Conservation of primary structure in the lipoyl-bearing and dihydrolipoyl dehydrogenase binding domains of mammalian branched-chain .alpha.-keto acid dehydrogenase complex: molecular cloning of human and bovine transacylase (E2) cDNAs-Reference-Cited by-同舟云学术

Conservation of primary structure in the lipoyl-bearing and dihydrolipoyl dehydrogenase binding domains of mammalian branched-chain .alpha.-keto acid dehydrogenase complex: molecular cloning of human and bovine transacylase (E2) cDNAs

Published:1988-03-22 Issue:6 Volume:27 Page:1972-1981
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Lau Kim S.,Griffin Thomas A.,Hu Chii Whei C.,Chuang David T.

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi00406a025

Reference48 articles.

1. Self-assembly and catalytic activity of the pyruvate dehydrogenase multienzyme complex of Escherichia coli

2. Subunit structure of dihydrolipoyl transacetylase component of pyruvate dehydrogenase complex from Escherichia coli

3. Subunit structure of dihydrolipoyl transacetylase component of pyruvate dehydrogenase complex from bovine heart.

4. Primary structure around the lipoate-attachment site on the E2 component of bovine heart pyruvate dehydrogenase complex

5. Rapid intersite transfer of acetyl groups and movement of pyruvate dehydrogenase component in the kidney pyruvate dehydrogenase complex.

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