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...
Saved in:
Published in | Biochemical and biophysical research communications Vol. 65; no. 2; pp. 765 - 769 |
---|---|
Main Authors | , |
Format | Journal Article |
Language | English |
Published |
United States
Elsevier Inc
22.07.1975
|
Subjects | |
Online Access | Get full text |
Cover
Loading…
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 content type line 23 |
ISSN: | 0006-291X 1090-2104 |
DOI: | 10.1016/S0006-291X(75)80211-7 |