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Sequence conservation in the α and β subunits of pyruvate dehydrogenase and its similarity to branched‐chain α‐keto acid dehydrogenase
Author(s) -
Wexler Isaiah D.,
Hemalatha Sullia G.,
Patel Mulchand S.
Publication year - 1991
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(91)80479-m
Subject(s) - pyruvate dehydrogenase complex , branched chain alpha keto acid dehydrogenase complex , protein subunit , homology (biology) , biochemistry , dehydrogenase , peptide sequence , amino acid , biology , oxoglutarate dehydrogenase complex , pyruvate dehydrogenase phosphatase , chemistry , enzyme , gene
Amino acid sequence comparison of 8α and 6β subunits of the α‐keto acid dehydrogenase (E 1 ) component of the pyruvate dehydrogenase complex and branched‐chain α‐keto acid dehydrogenase complex from multiple species was performed by computer analysis. In addition to 2 previously recognized regions of homology in the α subunit, a 3rd region of extensive homology was identified in E 1 α, and may be one of the sites involved in subunit interaction. E 1 β contains 4 regions of extensive homology. Region 1 contains 10 amino acids that are homologous to a 10‐amino acid stretch in Escherichia coli E 1 . Regions 2 and 3 have sequence homologies with other dehydrogenases suggesting that these regions may be involved in catalysis.