Substrate Specificity of CTP Synthetase from Escherichia coli

Mn2+ and substrate interactions with glutamine synthetase from Escherichia coli.

Substrate specificity of the pyruvate dehydrogenase complex from Escherichia coli.

The investigation of the substrate specificity of the pyruvate dehydrogenase complex from Escherichia coli allows a description of the binding region of pyruvate. Substrate analogs with electronegative substitutions in the methyl group show a strong competitive inhibition of the overall reaction of the pyruvate dehydrogenase complex. The most efficient inhibitor is fluoropyruvate which has a mo...

Substrate specificity of a glucose permease of Escherichia coli.

Rogers, Dexter (Utah State University, Logan) and Shon-hua Yu. Substrate specificity of a glucose permease of Escherichia coli. J. Bacteriol. 84:877-881. 1962.-A study was made of d-galactose uptake by galactose-negative Escherichia coli strain A (Weigle). Uptake probably occurred through a glucose-permease system, because d-glucose and a variety of nonmetabolizable glucose derivatives inhibite...

Inhibition of Escherichia coli CTP Synthetase by NADH and Other Nicotinamides and Their Mutual Interactions with CTP and GTP.

CTP synthetases catalyze the last step of pyrimidine biosynthesis and provide the sole de novo source of cytosine-containing nucleotides. As a central regulatory hub, they are regulated by ribonucleotide and enzyme concentration through ATP and UTP substrate availability, CTP product inhibition, GTP allosteric modification, and quaternary structural changes including the formation of CTP-inhibi...

Substrate Specificity and Induction of Thymidine Phosphorylase in Escherichia Coli.

Purified preparations from Escherichia coli of the enzyme thymidine :orthophosphate deoxyribosyltransferase (EC 2.4. 2.4) or thymidine phosphorylase are specific for deoxyribose lphosphate. A number of pyrimidine bases function in the reaction, however, including uracil, 5-bromoand 5-aminouracil, 2-thiothymine, and 2-thiouracil, whereas deoxycytidine is inert (1). The level of enzyme in extract...