Entry |
|
Name |
long-chain acyl-protein thioester reductase;
luxC (gene name);
acyl-CoA reductase;
acyl coenzyme A reductase;
long-chain-aldehyde:NADP+ oxidoreductase (acyl-CoA-forming);
long-chain-fatty-acyl-CoA reductase
|
Class |
Oxidoreductases;
Acting on the aldehyde or oxo group of donors;
With NAD+ or NADP+ as acceptor
 |
Sysname |
long-chain-aldehyde:NADP+ oxidoreductase (protein thioester-forming)
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Reaction(IUBMB) |
a long-chain aldehyde + [protein]-L-cysteine + NADP+ = a [protein]-S-(long-chain fatty acyl)-L-cysteine + NADPH + H+ [RN: R10549]
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Reaction(KEGG) |
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Substrate |
|
Product |
[protein]-S-(long-chain fatty acyl)-L-cysteine;
NADPH [CPD: C00005];
H+ [CPD: C00080]
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Comment |
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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History |
EC 1.2.1.50 created 1986, modified 2016
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Pathway |
ec00073 | Cutin, suberine and wax biosynthesis |
ec01110 | Biosynthesis of secondary metabolites |
|
Orthology |
K03400 | long-chain-fatty-acyl-CoA reductase |
|
Genes |
» show all
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Reference |
|
Authors |
Riendeau D, Rodriguez A, Meighen E. |
Title |
Resolution of the fatty acid reductase from Photobacterium phosphoreum into acyl protein synthetase and acyl-CoA reductase activities. Evidence for an enzyme complex. |
Journal |
J Biol Chem 257:6908-15 (1982) |
Reference |
2 |
Authors |
Wall, L. and Meighen, E.A. |
Title |
Subunit structure of the fatty-acid reductase complex from Photobacterium phosphoreum. |
Journal |
Biochemistry 25:4315-4321 (1986) |
Reference |
|
Authors |
Lin JW, Chao YF, Weng SF |
Title |
Nucleotide sequence of the luxC gene encoding fatty acid reductase of the lux operon from Photobacterium leiognathi. |
Journal |
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Other DBs |
ExplorEnz - The Enzyme Database: | 1.2.1.50 |
ExPASy - ENZYME nomenclature database: | 1.2.1.50 |
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