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Substrate specificity of Arabidopsis 3-ketoacyl-CoA synthases.

Abstract：

: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 FAE1 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 mono-unsaturated C16 to C24 acyl-CoAs while At4g34510 KCS was specific for saturated fatty acyl-CoA substrates.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Blacklock BJ,Jaworski JG

doi

10.1016/j.bbrc.2006.05.162

subject

Has Abstract

pub_date

2006-07-28 00:00:00

pages

583-90

issue

2

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(06)01241-1

journal_volume

346

pub_type

杂志文章

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