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Stereochemistry of the methylmalonyl‐CoA decarboxylation reaction
Author(s) -
Hoffmann Artur,
Dimroth Peter
Publication year - 1987
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(87)80888-8
Subject(s) - decarboxylation , chemistry , steric effects , substrate (aquarium) , walden inversion , stereochemistry , biochemistry , catalysis , biology , ecology
The steric course of the decarboxylation of ( S )‐methylmalonyl‐CoA to propionyl‐CoA, catalyzed by the biotin‐dependent sodium pump methylmalonyl‐CoA decarboxylase of Veillonella alcalescens was determined. The decarboxylation of ( S )‐methylmalonyl‐CoA in 3 H 2 O yielded ( R )‐[2‐ 3 H]propionyl‐CoA; and the decarboxylation of ( S )‐[2‐ 3 H]methylmalonyl‐CoA in H 2 O produced ( S )‐[2‐ 3 H]propionyl‐CoA. The results demonstrate retention of configuration during the decarboxylation reaction. The substrate stereochemistry of methylmalonyl‐CoA decarboxylase is thus the same as that of all other biotin‐containing enzymes investigated.