Medium-chain acyl coenzyme A dehydrogenase from pig kidney has intrinsic enoyl coenzyme A hydratase activity

Lau, Sze-Mei; Powell, Pat; Büttner, Hermann; Ghisla, Sandro; Thorpe, Colin

Medium-chain acyl coenzyme A dehydrogenase from pig kidney has intrinsic enoyl coenzyme A hydratase activity

Dateien

Medium_chain_acyl_coenzyme_A_dehydrogenase_from_pig_kidney_has_intrinsic_enoyl_coenzyme_A_hydratase_activity.pdfGröße: 1.2 MBDownloads: 630

Datum

1986

Autor:innen

Lau, Sze-Mei

Powell, Pat

Büttner, Hermann

Ghisla, Sandro

Thorpe, Colin

Open Access-Veröffentlichung

Open Access Green

Sammlungen

Biologie

Publikationstyp

Zeitschriftenartikel

Publikationsstatus

Published

Erschienen in

Biochemistry. 1986, 25(15), pp. 4184-4189. ISSN 0006-2960. eISSN 1520-4995. Available under: doi: 10.1021/bi00363a003

Zusammenfassung

The flavoprotein medium-chain acyl coenzyme A (acyl-CoA) dehydrogenase from pig kidney exhibits an intrinsic hydratase activity toward crotonyl-CoA yielding L-3-hydroxybutyryl-CoA. The maximal turnover number of about 0.5 min-1 is 500-1000-fold slower than the dehydrogenation of butyryl-CoA using electron-transferring flavoprotein as terminal acceptor. trans-2-Octenoyl- and trans-2-hexadecenoyl-CoA are not hydrated significantly. Hydration is not due to contamination with the short-chain enoyl-CoA hydratase crotonase. Several lines of evidence suggest that hydration and dehydrogenation reactions probably utilize the same active site. These two activities are coordinately inhibited by 2-octynoyl-CoA and (methylenecyclopropyl) acetyl-CoA [whose targets are the protein and flavin adenine dinucleotide (FAD) moieties of the dehydrogenase, respectively]. The hydration of crotonyl-CoA is severely inhibited by octanoyl-CoA, a good substrate of the dehydrogenase. The apoenzyme is inactive as a hydratase but recovers activity on the addition of FAD. Compared with the hydratase activity of the native enzyme, the 8-fluoro-FAD enzyme exhibits a roughly 2-fold increased activity, whereas the 5-deaza-FAD dehydrogenase is only 20% as active. A mechanism for this unanticipated secondary activity of the acyl-CoA dehydrogenase is suggested.

Fachgebiet (DDC)

570 Biowissenschaften, Biologie

Zitieren

ISO 690

LAU, Sze-Mei, Pat POWELL, Hermann BÜTTNER, Sandro GHISLA, Colin THORPE, 1986. Medium-chain acyl coenzyme A dehydrogenase from pig kidney has intrinsic enoyl coenzyme A hydratase activity. In: Biochemistry. 1986, 25(15), pp. 4184-4189. ISSN 0006-2960. eISSN 1520-4995. Available under: doi: 10.1021/bi00363a003

BibTex

@article{Lau1986Mediu-8627,
  year={1986},
  doi={10.1021/bi00363a003},
  title={Medium-chain acyl coenzyme A dehydrogenase from pig kidney has intrinsic enoyl coenzyme A hydratase activity},
  number={15},
  volume={25},
  issn={0006-2960},
  journal={Biochemistry},
  pages={4184--4189},
  author={Lau, Sze-Mei and Powell, Pat and Büttner, Hermann and Ghisla, Sandro and Thorpe, Colin}
}

RDF

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    <dcterms:abstract xml:lang="eng">The flavoprotein medium-chain acyl coenzyme A (acyl-CoA) dehydrogenase from pig kidney exhibits an intrinsic hydratase activity toward crotonyl-CoA yielding L-3-hydroxybutyryl-CoA. The maximal turnover number of about 0.5 min-1 is 500-1000-fold slower than the dehydrogenation of butyryl-CoA using electron-transferring flavoprotein as terminal acceptor. trans-2-Octenoyl- and trans-2-hexadecenoyl-CoA are not hydrated significantly. Hydration is not due to contamination with the short-chain enoyl-CoA hydratase crotonase. Several lines of evidence suggest that hydration and dehydrogenation reactions probably utilize the same active site. These two activities are coordinately inhibited by 2-octynoyl-CoA and (methylenecyclopropyl) acetyl-CoA [whose targets are the protein and flavin adenine dinucleotide (FAD) moieties of the dehydrogenase, respectively]. The hydration of crotonyl-CoA is severely inhibited by octanoyl-CoA, a good substrate of the dehydrogenase. The apoenzyme is inactive as a hydratase but recovers activity on the addition of FAD. Compared with the hydratase activity of the native enzyme, the 8-fluoro-FAD enzyme exhibits a roughly 2-fold increased activity, whereas the 5-deaza-FAD dehydrogenase is only 20% as active. A mechanism for this unanticipated secondary activity of the acyl-CoA dehydrogenase is suggested.</dcterms:abstract>
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