| Literature DB >> 3279419 |
K S Browning1, D J Uhlinger, L J Reed.
Abstract
Rabbit antiserum to the dihydrolipoamide dehydrogenase (dihydrolipoamide:NAD+ oxidoreductase, EC 1.8.1.4) component of the pyruvate dehydrogenase complex from bakers' yeast was used to screen plaques produced by a lambda gt11 yeast cDNA library. A 2.1-kilobase insert was isolated that also hybridized to a 17-base mixed oligonucleotide probe corresponding to the amino-terminal sequence of the yeast dihydrolipoamide dehydrogenase. The cDNA has a coding sequence of 499 amino acids that corresponds to a 21-residue signal peptide and a 478-residue mature protein (Mr = 51,558). Computer analysis shows that yeast dihydrolipoamide dehydrogenase has about 41% amino acid identity with Escherichia coli dihydrolipoamide dehydrogenase. Particularly striking is the conservation of sequence in the active site region of the dihydrolipoamide dehydrogenases from E. coli, yeast, and pig heart.Entities:
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Year: 1988 PMID: 3279419 PMCID: PMC279873 DOI: 10.1073/pnas.85.6.1831
Source DB: PubMed Journal: Proc Natl Acad Sci U S A ISSN: 0027-8424 Impact factor: 11.205