Mechanistic aspects of coenzyme B12-dependent rearrangements
β Scribed by Jack Halpern
- Publisher
- Elsevier Science
- Year
- 1989
- Tongue
- English
- Weight
- 47 KB
- Volume
- 36
- Category
- Article
- ISSN
- 0162-0134
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π SIMILAR VOLUMES
The crystal structure of glutamate mutase with bound coenzyme B(12) suggests a radical shuttling mechanism within the active site of the enzyme. Quantum chemical calculations of the rearrangement in combination with kinetic and mutational studies suggest the catalytic mechanism of this enzyme to pro
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 fr