Crystal Structures of the Wild Type and the Glu376Gly/Thr255Glu Mutant of Human Medium-Chain Acyl-CoA Dehydrogenase: Influence of the Location of the Catalytic Base on Substrate Specificity-Reference-Cited by-同舟云学术

Crystal Structures of the Wild Type and the Glu376Gly/Thr255Glu Mutant of Human Medium-Chain Acyl-CoA Dehydrogenase: Influence of the Location of the Catalytic Base on Substrate Specificity

Published:1996-01-01 Issue:38 Volume:35 Page:12412-12420
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Lee Hyun-Joo K.¹,Wang Ming¹,Paschke Rosemary¹,Nandy Andreas¹,Ghisla Sandro¹,Kim Jung-Ja P.¹

Affiliation:

1. Department of Biochemistry, Medical College of Wisconsin, Milwaukee, Wisconsin 53226, and Faculty of Biology, University of Konstanz, P.O. Box 5560-M644, D-78434 Konstanz, Germany

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi9607867

Reference29 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. Beinert, H. (1963) inThe Enzymes, 2nd ed. (Bpyer, P. D., Lardy, H. & Myrback, K., Eds.) Vol. 7, pp 447−466, Academic Press, New York.

3. 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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