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Information on EC 1.2.1.50 - long-chain acyl-protein thioester reductase and Organism(s) Homo sapiens and UniProt Accession Q8WVX9

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EC Tree
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.
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Homo sapiens
UNIPROT: Q8WVX9
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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
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
acyl coenzyme A reductase
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acyl-CoA reductase
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long-chain-fatty-acyl-CoA reductase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
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oxidation
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reduction
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SYSTEMATIC NAME
IUBMB Comments
long-chain-aldehyde:NADP+ oxidoreductase (protein thioesther-forming)
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.
CAS REGISTRY NUMBER
COMMENTARY hide
50936-56-6
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75718-33-1
complex of three enzymes