Kinetic mechanism and order of substrate binding for sn-glycerol-3-phosphate acyltransferase from squash (Cucurbita moschata)

Autor: Hayman, Matthew W., Fawcett, Tony, Slabas, Antoni R.
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Zdroj: FEBS Letters; Mar2002, Vol. 514 Issue 2/3, p281, 4p
Abstrakt: sn-Glycerol-3-phosphate acyltransferase (G3PAT, EC 2.3.1.15), a component of glycerolipid biosynthesis, is an important enzyme in chilling sensitivity in plants. The three-dimensional structure of the enzyme from squash (Cucurbita moschata), without bound substrate, has been determined [Turnbull et al. (2001) Acta Crystallogr. D 57, 451–453; Turnbull et al. (2001) Structure 9, 347–353]. Here we report the kinetic mechanism of plastidial G3PAT from squash and the order of substrate binding using acyl-acyl carrier protein (acyl-ACP) substrates. The reaction proceeds via a compulsory-ordered ternary complex with acyl-ACP binding before glycerol-3-phosphate. We have also determined that the reaction will proceed with C4:0-CoA, C6:0-CoA and C12:0-ACP substrates, allowing a wider choice of acyl groups for future co-crystallisation studies. [Copyright &y& Elsevier]
Databáze: Complementary Index
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