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

FEBS Letters

Hayman, Matthew W¹  Slabas, Antoni R¹  Fawcett, Tony¹ 

[1] The University of Durham, Department of Biological Sciences, Science Laboratories, South Road, Durham DH1 3LE, UK

关键词: Glycerol-3-phosphate acyltransferase;    Acyl-acyl carrier protein;    Substrate binding;    Cucurbita moschata;    ACP;    acyl carrier protein;    G3PAT;    glycerol-3-phosphate acyltransferase (EC 2.3.1.15);    LPA;    lysophosphatidic acid;   

DOI  :  10.1016/S0014-5793(02)02381-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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 C_4:0-CoA, C_6:0-CoA and C_12:0-ACP substrates, allowing a wider choice of acyl groups for future co-crystallisation studies.

【 授权许可】

Unknown