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.
Ferone R., 1985: Folylpoly gamma glutamate synthetase dihydrofolate synthetase cloning and high expression of the escherichia coli fol c gene and purification and properties of the gene product. Journal Of Biological Chemistry: 5625-5630 The E. coli gene for folylpolyglutamate synthetase-dihydrofolate synthetase was localized to plasmids pLC22-45, 24-31 and 28-44 of the Clarke-Carbon E. coli colony [...]
Chock P.B., 1981: Fluorometric studies of aza epsilon adenylylated glutamine synthetase from escherichia coli. Journal Of Biological Chemistry2: 6010-6016 Glutamine synthetase in E. coli is regulated by adenylylation and deadenylylation reactions. The adenylylation reaction converts the divalent cation requirement of the enzyme from Mg2+ to Mn2+. Previously, the catalytic action of unadenylylated glutamine synthetase was [...]
Watkins W.D., 1987: Fluorometric method for enumeration of escherichia coli in molluscan shellfish. Journal Of Food Protection: 685-690 A novel procedure for enumerating Escherichia coli in molluscan shellfish has been developed and evaluated. The method, a singular modification of the Apha most probable number (Mpn) procedure, incorporates a fluorogenic molecule, 4-methylumbelliferyl-.beta.-D-glucuronide (Mug), into the confirmed [...]
“Schachman H.K., 1985: Fluorine 19 nmr studies of communication between catalytic and regulatory subunits in aspartate transcarbamoylase. Journal Of Biological Chemistry1: 11659-11662 19f nuclear magnetic resonance (Nmr) spectroscopy was used to study “”communication”” between the catayltic and regulatory subunits in aspartate transcarbamoylase of Escherichia coli. Hybrid enzymes composed of fluorotyrosine-labeled regulatory subunits and native catalytic [...]
Schachman H.K., 1985: Fluorine 19 nmr studies of fluorotyrosine labeled aspartate transcarbamoylase properties of the enzyme and its catalytic and regulatory subunits. Journal Of Biological Chemistry1: 11651-11658 Aspartate transcarbamoylase labeled with 3-fluorotyrosine was purified from an Escherichia coli strain which was auxotrophic for tyrosine and overproduced aspartate transcarbamoylase upon uracil starvation. The labeled enzyme in [...]
Hammes G.G., 1979: Fluorescence studies of the pyruvate dehydrogenase multi enzyme complex from escherichia coli. Biochemistry: 1229 Reduced lipoic acids on the pyruvate dehydrogenase multienzyme complex from E. coli were preferentially labeled using the differential reactivity of lipoic acids in different environments. The lipoic acids were labeled with N-ethylmaleimide, N-(3-pyrene)maleimide (MalPy) and N-maleimide (Ddpm). As [...]
Hammes G.G., 1982: Fluorescence polarization study of the alpha keto glutarate dehydrogenase complex from escherichia coli. Biochemistry: 6489-6496 The lipoic acids of the.alpha.-ketoglutarate dehydrogenase multienzyme complex from E. coli were modified with 2 fluorescent probes, N-(1-pyrenyl)-maleimide and 5-ethyl]amino]-naphthylene-1-sulfonic acid. Time-resolved fluorescence polarization of partially labeled complexes (18-77% inhibition of enzyme activity) reveals a complex depolarization [...]
Souzu, H., 1986: Fluorescence polarization studies on escherichia coli membrane stability and its relation to the resistance of the cell to freeze thawing i. membrane stability in cells of differing growth phase. Biochimica et Biophysica Acta 861(2): 353-360 Physical properties of Escherichia coli membrane lipids in logarithmic- and stationary-phase cells were studied by measuring the [...]
Tokushige, M.; Iinuma, K.; Yamamoto, M.; Nishijima, Y., 1980: Fluorescence energy transfer in tryptophanase ec 22.214.171.124. Biochemical and Biophysical Research Communications 96(2): 863-869 Excitation of apotryptophanase from Escherichia coli B/lt7-A at 290 nm yielded a fluorescence emission centered at 340 nm. Binding of pyridoxal phosphate to apoenzyme induced quenching of protein fluorescence concomitant with an [...]
Saier M.H.Jr, 1980: Fine control of adenylate cyclase by the phosphoenol pyruvate and sugar phospho transferase systems in escherichia coli and salmonella typhimurium. Journal Of Bacteriology: 603-610 Inhibition of cellular adenylate cyclase activity by sugar substrates of the phosphoenolpyruvate-dependent phosphotransferase system was reliant on the activities of the protein components of this enzyme system and [...]