Inactivation of short-chain acyl-coenzyme A dehydrogenase from pig liver by 2-pentynoyl-coenzyme A.
2-Pentynoyl-CoA is a mechanism-based inactivator of the flavoprotein short-chain acyl-CoA dehydrogenase from pig liver. Inactivation is associated with the formation of an intermediate absorbing at 800 nm and results in the incorporation of 0.86 +/- 0.13 molecules of radiolabeled inhibitor per subunit. A rapid procedure was devised to isolate the labeled peptide. A glutamate residue was identified as the target of 2-pentynoyl-CoA treatment and proved homologous to the proposed catalytic base, GLU376, in the corresponding medium-chain acyl-CoA dehydrogenase sequence. These results are discussed in terms of the lack of conservation of this glutamate residue in the acyl-CoA dehydrogenase enzyme family.
Lundberg
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Department of Chemistry and Biochemistry, University of Delaware, Newark 19716.
Thorpe
C
C
D000214:Acyl Coenzyme A / Q000494:pharmacology*; D042964:Acyl-CoA Dehydrogenase; D044944:Acyl-CoA Dehydrogenases / Q000037:antagonists & inhibitors* / Q000737:chemistry; D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D005971:Glutamates / Q000737:chemistry; D008099:Liver / Q000201:enzymology*; D008969:Molecular Sequence Data; D010449:Peptide Mapping; D017386:Sequence Homology, Amino Acid; D013552:Swine
D000214:Acyl Coenzyme A; D005971:Glutamates; C083148:2-pentynoyl-coenzyme A; D044944:Acyl-CoA Dehydrogenases; D042964:Acyl-CoA Dehydrogenase