A prokaryotic acyl-CoA reductase performing reduction of fatty acyl-CoA to fatty alcohol.
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.
Department of Plant Breeding and Biotechnology, Swedish University of Agricultural Sciences, Alnarp, Sweden. per.hofvander@slu.se
Per
P
Hofvander
Thuy T P
TT
Doan
Mats
M
Hamberg
D000214:Acyl Coenzyme A / Q000378:metabolism*; D000445:Aldehyde Oxidoreductases / Q000737:chemistry / Q000378:metabolism*; D001426:Bacterial Proteins / Q000737:chemistry / Q000378:metabolism*; D005233:Fatty Alcohols / Q000378:metabolism*; D053520:Marinobacter / Q000201:enzymology* / Q000378:metabolism; D010084:Oxidation-Reduction; D010802:Phylogeny
D000214:Acyl Coenzyme A; D001426:Bacterial Proteins; D005233:Fatty Alcohols; D000445:Aldehyde Oxidoreductases; C021351:hexadecanal dehydrogenase (acylating)