2-Hydroxybenzoyl-CoA (o-Hydroxybenzoyl-coenzyme A) lithium is a coenzyme A thioester of o-hydroxybenzoic acid and substrate for esterolysis. 2-Hydroxybenzoyl-CoA lithium serves as a substrate for studies of acyl-CoA formation, acyl transfer, and peptide bond formation reactions and enzymes [1].
In Vitro, 2-Hydroxybenzoyl-CoA lithium undergoes esterolysis via phenolate-assisted water attack on the benzoyl moiety’s carbonyl carbon, with hydrolysis rate nearly constant over pH 9.6-12.1[1]. 2-Hydroxybenzoyl-CoA lithium exists predominantly in an intramolecular adenyl-benzoyl complex under physiological conditions, which may contribute to acyl-CoA substrate specificity of acyl-CoA: amino acid N-acyltransferases[1]. 2-Hydroxybenzoyl-CoA lithium has a characteristic ultraviolet absorption spectrum with a phenolate absorbance band that red shifts with increasing pH, exploitable for discontinuous enzymatic assays[1].
References:
[1]. Leslie T. Webster, et al. Coenzyme a thioesters of benzoic, hydroxybenzoic, phenylacetic, and bile acids. Methods in Enzymology. Academic Press. Volume 77, 1981. Pages 430-436.
In Vitro, 2-Hydroxybenzoyl-CoA lithium undergoes esterolysis via phenolate-assisted water attack on the benzoyl moiety’s carbonyl carbon, with hydrolysis rate nearly constant over pH 9.6-12.1[1]. 2-Hydroxybenzoyl-CoA lithium exists predominantly in an intramolecular adenyl-benzoyl complex under physiological conditions, which may contribute to acyl-CoA substrate specificity of acyl-CoA: amino acid N-acyltransferases[1]. 2-Hydroxybenzoyl-CoA lithium has a characteristic ultraviolet absorption spectrum with a phenolate absorbance band that red shifts with increasing pH, exploitable for discontinuous enzymatic assays[1].
References:
[1]. Leslie T. Webster, et al. Coenzyme a thioesters of benzoic, hydroxybenzoic, phenylacetic, and bile acids. Methods in Enzymology. Academic Press. Volume 77, 1981. Pages 430-436.