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The Enzymic Interconversion of Isobutyryl and n ‐Butyrylcarba(dethia)‐Coenzyme A: A Coenzyme‐B 12 ‐dependent Carbon Skeleton Rearrangement
Author(s) -
Brendelberger Günther,
Rétey János,
Ashworth Doreen M.,
Reynolds Kevin,
Willenbrock Frances,
Robinson John A.
Publication year - 1988
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.198810891
Subject(s) - mutase , cofactor , stereochemistry , chemistry , coenzyme a , derivative (finance) , carbon skeleton , enzyme , biochemistry , reductase , financial economics , economics
The synthetic carba(dethia) analogues of coenzyme A contain a —CO—CH 2 —instead of a —CO—S— group and are therefore hydrolytically stable. The isobutyrylcarba(dethia) coenzyme A 1 , whose synthesis is reported here, is isomerized to the n ‐butyryl derivative 2 by a cell extract from Streptomyces cinnamonensis (monitored by 1 H NMR). This new, coenzyme B 12 ‐dependent structural rearrangement is similar in many ways to the long‐known methylmalonyl‐CoA mutase reaction.