1.
Clin Chim Acta
; 68(1): 11-5, 1976 Apr 01.
Artigo
em Inglês
| MEDLINE
| ID: mdl-1261049
RESUMO
A defective pyruvate kinase (EC 2.7.1.40) is described. The abnormal PK is characterized by a shift in the R in equilibrium T equilibrium to the T-state. The Ko.5 for the substrate phosphoenol pyruvate is about 6 times higher than for the normal enzyme, while the KM value for the positive effector Fru-1, 6-P2 is increased. In agreement with a shift to the T-state is the increased affinity of the abnormal enzyme for the negative effectors ATP and alanine. The results are discussed in relation to other abnormal pyruvate kinases.