Premium
Selective inhibition of lignoceroyl‐CoA synthetase by adenosine 5′‐alkylphosphates
Author(s) -
Shiraishi Takayuki,
Tezuka Kazuko,
Uda Yutaka
Publication year - 1994
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(94)00992-9
Subject(s) - adenosine , chemistry , substrate (aquarium) , enzyme , biochemistry , stereochemistry , alkyl , substrate specificity , biology , organic chemistry , ecology
Structural analogs of adenosine 5′‐acylphosphates, which are intermediates of the reaction catalysed by acyl‐CoA synthetases, were synthesized by condensing primary alcohols with AMP to examine the inhibitory effects on the lignoceroyl‐CoA and palmitoyl‐CoA synthetase activities. Hexadecyl, octadecyl, eicosyl, docosyl and tetracosyl esters of AMP were remarkably potent inhibitors of the lignoceroyl‐CoA formation. On the other hand, the eicosyl, docosyl or tetracosyl esters of AMP did not behave as significant inhibitors of the palmitoyl‐CoA formation at the concentration at which the two other shorter chain analogs were effective. Namely, these longer alkyl esters of AMP have selective inhibitory effects on the lignoceroyl‐CoA synthetase activity. The K i value of adenosine 5′‐tetracosylphosphate, the most potent inhibitor, was about one tenth lower than the K m value for the substrate lignoceric acid. Furthermore, the results support the notion that lignoceroyl‐CoA synthetase is distinct from palmitoyl‐CoA synthetase.