Evidence for a Mechanism Involving Transient Fragmentation in Carbon Skeleton Rearrangements Dependent on Coenzyme B 12 | Zendy

Beatrix Birgitta | Zendy; Zelder Oskar | Zendy; Kroll Friedrich K. | Zendy; Örlygsson Gissur | Zendy; Golding Bernard T. | Zendy; Buckel Wolfgang | Zendy

AI Assistant Blog Pricing

Home ZAIA Blog

Premium

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 ).

This content is not available in your region!

Continue researching here.

Having issues? You can contact us here

Accelerating Research