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.
Berger, S.; Ellersiek, U.; Westhoff, P.; Steinmuller, K., 1993: Studies on the expression of NDH-H, a subunit of the NAD(P)H-plastoquinone-oxidoreductase of higher-plant chloroplasts. Planta 190(1): 25-31 The plastid genomes of higher plants contain eleven reading frames (ndhA-K) that are homologous to genes encoding subunits of the mitochondrial Nadh-ubiquinone-oxidoreductase (complex I). The carboxy-terminal end of the [...]
Chapman, K. A.; Delauney, A. J.; Kim, J. H.; Verma, D. P. S., 1994: Structural organization of de novo purine biosynthesis enzymes in plants: 5-aminoimidazole ribonucleotide carboxylase and 5-aminoimidazole-4-N-succinocarboxamide ribonucleotide synthetase cDNAs from Vigna aconitifolia. Plant Molecular Biology 24(2): 389-395 Nodules of tropical legumes generally export symbiotically fixed nitrogen in the form of ureides that [...]
Issakidis, E; Miginiac-Maslow, M; Decottignies, P; Jacquot, Jp; Cretin, C; Gadal, P., 1992: Site-directed mutagenesis reveals the involvement of an additional thioredoxin-dependent regulatory site in the activation of recombinant sorghum leaf NADP-malate dehydrogenase. Journal of biological chemistry, 267(30): 21577-21583 The chloroplastic enzyme Nadp-malate dehydrogenase is activated by a reversible thiol/disulfide interchange with reduced thioredoxin. Its [...]
Ward, Lawrence J. H.; Beresford, Tom P. J.; Lubbers, Mark W.; Jarvis, Brion D. W.; Jarvis, Audrey W., 1993: Sequence analysis of the lysin gene region of the prolate lactococcal bacteriophage c2. Canadian Journal Of Microbiology. 39(8): 767-774 Approximately 80% of the genome of the prolate-headed lactococcal bacteriophage c2 was cloned into shuttle vectors pSA3 [...]
Lai, C. Y.; Baumann, P., 1992: Sequence analysis of a DNA fragment from Buchnera aphidicola (an endosymbiont of aphids) containing genes homologous to dnaG, rpoD, cysE, and secB. Gene 119(1): 113-118 The aphid, Schizaphis graminum, contains a prokaryotic, obligately intracellular endosymbiont, Buchnera aphidicola, which is necessary for the survival of the host. A recent study [...]
Liu, Shie Chau; Ogretmen, Besim; Chuang, Yao Yu; Stark, Benjamin C., 1992: Selection and characterization of alpha-amylase-overproducing recombinant Escherichia coli containing the bacterial hemoglobin gene. Applied Microbiology & Biotechnology. 38(2): 239-242 We previously reported that the presence of the bacterial (Vitreoscilla) hemoglobin gene enhances alpha-amylase production in recombinant Escherichia coli strain Mk7 Using the growth [...]
Romaniec, M. P. M.; Huskisson, N.; Barker, P.; Demain, A. L., 1993: Purification and properties of the Clostridium thermocellum bglB gene product expressed in Escherichia coli. Enzyme & Microbial Technology. 15(5): 393-400 The Clostridium thermocellum beta-glucosidase B was purified to homogeneity in its recombinant form from Escherichia coli. The purification protocol included ion exchange, hydrophobic [...]
Berry-Lowe, Sl; Grimm, B; Smith, Ma; Gamini-Kannangara, C., 1992: Purification and characterization of glutamate 1-semialdehyde aminotransferase from barley expressed in Escherichia coli. Plant physiology 99(4): 1597-1603 The immediate precursor in the synthesis of tetrapyrroles is delta-aminolevulinate (Ala). Ala is synthesized from glutamate in higher plants, algae, and certain bacteria. Glutamate 1-semialdehyde aminotransferase (Ec 22.214.171.124) (Gsa-At), [...]
Rodriguez-Palenzuela, P; Burr, Tj; Collmer, A., 1991: Polygalacturonase is a virulence factor in Agrobacterium tumefaciens biovar 3. Journal of bacteriology 173(20): 6547-6552 Agrobacterium tumefaciens biovar 3 causes both crown gall and root decay of grapes. All biovar 3 strains, regardless of their tumorigenicity, produce in culture a single polygalacturonase with a pI around 4. A. [...]