Specificity determinants for the pyruvate dehydrogenase component reaction mapped with mutated and prosthetic group modified lipoyl domains.

doi:10.1074/jbc.275.18.13645

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Article

Specificity determinants for the pyruvate dehydrogenase component reaction mapped with mutated and prosthetic group modified lipoyl domains.

The Journal of biological chemistry - 5 May 2000

Gong X, Peng T, Yakhnin A, Zolkiewski M, Quinn J, Yeaman S J, Roche T E

Abstract excerpt

Efficient catalysis in the second step of the pyruvate dehydrogenase (E1) component reaction requires a lipoyl group to be attached to a lipoyl domain that displays appropriately positioned specificity residues. As substrates, the human dihydrolipoyl acetyltransferase provides an N-terminal (L1) and an inner (L2) lipoyl domain. We evaluated the specificity requirements for the E1 reaction with 27 mutant L2...

Topics

Animals
Binding Sites
Cattle
Escherichia coli
Humans
Mutation
Protein Conformation
Pyruvate Dehydrogenase Complex
Structure-Activity Relationship
Substrate Specificity

Source

Open in PubMed

Identifiers

PMID: 10788482
DOI: 10.1074/jbc.275.18.13645

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