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The Selectivity for Cysteine over Serine in Coenzyme A Biosynthesis
Author(s) -
Strauss Erick,
Begley Tadhg P.
Publication year - 2005
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.200400340
Subject(s) - serine , cysteine , biosynthesis , selectivity , coenzyme a , cofactor , chemistry , enzyme , biochemistry , amino acid , stereochemistry , catalysis , reductase
The cysteine‐derived thiol group of coenzyme A (CoA) is the key functional group involved in catalysis by this cofactor. Since CoA analogues are potent antibiotics, it is critical that CoA biosynthetic enzymes show high selectivity for the incorporation of cysteine over closely related amino acids such as serine (see scheme). In this study, we determine that the cysteine/serine selectivity ratio in CoA biosynthesis is >5.0×10 5 , and localize this selectivity to two enzymes in the pathway.