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

Characterization of a structurally and functionally diverged acyl-acyl carrier protein desaturase... A cDNA for a structurally variant acyl-acyl carrier protein (ACP) desaturase was isolated from milkweed (Asclepias syriaca) seed, a tissue enriched in palmitoleic (16:1Δ9)* and cis-vaccenic (18:1Δ11) acids. Extracts of Escherichia coli that express the milkweed cDNA catalyzed Δ9 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 Δ9-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 Δ9-18:0-ACP desaturases. Based on the activity of an N-terminal deletion mutant of aΔ9 -18:0-ACP desaturase, this structural feature likely does not account for differences in substrate specificities. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Plant Molecular Biology Springer Journals

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

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Publisher
Kluwer Academic Publishers
Copyright
Copyright © 1997 by Kluwer Academic Publishers
Subject
Life Sciences; Biochemistry, general; Plant Sciences; Plant Pathology
ISSN
0167-4412
eISSN
1573-5028
D.O.I.
10.1023/A:1005821007291
Publisher site
See Article on Publisher Site

Abstract

A cDNA for a structurally variant acyl-acyl carrier protein (ACP) desaturase was isolated from milkweed (Asclepias syriaca) seed, a tissue enriched in palmitoleic (16:1Δ9)* and cis-vaccenic (18:1Δ11) acids. Extracts of Escherichia coli that express the milkweed cDNA catalyzed Δ9 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 Δ9-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 Δ9-18:0-ACP desaturases. Based on the activity of an N-terminal deletion mutant of aΔ9 -18:0-ACP desaturase, this structural feature likely does not account for differences in substrate specificities.

Journal

Plant Molecular BiologySpringer Journals

Published: Oct 14, 2004

References

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