Transient kinetic studies of fatty acid synthetase. A kinetic self-editing mechanism for the loading of acetyl and malonyl residues and the role of coenzyme A.-Reference-Cited by-同舟云学术

Transient kinetic studies of fatty acid synthetase. A kinetic self-editing mechanism for the loading of acetyl and malonyl residues and the role of coenzyme A.

Published:1984-01 Issue:1 Volume:259 Page:134-140
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Soulié J M,Sheplock G J,Tian W X,Hsu R Y

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference17 articles.

1. .;Linn;J. Biol. Chem.,1980

2. Coenzyme A requirement for the termination reaction of rat liver fatty acid synthetase.

3. The coenzyme A requirement of mammalian fatty acid synthetase: Evidence for involvement in the elongation of acyl-enzyme thioesters

4. The free coenzyme A requirement of animal fatty acid synthetase. Participation in the continuous exchange of acetyl and malonyl moieties between coenzyme a thioester and enzyme.

5. Evidence that the coenzyme a requirement for avian fatty acid synthase is not for the ermination reaction

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