FUNCTION AND ROLE OF NAD+ IN MECHANISM OF ACTION OF RABBIT-MUSCLE GLYCERALDEHYDEPHOSPHATE DEHYDROGENASE

被引：30

作者：

DEVIJLDER, JJ

HILVERS, AG

VANLIS, JMJ

SLATER, EC

机构：

[1] Laboratory of Biochemistry, B. C. P. Jansen Institute, University of Amsterdam, Amsterdam

[2] Laboratory of Clinical Biochemistry, Central Hospital, Alkmaar

来源：

BIOCHIMICA ET BIOPHYSICA ACTA | 1969年 / 191卷 / 02期

关键词：

D O I：

10.1016/0005-2744(69)90241-1

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

1. 1. NAD+ is required for the oxidation of NADH by 1,3-diphosphoglycerate or acetyl phosphate. 2. 2. The maximal rate of acetyl phosphate reduction by NADH or APADH is reached when about 3 moles NAD+ per mole enzyme are added. Larger amounts of NAD+ inhibit with a Ki (NADH as substrate) equal to 45 μM. 3. 3. The NAD-binding site with the lowest affinity for NAD+ appears to be the most active in the dehydrogenase reaction. Under optimal conditions the E-(NAD)3 complex is the catalytically active enzyme. 4. 4. The E-(NAD)3 complex appears also to be the form with maximal catalytic activity in the transferase reactions. 5. 5. NAD+ can be replaced by APAD+ in both the dehydrogenase and arsenolysis reactions. © 1969.

引用

页码：221 / +

页数：1

共 29 条

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[12] REACTION MECHANISM OF D-GLYCERALDEHYDE-3-PHOSPHATE - NAD+ OXIDOREDUCTASE ( PHOSPHORYLATING ) OF RABBIT MUSCLE [J].