Characterization of a structurally and functionally diverged acyl-acyl carrier protein desaturase from milkweed seed

被引：38

作者：

Cahoon, EB ^{[1
]}

Coughlan, SJ ^{[1
]}

Shanklin, J ^{[1
]}

机构：

[1] PIONEER HI BRED INT INC,DEPT BIOTECHNOL RES,JOHNSTON,IA 50131

来源：

PLANT MOLECULAR BIOLOGY | 1997年 / 33卷 / 06期

关键词：

fatty acid desaturase; Asclepias syriaca;

D O I：

10.1023/A:1005821007291

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：

A cDNA for a structurally variant acyl-acyl carrier protein (ACP) desaturase was isolated from milkweed (Asclepias syriaca) seed, a tissue enriched in palmitoleic (16:1 Delta(9))* and cis-vaccenic (18:1 Delta(11)) acids. Extracts of Escherichia coli that express the milkweed cDNA catalyzed Delta(9) desaturation of acyl-ACP substrates, and the recombinant enzyme exhibited seven- to ten-fold greater specificity for palmitoyl (16:0)-ACP and 30-fold greater specificity for myristoyl (14:0)-ACP than did known Delta(9)-stearoyl (18:0)-ACP desaturases. Like other variant acyl-ACP desaturases reported to date, the milkweed enzyme contains fewer amino acids near its N-terminus compared to previously characterized Delta(9)-18:0-ACP desaturases. Based on the activity of an N-terminal deletion mutant of a Delta(9)-18:0-ACP desaturase, this structural feature likely does not account for differences in substrate specificities.

引用

页码：1105 / 1110

页数：6

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