BIOMAT Database Logo BIOMAT Database Logo

Glutamine-dependent carbamyl-phosphate synthetase (Escherichia coli); preparation of subunits. 1978

P P Trotta, and M E Burt, and L M Pinkus, and L F Estis, and R H Haschemeyer, and A Meister

UI MeSH Term Description Entries
D008970 Molecular Weight The sum of the weight of all the atoms in a molecule. Molecular Weights,Weight, Molecular,Weights, Molecular
D010770 Phosphotransferases A rather large group of enzymes comprising not only those transferring phosphate but also diphosphate, nucleotidyl residues, and others. These have also been subdivided according to the acceptor group. (From Enzyme Nomenclature, 1992) EC 2.7. Kinases,Phosphotransferase,Phosphotransferases, ATP,Transphosphorylase,Transphosphorylases,Kinase,ATP Phosphotransferases
D002223 Carbamoyl-Phosphate Synthase (Glutamine-Hydrolyzing) An enzyme that catalyzes the formation of carbamoyl phosphate from ATP, carbon dioxide, and glutamine. This enzyme is important in the de novo biosynthesis of pyrimidines. EC 6.3.5.5. Carbamyl Phosphate Synthase (Glutamine),Carbamoyl-Phosphate Synthase (Glutamine),Carbamoylphosphate Synthetase II,Carbamyl Phosphate Synthase II,Carbamyl-Phosphate Synthase (Glutamine),Synthetase II, Carbamoylphosphate
D004926 Escherichia coli A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc. Alkalescens-Dispar Group,Bacillus coli,Bacterium coli,Bacterium coli commune,Diffusely Adherent Escherichia coli,E coli,EAggEC,Enteroaggregative Escherichia coli,Enterococcus coli,Diffusely Adherent E. coli,Enteroaggregative E. coli,Enteroinvasive E. coli,Enteroinvasive Escherichia coli
D000494 Allosteric Regulation The modification of the reactivity of ENZYMES by the binding of effectors to sites (ALLOSTERIC SITES) on the enzymes other than the substrate BINDING SITES. Regulation, Allosteric,Allosteric Regulations,Regulations, Allosteric
D046911 Macromolecular Substances Compounds and molecular complexes that consist of very large numbers of atoms and are generally over 500 kDa in size. In biological systems macromolecular substances usually can be visualized using ELECTRON MICROSCOPY and are distinguished from ORGANELLES by the lack of a membrane structure. Macromolecular Complexes,Macromolecular Compounds,Macromolecular Compounds and Complexes,Complexes, Macromolecular,Compounds, Macromolecular,Substances, Macromolecular

Related Publications

P P Trotta, and M E Burt, and L M Pinkus, and L F Estis, and R H Haschemeyer, and A Meister
Carbamyl phosphate synthetase (glutamine-utilizing) from Escherichia coli.
January 1985, Methods in enzymology,
P P Trotta, and M E Burt, and L M Pinkus, and L F Estis, and R H Haschemeyer, and A Meister
Catalytic domains of carbamyl phosphate synthetase. Glutamine-hydrolyzing site of Escherichia coli carbamyl phosphate synthetase.
August 1986, The Journal of biological chemistry,
P P Trotta, and M E Burt, and L M Pinkus, and L F Estis, and R H Haschemeyer, and A Meister
Interaction of Escherichia coli carbamyl phosphate synthetase with glutamine.
May 1973, Biochemistry,
P P Trotta, and M E Burt, and L M Pinkus, and L F Estis, and R H Haschemeyer, and A Meister
Mechanism and regulation of the glutamine-dependent carbamyl phosphate synthetase of Escherichia coli.
January 1989, Advances in enzymology and related areas of molecular biology,
P P Trotta, and M E Burt, and L M Pinkus, and L F Estis, and R H Haschemeyer, and A Meister
Glutamine-dependent carbamyl phosphate synthetase: catalysis and regulation.
January 1977, Advances in enzyme regulation,
P P Trotta, and M E Burt, and L M Pinkus, and L F Estis, and R H Haschemeyer, and A Meister
Activation by fusion of the glutaminase and synthetase subunits of Escherichia coli carbamyl-phosphate synthetase.
August 1997, The Journal of biological chemistry,
P P Trotta, and M E Burt, and L M Pinkus, and L F Estis, and R H Haschemeyer, and A Meister
Yeast carbamyl phosphate synthetase. Structure of the yeast gene and homology to Escherichia coli carbamyl phosphate synthetase.
December 1983, The Journal of biological chemistry,
P P Trotta, and M E Burt, and L M Pinkus, and L F Estis, and R H Haschemeyer, and A Meister
Evidence for the presence of two nonidentical subunits in carbamyl phosphate synthetase of Escherichia coli.
March 1972, Biochemistry,
P P Trotta, and M E Burt, and L M Pinkus, and L F Estis, and R H Haschemeyer, and A Meister
Regulation and mutation affecting a glutamine dependent formation of carbamyl phosphate in Escherichia coli.
February 1964, Biochemical and biophysical research communications,
P P Trotta, and M E Burt, and L M Pinkus, and L F Estis, and R H Haschemeyer, and A Meister
Carbamyl phosphate synthetase III, an evolutionary intermediate in the transition between glutamine-dependent and ammonia-dependent carbamyl phosphate synthetases.
October 1994, Journal of molecular biology,
Copied contents to your clipboard!