Review Article Coenzyme-B12-Dependent Glutamate Mutase

✍ Scribed by E.Neil G. Marsh

• Publisher: Elsevier Science
• Year: 2000
• Tongue: English
• Weight: 210 KB
• Volume: 28
• Category: Article
• ISSN: 0045-2068
• DOI: 10.1006/bioo.2000.1168

✦ Synopsis

Adenosylcobalamin (coenzyme B12)-dependent glutamate mutase catalyzes a most unusual carbon skeleton rearrangement involving the isomerization of l-glutamate to L-threo-methylaspartate, a reaction that is without precedent in organic chemistry. This reaction proceeds through a mechanism involving free radical intermediates that are initiated by homolysis of the cobalt-carbon bond of the coenzyme. The enzyme serves as a paradigm for adenosylcobalamin-dependent catalysis and, more generally, provides insights into how enzymes generate and control reactive free radical species. This review describes how recent studies on the mechanism and structure of glutamate mutase have contributed to our understanding of adenosylcobalamin-mediated catalysis. Copyright 2000 Academic Press.