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.
Klibanov A.M., 1985: Preparative resolution of d l threonine catalyzed by immobilized phosphatase. Biotechnology & Bioengineering: 247-252 Hydrolysis of L- and D-O-phosphothreonines catalyzed by 4 different phosphatases, alkaline phosphatases from calf intestine and Escherichia coli and acid phosphatases from wheat germ and potato, was kinetically studied. Alkaline phosphatases have comparable reactivities towards the optical isomers. [...]
Dzantiev B.B., 1986: Preparation of insulin conjugate with escherichia coli beta galactosidase for enzyme immunoassay. Bioorganicheskaya Khimiya: 327-331 A modified procedure has been worked out for preparing a conjugate of porcine insulin with Escherichia coli.beta.-galactoside employing a heterobifunctional reagent, N-hydroxysuccinimidyl m-maleimidobenzoate. Optimal conditions for insulin acylation and subseqent coupling with.beta.-galactosidase were selected that afforded the [...]
Amarakone, S. P.; Kawashima, K.; Hayashi, T., 1983: Preparation of immobilized enzymes by radio polymerization preparation of beta galactosidase and its utilization for the continuous determination of lactose. Report of National Food Research Institute (42): 87-96 Beta.-Galactosidase of Escherichia coli origin was immobilized in the form of beads by the radiopolymerization of different combinations of [...]
Mosbach K., 1985: Preparation of a soluble bifunctional enzyme by gene fusion. Bio Technology (new York): 821-823 Within the cellular framework are a number of sequentially operating enzyme systems, in many cases in the form of bi- or even multifunctional proteins each consisting of a single type of polypeptide chain but having two or more [...]
Yang G Y., 1983: Preparation immobilization and properties of penicillin acylase from escherichia coli. Proceedings Of The National Science Council Re Ic Of China Part A Applied Sciences: 20-26 Penicillin acylase (Pa) was induced and extracted from E. coli Gsm6, cultivated in phenyl acetate and yeast extract and purified by fractionation with streptomycin sulfate, ammonium [...]
Margolin, A. L.; Izumrudov, V. A.; Svedas, V. K.; Zezin, A. B.; Kabanov, V. A.; Berezin, I. V., 1981: Preparation and properties of penicillin amidase ec 126.96.36.199 immobilized in poly electrolyte complexes. Biochimica et Biophysica Acta 660(2): 359-365 Immobilization of penicillin amidase (acylamide amidohydrolase, Ec 188.8.131.52) from Escherichia coli was carried out on negatively charged [...]
Jensen, H. B.; Miron, T., 1980: Preparation and properties of insoluble forms of bacterio phage t 4 lysozyme ec 184.108.40.206 and chicken egg white lysozyme. Journal of Solid Phase Biochemistry 5(1): 45-60 Bacteriophage T4 lysozyme and chicken egg white lysozyme were covalently bound to CNBr activated Sepharose and to glutaraldehyde activated polyacrylhydrazido-Sepharose. The latter method [...]
Dalgaard L., 1983: Preparation and hydrolysis of n glucuronides of pyridine and piperidine. Acta Chemica Scandinavica Series B Organic Chemistry & Biochemistry: 923-928 N-Glucuronides of pyridine and 3-methylpyridine were prepared and the chemical and enzymatic cleavage by base of.beta.-glucuronidase was studied, respectively. A Km value of 0.08 M was found using Escherichia coli or Helix [...]
Bejar, R.; Curbelo, V.; Davis, C.; Gluck, L., 1981: Premature labor bacterial sources of phospho lipase. Obstetrics and Gynecology 57(4): 479-482 Human term labor is thought to be initiated by amniotic and chorionic phospholipase A2, an enzyme that liberates arachidonic acid esters from the phospholipids of these membranes, leading to the synthesis of prostaglandins by [...]
Moews, P. C.; Knox, J. R., 1979: Predicted secondary structures of 4 penicillin beta lactamases ec 220.127.116.11 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 [...]