INTERACTION OF ACETYL-COA FRAGMENTS WITH RAT-LIVER ACETYL-COA CARBOXYLASE

被引：1

作者：

RABINKOV, AG ^{[1
]}

VELIKODVORSKAYA, VV ^{[1
]}

KOPELEVICH, VM ^{[1
]}

TOLOSA, EA ^{[1
]}

GUNAR, VI ^{[1
]}

机构：

[1] ALL UNION VITAMIN RES INST,MOSCOW,USSR

来源：

EUROPEAN JOURNAL OF BIOCHEMISTRY | 1990年 / 193卷 / 02期

关键词：

D O I：

10.1111/j.1432-1033.1990.tb19345.x

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：

The interaction of acetyl‐CoA fragments with rat liver acetyl‐CoA carboxylase has been studied. Dephosphorylated acetyl‐CoA did not actually differ from acetyl‐CoA in its substrate properties. Non‐nucleotide analogues of the substrate, S‐acetylpantatheine and it's 4′‐phosphate, also possess substrate properties (Vmax= 1.5% and 15% of the maximal rate value of acetyl‐CoA carboxylation, respectively). The nucleotide fragment in the acetyl‐CoA molecule produces a marked effect on the thermodynamics of the substrate‐enzyme interaction, and is apparently involved in activation and appropriate orientation of the acetyl group in the active site. The better substrate properties of S‐acetylpantetheine 4′‐phosphate and the inhibitory properties of pantetheine 4′‐phosphate, compared to the unphosphorylated analogues, evidence an important role of the 5′‐β‐phosphate of 3′‐phosphorylated ADP residue in acetyl‐CoA binding to the enzyme. Copyright © 1990, Wiley Blackwell. All rights reserved

引用

页码：351 / 353

页数：3

共 16 条

[1]

AMONTOV S V, 1988, Molekulyarnaya Biologiya (Moscow), V22, P195

[2] SYNTHESIS OF ACETYL-COA AND ACETYL-DEPHOSPHO-COA BY ACETYL-COA SYNTHETASE IN RAT [J].