Hepatic microsomal short-chain β-hydroxyacyl-CoA dehydrase distinct from the fatty acid elongation component: Substrate specificity of the membrane-extracted enzyme
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Biochemistry,Biophysics
Reference23 articles.
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2. An analysis of partial reactions in the overall chain elongation of saturated and unsaturated fatty acids by rat liver microsomes.
3. Solubilization and partial purification of an enzyme involved in rat liver microsomal fatty acid chain elongation: beta-hydroxyacyl-CoA dehydrase.
4. Evidence for a second microsomal trans-2-enoyl coenzyme A reductase in rat liver. NADPH-specific short chain reductase.
5. Rat hepatic microsomal acetoacetyl-CoA reductase. A beta-ketoacyl-CoA reductase distinct from the long chain beta-ketoacyl-CoA reductase component of the microsomal fatty acid chain elongation system.
Cited by 7 articles. 订阅此论文施引文献 订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献
1. Thermodynamics of Enzyme‐Catalyzed Reactions: Part 4. Lyases;Journal of Physical and Chemical Reference Data;1995-09
2. Evidence that β-hydroxyacyl-CoA dehydrase purified from rat liver microsomes is of peroxisomal origin;Biochemical Journal;1992-10-01
3. Enoyl-CoA hydratase;Enzyme Handbook 1;1990
4. Biochemical and immunological identity of the hepatic peroxisomal and microsomal trans-2-enoyl CoA hydratase bifunctional protein;Archives of Biochemistry and Biophysics;1987-02
5. Evidence for multiple condensing enzymes in rat hepatic microsomes catalyzing the condensation of saturated, monounsaturated, and polyunsaturated acyl coenzyme A.;Journal of Biological Chemistry;1986-06
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