The Enzymic Interconversion of Isobutyryl and  n ‐Butyrylcarba(dethia)‐Coenzyme A: A Coenzyme‐B 12 ‐dependent Carbon Skeleton Rearrangement | Zendy

Brendelberger Günther | Zendy; Rétey János | Zendy; Ashworth Doreen M. | Zendy; Reynolds Kevin | Zendy; Willenbrock Frances | Zendy; Robinson John A. | Zendy

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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.

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