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Review Article Coenzyme-B(12)-Dependent Glutamate Mutase
1Department of Chemistry, University of Michigan, Ann Arbor, Michigan, 48109-1055
Bioorganic Chemistry
|February 7, 2001
Summary
Adenosylcobalamin (coenzyme B12)-dependent glutamate mutase uniquely rearranges the carbon skeleton of l-glutamate. This enzyme
Area of Science:
- Biochemistry
- Enzymology
- Organic Chemistry
Background:
- Adenosylcobalamin (coenzyme B12) is essential for various enzymatic reactions.
- Glutamate mutase catalyzes an unprecedented carbon skeleton rearrangement.
- Free radical mechanisms are involved in adenosylcobalamin-dependent catalysis.
Purpose of the Study:
- To review recent studies on glutamate mutase.
- To elucidate the mechanism and structure of glutamate mutase.
- To understand adenosylcobalamin-mediated catalysis.
Main Methods:
- Structural analysis of glutamate mutase.
- Mechanistic studies of the enzymatic reaction.
- Investigation of free radical intermediates.
Main Results:
- The enzyme catalyzes the isomerization of l-glutamate to L-threo-methylaspartate.
- The reaction mechanism involves homolysis of the cobalt-carbon bond, generating free radicals.
- Glutamate mutase serves as a model for radical-generating enzymes.
Conclusions:
- Recent structural and mechanistic studies enhance understanding of glutamate mutase.
- The enzyme provides insights into enzymatic control of reactive free radicals.
- Adenosylcobalamin-dependent catalysis is a unique biochemical process.
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