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Evidence for a Mechanism Involving Transient Fragmentation in Carbon Skeleton Rearrangements Dependent on Coenzyme B 12
Author(s) -
Beatrix Birgitta,
Zelder Oskar,
Kroll Friedrich K.,
Örlygsson Gissur,
Golding Bernard T.,
Buckel Wolfgang
Publication year - 1995
Publication title -
angewandte chemie international edition in english
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 0570-0833
DOI - 10.1002/anie.199523981
Subject(s) - adenosylcobalamin , chemistry , stereochemistry , photochemistry , cofactor , enzyme , biochemistry
Enzyme kinetics and EPR spectroscopy provide evidence that in the reversible rearrangement of ( S )‐glutamate ( 1 ) to (2 S , 3 S )‐3‐methylaspartate ( 2 ), which is catalyzed by the coenzyme B 12 dependent glutamate mutase from Clostridium cochlearium , the substrate 1 fragments into acrylate ( 3 ) and glycine radical ( 4 ), which recombine to 2 . Ado‐CH 2 ‐Cbl 5′‐adenosylcobalamin (coenzyme B 12 ).