Deamination of the microbial toxin trans L ¯ ¯ ‐2‐AMINO‐4‐METHOXY‐3‐BUTENOIC acid and its parent vinylglycine by sheep liver serine-threonine dehydratase

The microbial toxin trans L ¯ ¯ ‐2‐amino‐4‐methoxy‐3‐butenoic acid and its parent vinylglycine are deaminated to alpha ketoacids by sheep liver serine threonine dehydratase. The ability of the dehydratase to deaminate the above compounds is consistent with the proposed mechanism for dehydratases. Si...

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Published inBiochemical and biophysical research communications Vol. 65; no. 2; pp. 765 - 769
Main Authors Kapke, Gordon, Davis, Leodis
Format Journal Article
LanguageEnglish
Published United States Elsevier Inc 22.07.1975
Subjects
Alkenes
Aminobutyrates
Animals
Glycine
Kinetics
L-Serine Dehydratase - metabolism
Liver - enzymology
Sheep
Toxins, Biological
Vinyl Compounds
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Summary:The microbial toxin trans L ¯ ¯ ‐2‐amino‐4‐methoxy‐3‐butenoic acid and its parent vinylglycine are deaminated to alpha ketoacids by sheep liver serine threonine dehydratase. The ability of the dehydratase to deaminate the above compounds is consistent with the proposed mechanism for dehydratases. Since these compounds irreversibly inhibit pig heart aspartate aminotransferase (1), the dehydratase may act as a detoxification pathway.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
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ISSN:0006-291X
1090-2104
DOI:10.1016/S0006-291X(75)80211-7