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A mechanism for the transfer of the carboxyl‐group from 1'‐ N ‐carboxybiotin to acceptor substrates by biotin‐containing enzymes
Author(s) -
Goodall G.J.,
Prager R.,
Wallace J.C.,
Keech D.B.
Publication year - 1983
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(83)81150-8
Subject(s) - acceptor , chemistry , substrate (aquarium) , biotin , enzyme , molecule , stereochemistry , reaction mechanism , catalysis , biochemistry , organic chemistry , biology , ecology , physics , condensed matter physics
Previous proposals for the mechanism by which biotin‐dependent enzymes catalyse the transfer of the carboxyl group from 1'‐ N ‐carboxybiotin to acceptor molecules do not appear to be consistent with all of the experimental observations now available. We propose a multi‐step mechanism in which (a) substrate and then carboxybiotin bind at the second partial reaction site, (b) a base positioned adjacent to the 3'‐ N of the carboxybiotin abstracts a proton from the 3'‐ N and (c) the resulting enolate ion and the acceptor substrate undergo a concerted reaction resulting in carboxyl‐group transfer.