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Mechanism of action of coenzyme B_(12). Hydrogen transfer in the isomerization of β-methylaspartate to glutamate

Eagar, R. G., Jr. and Baltimore, B. G. and Herbst, M. M. and Barker, H. A. and Richards, J. H. (1972) Mechanism of action of coenzyme B_(12). Hydrogen transfer in the isomerization of β-methylaspartate to glutamate. Biochemistry, 11 (2). pp. 253-264. ISSN 0006-2960. doi:10.1021/bi00752a017.

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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.

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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.
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Caltech Gates and Crellin Laboratories of Chemistry4228
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Official Citation:Mechanism of action of coenzyme B12. Hydrogen transfer in the isomerization of .beta.-methylaspartate to glutamate R. G. Eagar Jr., B. G. Baltimore, M. M. Herbst, H. A. Barker, and J. H. Richards Biochemistry 1972 11 (2), 253-264 DOI: 10.1021/bi00752a017
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:57077
Deposited By: Tony Diaz
Deposited On:01 May 2015 17:22
Last Modified:10 Nov 2021 21:07

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