Animal fatty acid synthetase. Identification of the residues comprising the novel arrangement of the beta-ketoacyl synthetase site and their role in its cold inactivation.-Reference-Cited by-同舟云学术

Animal fatty acid synthetase. Identification of the residues comprising the novel arrangement of the beta-ketoacyl synthetase site and their role in its cold inactivation.

Published:1982-03 Issue:6 Volume:257 Page:3230-3235
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Stoops J K,Wakil S J

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference12 articles.

1. Animal fatty acid synthetase. A novel arrangement of the beta-ketoacyl synthetase sites comprising domains of the two subunits.

2. Further evidence for the multifunctional enzyme characteristic of the fatty acid synthetases of animal tissues

3. Yeast fatty acid synthetase: Structure--function relationship and nature of the -ketoacyl synthetase site

4. The yeast fatty acid synthetase. Structure-function relationship and the role of the active cysteine-SH and pantetheine-SH.

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