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

Edgar B. Cahoon, Sean J. Coughlan, John Shanklin

Research output: Contribution to journalArticle

32 Scopus citations

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 substances, 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 a Δ9-18:0-ACP desaturase, this structural feature likely does not account for differences in substrate specificities.

Original languageEnglish (US)
Pages (from-to)1105-1110
Number of pages6
JournalPlant Molecular Biology
Volume33
Issue number6
DOIs
StatePublished - Apr 1997

Keywords

  • Asclepias syriaca
  • fatty acid desaturase

ASJC Scopus subject areas

  • Agronomy and Crop Science
  • Genetics
  • Plant Science

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