Does microsomal glycerophosphate acyltransferase also catalyze the acylation of dihydroxyacetone phosphate?

FEBS Letters

Hajra, Amiya K.¹  Datta, Nabanita S.¹ 

[1] Neuroscience Laboratory, Mental Health Research Institute and the Department of Biological Chemistry, University of Michigan, 1103 E. Huron, Ann Arbor, MI 48109, USA

关键词: Liver microsome;    Glycerophosphate acyltransferase;    Dihydroxyacetone phosphate acyltransferase;    DHAP;    dihydroxyacetone phosphate;    GP;    sn-glycerol-3-phosphate;    AT;    acyltransferase;   

DOI  :  10.1016/0014-5793(84)80954-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Rat liver microsomal dihydroxyacetone phosphate acyltransferase, in contrast to the glycerophosphate acyltransferase, was found to be active at low pH (5.5), stable towards heat (55 °C, 15 min) and trypsin (in the absence of detergents) and was not inhibited by high concentrations of N-ethyl maleimide. Dihydroxyacetone phosphate acyltransferase is only slightly and non-competitively inhibited by sn-glycerol-3-phosphate whereas glycerophosphate acyltransferase is strongly inhibited by dihydroxyacetone phosphate in a competitive manner. Kinetic analysis indicates that this competitive inhibition is not due to the competition of two common substrates for the same active center of one enzyme. These results demonstrate that microsomal glycerophosphate acyltransferase and dihydroxyacetone phosphate acyltransferase are two distinct and separate enzymes.

【 授权许可】

Unknown