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8168646 
Journal Article 
Properties and mechanism of human erythrocyte phosphoglycerate kinase 
Soong Lee, C; O'Sullivan, WJ 
1975 
Yes 
Journal of Biological Chemistry
ISSN: 0021-9258
EISSN: 1083-351X 
250 
4 
1275-1281 
English 
Detailed kinetic studies, including initial velocity, product inhibition, and substrate analog inhibition measurements, have been carried out on the reverse reaction catalyzed by human erythrocyte phosphoglycerate kinase with MgATP2- as the phosphoryl group donor. The results are consistent with the reaction conforming to a rapid equilibrium random mechanism. Substantially similar results were obtained for other activating metal ions (manganese, calcium, and cobalt) and other nucleoside triphosphates (ATP, GTP). An ADP ATP exchange reaction was invariably associated with the purified enzyme but definitive evidence that it was an intrinsic property of the enzyme was not obtained.