Role of nicotinamide adenine dinucleotide as an effector in formation and reactions of acylglyceraldehyde-3-phosphate dehydrogenase.
Role of nicotinamide adenine dinucleotide as an effector in formation and reactions of acylglyceraldehyde-3-phosphate dehydrogenase.
复制标题
烟酰胺腺嘌呤二核苷酸作为效应物在酰基甘油醛-3-磷酸脱氢酶的形成和反应中的作用。
DOI:
10.1021/bi00522a028
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发表时间:
1981
期刊:
影响因子:
2.9
通讯作者:
Bernhard,SA
中科院分区:
文献类型:
--
作者:
Malhotra,OP;Bernhard,SA
O. P. Malhotra* and Sidney A. Bernhard* abstract: The equilibrium spectral and reactivity properties of a chromophoric acylglyceraldehyde-3-phosphate dehydrogenase (FA-GPDH) have been previously reported. Transient studies of these properties are reported herein. As with true 3-phosphoglyceroyl-enzyme these properties depend on the presence of bound coenzyme (NAD+). The reactivity of the acyl-enzyme toward acceptors (phosphate and arsenate) parallels the extent of its NAD+-induced spectral change [Malhotra, O. P., & Bernhard, S. A.(1973) Proc. Natl. Acad. Sci USA 70, 2077-2081]. The transcient deacylation of FA-GPDH, preincubated with NAD" 1", is kinetically biphasic. The relative amplitudes of the fast vs. the slowphase depend on NAD" 1" concentration but are independent of the nature and concentration of the acyl acceptor. At saturating NAD" 1" and acceptor concentrations, kinetic biphasicity persists. Perturbation of the acyl-apoenzyme spectrum by NAD" 1" is also ki-