Published January 1972
| public
Journal Article
Mechanism of action of coenzyme B_(12). Hydrogen transfer in the isomerization of β-methylaspartate to glutamate
Abstract
Use of a mixture of unlabeled and tetradeuterio-,Bmethylaspartate with coenzyme B_(12) dependent β-methylaspartate-glutamate mutase has shown that the hydrogen that migrates becomes one of three equivalent hydrogens during the isomerization. Kinetic isotope effects suggest that cleavage of the bond in the substrate from carbon to that hydrogen which migrates is an important component of the rate-determining step. The evidence also supports the existence of an intermediate which can partition with similar probabilities to β-methylaspartate or to glutamate. Mechanistic implications of these findings are discussed.
Additional Information
© 1972 American Chemical Society. Received July 12, 1971. Contribution No. 4228 from the Gates and Crellin Laboratories of Chemistry and Church Laboratory of Chemical Biology, California Institute of Technology, Pasadena, California 91109, and from the Department of Biochemistry, University of California, Berkeley, California 94720.Additional details
- Eprint ID
- 57077
- DOI
- 10.1021/bi00752a017
- Resolver ID
- CaltechAUTHORS:20150429-081550145
- GMS-10218
- NIH
- AI-00563
- NIH
- Created
-
2015-05-01Created from EPrint's datestamp field
- Updated
-
2021-11-10Created from EPrint's last_modified field
- Other Numbering System Name
- Caltech Gates and Crellin Laboratories of Chemistry
- Other Numbering System Identifier
- 4228