Direct Hydrogen Transfer by Methylmalonyl Coenzyme a Mutase.
نویسندگان
چکیده
In this scheme, the racemase involves a rearrangement of the hydrogen about the asymmetrical carbon (6,7), while the mutase reaction involves an intramolecular migration (8, 9) of the thioester group (l&12). Two approaches are available to determine the source of the hydrogen that arises on carbon 3 of succinyl-CoA as a result of methylmalonyl-Coil mutase action. The first or indirect approach, namely, the use of tritiated water, has determined that this hydrogen does not originate from water (13). This approach is indicative, but not conclusive, when dilute isotopes are used, because of the possibility of isotope discrimination. Proof as to the origin of the
منابع مشابه
The Absolute Configuration of Methylmalonyl Coenzyme A and Stereochemistry of the Methylmalonyl Coenzyme A Mutase Reaction*
Rropionyl coenzyme A was carboxylated with epimerasefree carboxylase, and the resulting methylmalonyl coenzyme A (a) was reduced with Raney nickel. Isolation of (-)(R)-P-hydroxyisobutyric acid N-phenylcarbamate (11) from the reaction mixture showed that methylmalonyl coenzyme A (a) has the (S) configuration. Propionyl coenzyme A was also converted to deuteriosuccinate with a DrO extract of a be...
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Rropionyl coenzyme A was carboxylated with epimerasefree carboxylase, and the resulting methylmalonyl coenzyme A (a) was reduced with Raney nickel. Isolation of (-)(R)-P-hydroxyisobutyric acid N-phenylcarbamate (11) from the reaction mixture showed that methylmalonyl coenzyme A (a) has the (S) configuration. Propionyl coenzyme A was also converted to deuteriosuccinate with a DrO extract of a be...
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ورودعنوان ژورنال:
- The Journal of biological chemistry
دوره 239 شماره
صفحات -
تاریخ انتشار 1964