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Oxidation-reduction of general acyl-CoA dehydrogenase by the butyryl-CoA/crotonyl-CoA couple : a new investigation of the rapid reaction kinetics

Oxidation-reduction of general acyl-CoA dehydrogenase by the butyryl-CoA/crotonyl-CoA couple : a new investigation of the rapid reaction kinetics

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SCHOPFER, Lawrence M., Vincent MASSEY, Sandro GHISLA, Colin THORPE, 1988. Oxidation-reduction of general acyl-CoA dehydrogenase by the butyryl-CoA/crotonyl-CoA couple : a new investigation of the rapid reaction kinetics. In: Biochemistry. 27(17), pp. 6599-6611. ISSN 0006-2960. eISSN 1520-4995

@article{Schopfer1988Oxida-8315, title={Oxidation-reduction of general acyl-CoA dehydrogenase by the butyryl-CoA/crotonyl-CoA couple : a new investigation of the rapid reaction kinetics}, year={1988}, doi={10.1021/bi00417a059}, number={17}, volume={27}, issn={0006-2960}, journal={Biochemistry}, pages={6599--6611}, author={Schopfer, Lawrence M. and Massey, Vincent and Ghisla, Sandro and Thorpe, Colin} }

<rdf:RDF xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#" xmlns:bibo="http://purl.org/ontology/bibo/" xmlns:dc="http://purl.org/dc/elements/1.1/" xmlns:dcterms="http://purl.org/dc/terms/" xmlns:xsd="http://www.w3.org/2001/XMLSchema#" > <rdf:Description rdf:about="https://kops.uni-konstanz.de/rdf/resource/123456789/8315"> <dc:creator>Thorpe, Colin</dc:creator> <dcterms:abstract xml:lang="eng">Pig kidney general acyl-CoA dehydrogenase (GAD) can be reduced by butyryl-CoA to form reduced enzyme and crotonyl-CoA. This reaction is reversible. Stopped-flow, kinetic investigations on GAD have been made, using the following reaction pairs: oxidized GAD/butyryl-CoA, oxidized GAD/crotonyl-CoA, oxidized GAD/α,β-dideuteriobutyryl-CoA, reduced GAD/butyryl-CoA, and reduced GAD/crotonyl-CoA (in 50 mM potassium phosphate buffer, pH 7.6 at 4°C). Reduction of GAD by butyryl-CoA is triphasic. The slowest phase is 100-fold slower than the preceding phase and appears to represent a secondary process not directly related to the primary reduction events. The first two fast phases are responsible for reduction of GAD. Reduction proceeds via a reduced enzyme/crotonyl-CoA charge-transfer complex. α,β-Dideuteriobutyryl-CoA elicits a major deuterium isotope effect (15-fold) on the reduction reaction. Oxidation of GAD by crotonyl-CoA is biphasic. Oxidation proceeds via the same reduced enzyme/crotonyl-CoA charge-transfer complex seen during reduction. The oxidation reaction ends in a mixture composed largely of oxidized GAD species. From the data, we constructed a mechanism for the reduction/oxidation of GAD by butyryl-CoA/crotonyl-CoA. This mechanism was then used to simulate all of the observed kinetic time course data, using a single set of kinetic parameters. A close correspondence between the observed and simulated data was obtained.</dcterms:abstract> <dc:contributor>Massey, Vincent</dc:contributor> <dcterms:issued>1988</dcterms:issued> <dc:contributor>Thorpe, Colin</dc:contributor> <dc:rights>deposit-license</dc:rights> <dc:format>application/pdf</dc:format> <dc:creator>Schopfer, Lawrence M.</dc:creator> <dcterms:title>Oxidation-reduction of general acyl-CoA dehydrogenase by the butyryl-CoA/crotonyl-CoA couple : a new investigation of the rapid reaction kinetics</dcterms:title> <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-03-24T17:42:37Z</dc:date> <dc:creator>Ghisla, Sandro</dc:creator> <dcterms:bibliographicCitation>First publ. in: Biochemistry 27 (1988), 17, pp. 6599-6611</dcterms:bibliographicCitation> <dc:contributor>Ghisla, Sandro</dc:contributor> <dcterms:rights rdf:resource="https://creativecommons.org/licenses/by-nc-nd/2.0/legalcode"/> <bibo:uri rdf:resource="http://kops.uni-konstanz.de/handle/123456789/8315"/> <dc:contributor>Schopfer, Lawrence M.</dc:contributor> <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-03-24T17:42:37Z</dcterms:available> <dc:language>eng</dc:language> <dc:creator>Massey, Vincent</dc:creator> </rdf:Description> </rdf:RDF>

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