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Information on EC 1.2.1.50 - long-chain acyl-protein thioester reductase

for references in articles please use BRENDA:EC1.2.1.50

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IUBMB Comments

Together with a hydrolase component (EC 3.1.2.2 and EC 3.1.2.14) and a synthetase component (EC 6.2.1.19), this enzyme forms a multienzyme fatty acid reductase complex that produces the long-chain aldehyde substrate of the bacterial luciferase enzyme (EC 1.14.14.3). The enzyme is acylated by receiving an acyl group from EC 6.2.1.19, and catalyses the reduction of the acyl group, releasing the aldehyde product. The enzyme is also able to accept the acyl group from a long-chain acyl-CoA.

The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea

Synonyms
acyl-coa reductase, fatty acyl-coa reductase 1, amfar1, acyl coenzyme a reductase, fatty acyl-coa reductase 2, fatty acyl-coa reductase 6, more

REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
a long-chain aldehyde + [protein]-L-cysteine + NADP+ = a [protein]-S-(long-chain fatty acyl)-L-cysteine + NADPH + H+
show the reaction diagram
together with EC 6.2.1.19 forms a fatty acid reductase system which produces the substrate of EC 1.14.14.3, thus being a part of the bacterial luciferase system
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PATHWAY SOURCE
PATHWAYS
MetaCyc
bacterial bioluminescence
Highest Expressing Human Cell Lines
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