KEGG   ENZYME: 1.2.1.50
Entry
EC 1.2.1.50                 Enzyme                                 
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)
Reaction(IUBMB)
a long-chain aldehyde + [protein]-L-cysteine + NADP+ = a [protein]-S-(long-chain fatty acyl)-L-cysteine + NADPH + H+ [RN:R10549]
Reaction(KEGG)
R10549;
(other) R02620
Substrate
long-chain aldehyde [CPD:C00609];
[protein]-L-cysteine [CPD:C02743];
NADP+ [CPD:C00006]
Product
[protein]-S-(long-chain fatty acyl)-L-cysteine;
NADPH [CPD:C00005];
H+ [CPD:C00080]
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.
History
EC 1.2.1.50 created 1986, modified 2016
Pathway
ec00073  Cutin, suberine and wax biosynthesis
ec01110  Biosynthesis of secondary metabolites
Orthology
K03400  long-chain-fatty-acyl-CoA reductase
Genes
PLUplu2079(luxC)
PLUMA4R40_10420
PAYPAU_02514(luxC)
PTTVY86_20605
PAKHB0X70_10715
PLUICE143_10625
VHAVIBHAR_06244
VCAM892_20825
VQICCZ37_17830
VFIVF_A0923(luxC)
VFMVFMJ11_A1041
VSAVSAL_II0964(luxC)
ELUXBTN50_1880
SWDSwoo_3633
IODEJO50_06695
SPLBSFPGR_03580(luxC)
SGRFSGFS_036660
 » show all
Reference
1  [PMID:7085612]
  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
3  [PMID:8447834]
  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
Biochem Biophys Res Commun 191:314-8 (1993)
DOI:10.1006/bbrc.1993.1219
  Sequence
Other DBs
ExplorEnz - The Enzyme Database: 1.2.1.50
IUBMB Enzyme Nomenclature: 1.2.1.50
ExPASy - ENZYME nomenclature database: 1.2.1.50
BRENDA, the Enzyme Database: 1.2.1.50
CAS: 50936-56-6

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