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Synthesis of acyl‐S‐pantetheine by rat liver microsomes
Author(s) -
Sribney Michael,
Dove Jerre L.
Publication year - 1978
Publication title -
lipids
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.601
H-Index - 120
eISSN - 1558-9307
pISSN - 0024-4201
DOI - 10.1007/bf02533712
Subject(s) - acylation , microsome , coenzyme a , chemistry , cofactor , diacylglycerol kinase , lipidology , biochemistry , acyl coa , enzyme , clinical chemistry , stereochemistry , reductase , catalysis , protein kinase c
The synthesis of acyl‐S‐pantetheine was found to occur in rat liver microsomal preparations. The reaction required ATP and a metal ion as cofactors, a fatty acid and the reduced form of pantetheine for optimal activity. The K m for pantetheine was 0.8 mM, for ATP 0.8 mM, and for oleic acid 0.3 mM. Mg 2+ (20 mM), Mn 2+ (5 mM), Ca 2+ (5 mM), and Fe 2+ (5 mM) produced approximately equal activity when all other conditions were optimal. The characterization of the product and other properties of the enzyme are described. The acyl‐S‐pantetheine formed does not act as an acyl donor in the acylation of sn ‐glycerol‐3‐phosphate, 1,2‐diacylglycerol, or lysolecithin.