Abstract

The reduction of acyl-CoA or acyl-ACP to fatty alcohol occurs via a fatty aldehyde intermediate. In prokaryotes this reaction is thought to be performed by separate enzymes for each reduction step while in eukaryotes these reactions are performed by a single enzyme without the release of the intermediate fatty aldehyde. However, here we report that a purified fatty acyl reductase from Marinobacter aquaeolei VT8, evolutionarily related to the fatty acyl reductases in eukaryotes, catalysed both reduction steps. Thus, there are at least two pathways existing among prokaryotes for the reduction of activated acyl substrates to fatty alcohol. The Marinobacter fatty acyl reductase studied has a wide substrate range in comparison to what can be found among enzymes so far studied in eukaryotes. (C) 2011 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

Keywords

Acyl-CoA reductase; Aldehyde reductase; Fatty alcohol; Fatty aldehyde; Marinobacter aquaeolei

Published in

FEBS Letters
2011, Volume: 585, number: 22, pages: 3538-3543
Publisher: ELSEVIER SCIENCE BV

SLU Authors

• Hofvander, Per

  • Department of Plant Breeding, Swedish University of Agricultural Sciences
    

UKÄ Subject classification

Organic Chemistry


Publication Identifiers

DOI: https://doi.org/10.1016/j.febslet.2011.10.016

Permanent link to this page (URI)

https://res.slu.se/id/publ/57202