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- W2023358841 abstract "Unfractionated extracts of Clostridium kluyveri are shown to convert the vinylacetyl thioester of N-acetylthioethanolamine (SE) almost quantitatively to the corresponding crotonyl derivative. Crotonyl-SE accumulates because it is not hydrated by crotonase (enoyl hydrase). When vinylacetylpantetheine is used as a substrate, crotonylpantetheine first accumulates and subsequently is converted by crotonase to β-hydroxybutyrylpantetheine. The enzyme vinylacetyl isomerase, which catalyzes the conversion of vinylacetyl thioesters to crotonyl thioesters, has been partially purified and some of its kinetic properties have been determined. The enzyme appears to be relatively specific for vinylacetyl thioesters. With a crotonase-free isomerase preparation, the conversion of vinylacetyl-SCoA to crotonyl-SCoA was observed spectrophotometrically. The isomerization reaction is relatively irreversible; with crotonyl-SE as the substrate no reaction could be detected. Vinylacetyl isomerase activity has also been observed in extracts of Clostridium tetanomorphum and sheep liver." @default.
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- W2023358841 date "1961-01-01" @default.
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- W2023358841 title "A vinylacetyl isomerase from Clostridium kluyveri" @default.
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- W2023358841 doi "https://doi.org/10.1016/0003-9861(61)90226-0" @default.
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