Literature DB >> 29894

The stereochemical course of acetate activation by yeast acetyl-CoA synthetase.

C F Midelfort, I Sarton-Miller.   

Abstract

The purified alpha-thiophosphate diastereoisomers of adenosine 5'-(1-thio)-triphosphate were used to study the stereochemical course of the reaction catalyzed by yeast acetyl-CoA synthetase. Asymmetrically labeled adenosine 5'-thiophosphate was formed from the "B" diastereoisomer of adenosine 5'-(1-thio)-triphosphate and [18O]acetate. The label was found to be in the opposite orientation from the leaving pyrophosphate group showing that the acetate activation step occurred with inversion of configuration at the alpha-phosphorus.

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Year:  1978        PMID: 29894

Source DB:  PubMed          Journal:  J Biol Chem        ISSN: 0021-9258            Impact factor:   5.157


  1 in total

1.  Bacillus anthracis o-succinylbenzoyl-CoA synthetase: reaction kinetics and a novel inhibitor mimicking its reaction intermediate.

Authors:  Yang Tian; Dae-Hwan Suk; Feng Cai; David Crich; Andrew D Mesecar
Journal:  Biochemistry       Date:  2008-11-25       Impact factor: 3.162

  1 in total

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