity with respect to the phosphorylation of a histidine residue in the.alpha. subunit that represents a step [...]
Villafranca J.J., 1985: Positional isotope exchange and kinetic experiments with escherichia coli gmp synthetase. Biochemistry: 5343-5350 The kinetic mechanism of Escherichia coli guanosine-5′-monophosphate synthetase has been determined by utilizing initial velocity kinetic patterns and positional isotope exchange experiments. The initial velocity patterns of MgATP, Xmp, and either Nh3 or glutamine (as nitrogen source) were consistent [...]