Jump to main content
Jump to site search

Issue 8, 2007
Previous Article Next Article

Stereochemistry of Δ4 dehydrogenation catalyzed by an ivy (Hedera helix) Δ9 desaturase homolog

Author affiliations

Abstract

The stereochemistry of palmitoyl-ACP Δ4 desaturase-mediated dehydrogenation has been examined by tracking the fate of deuterium atoms located on stereospecifically monodeuterated substrates-(4S)- and (4R)-[4-2H1]-palmitoyl-ACP and (5S)- and (5R)-[5-2H1]-palmitoyl-ACP. It was found that the introduction of the (Z)-double bond between C-4 and C-5 of a palmitoyl substrate occurs with pro-R enantioselectivity—a result which matches that obtained for a closely related homolog-castor stearoyl-ACP Δ9 desaturase. These data show that despite the difference in regioselectivity between the two enzymes, the stereochemistry of hydrogen removal is conserved.

Graphical abstract: Stereochemistry of Δ4 dehydrogenation catalyzed by an ivy (Hedera helix) Δ9 desaturase homolog

Back to tab navigation

Publication details

The article was received on 13 Dec 2006, accepted on 06 Mar 2007 and first published on 19 Mar 2007


Article type: Paper
DOI: 10.1039/B617942H
Citation: Org. Biomol. Chem., 2007,5, 1270-1275
  •   Request permissions

    Stereochemistry of Δ4 dehydrogenation catalyzed by an ivy (Hedera helix) Δ9 desaturase homolog

    A. E. Tremblay, E. Whittle, P. H. Buist and J. Shanklin, Org. Biomol. Chem., 2007, 5, 1270
    DOI: 10.1039/B617942H

Search articles by author

Spotlight

Advertisements