Structure of Human Isovaleryl-CoA Dehydrogenase at 2.6 Å Resolution: Structural Basis for Substrate Specificity,-Reference-Cited by-同舟云学术

Structure of Human Isovaleryl-CoA Dehydrogenase at 2.6 Å Resolution: Structural Basis for Substrate Specificity,

Published:1997-07-01 Issue:28 Volume:36 Page:8455-8464
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Tiffany Karen A.¹,Roberts David L.¹,Wang Ming¹,Paschke Rosemary¹,Mohsen Al-Walid A.¹,Vockley Jerry¹,Kim Jung-Ja P.¹

Affiliation:

1. Department of Biochemistry, Medical College of Wisconsin, Milwaukee, Wisconsin 53226, and Department of Medical Genetics, Mayo Clinic and Mayo Foundation, Rochester, Minnesota 55905

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi970422u

Reference42 articles.

1. Rat very-long-chain acyl-CoA dehydrogenase, a novel mitochondrial acyl-CoA dehydrogenase gene product, is a rate-limiting enzyme in long-chain fatty acid beta-oxidation system. cDNA and deduced amino acid sequence and distinct specificities of the cDNA-expressed protein.

2. Characterization of wild-type and an active site mutant of human medium chain acyl-CoA dehydrogenase after expression in Escherichia coli.

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