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A prokaryotic acyl‐CoA reductase performing reduction of fatty acyl‐CoA to fatty alcohol
Author(s) -
Hofvander Per,
Doan Thuy T.P.,
Hamberg Mats
Publication year - 2011
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2011.10.016
Subject(s) - reductase , biochemistry , fatty alcohol , acyl coa , enzyme , aldehyde , fatty acid , acyl group , acyl carrier protein , chemistry , alcohol , substrate (aquarium) , stereochemistry , biology , biosynthesis , organic chemistry , catalysis , ecology , alkyl
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.