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

Loading next page...
 
/lp/springer_journal/characterization-of-a-structurally-and-functionally-diverged-acyl-acyl-t7kcdHlPwh
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

You’re reading a free preview. Subscribe to read the entire article.


DeepDyve is your
personal research library

It’s your single place to instantly
discover and read the research
that matters to you.

Enjoy affordable access to
over 12 million articles from more than
10,000 peer-reviewed journals.

All for just $49/month

Explore the DeepDyve Library

Unlimited reading

Read as many articles as you need. Full articles with original layout, charts and figures. Read online, from anywhere.

Stay up to date

Keep up with your field with Personalized Recommendations and Follow Journals to get automatic updates.

Organize your research

It’s easy to organize your research with our built-in tools.

Your journals are on DeepDyve

Read from thousands of the leading scholarly journals from SpringerNature, Elsevier, Wiley-Blackwell, Oxford University Press and more.

All the latest content is available, no embargo periods.

See the journals in your area

DeepDyve Freelancer

DeepDyve Pro

Price
FREE
$49/month

$360/year
Save searches from Google Scholar, PubMed
Create lists to organize your research
Export lists, citations
Read DeepDyve articles
Abstract access only
Unlimited access to over
18 million full-text articles
Print
20 pages/month
PDF Discount
20% off