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• W2087806475 abstract "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 proceed via a fragmentation/recombination sequence with intermediates stabilized by partial protonation/deprotonation. Crucial residues in the active site have been identified. Solution structure studies indicate the mechanism of B(12) binding to the apoenzyme." @default.
• W2087806475 created "2016-06-24" @default.
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• W2087806475 date "2002-10-01" @default.
• W2087806475 modified "2023-09-23" @default.
• W2087806475 title "Coenzyme B12 dependent glutamate mutase" @default.
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• W2087806475 doi "https://doi.org/10.1016/s1367-5931(02)00368-x" @default.
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