Substrate specificity of Arabidopsis 3-ketoacyl-CoA synthases

被引：125

作者：

Blacklock, Brenda J. ^{[1
]}

Jaworski, Jan G.

机构：

[1] Indiana Univ Purdue Univ, Purdue Sch Sci, Dept Chem & Chem Biol, Indianapolis, IN 46202 USA

[2] Donald Danforth Plant Sci Ctr, St Louis, MO 63132 USA

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2006年 / 346卷 / 02期

关键词：

arabidopsis; 3-ketoacyl-CoA synthase; fatty acid elongation; condensing enzyme;

D O I：

10.1016/j.bbrc.2006.05.162

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The very long chain fatty acids (VLCFA) incorporated into plant lipids are derived from the iterative addition of C2 units provided by malonyl-CoA to an acyl-CoA by the 3-ketoacyl-CoA synthase (KCS) component of a fatty acid elongase (FAE) complex. Mining of the Arabidopsis genome sequence database revealed 20 genes with homology to seed-specific FAD KCS. Eight of the 20 putative KCSs were cloned. expressed in yeast, and isolated as (His)(6) fusion proteins. Five of the eight (At1g71160, At1g19440, At1g07720, At5g04530, and At4g34250) had little or no activity with C16 to C20 substrates while three demonstrated activity with C16, C18, and C20 saturated acyl-CoA substrates. At1g01120 KCS (KCS1) and At2g26640 KCS had broad substrate specificities when assayed with saturated and monounsaturated C16 to C24 acyl-CoAs while At4g34510 KCS was specific for saturated fatty acyl-CoA substrates. (c) 2006 Elsevier Inc. All rights reserved.

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页码：583 / 590

页数：8

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