KEGG ENZYME: 1.2.1.50

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

PLU:	plu2079(luxC)

PLUM:

A4R40_10420

PAY:	PAU_02514(luxC)

PTT:	VY86_20605

VHA:	VIBHAR_06244

VCA:	M892_20825

VQI:	CCZ37_17830

VFI:	VF_A0923(luxC)

VFM:	VFMJ11_A1041

VSA:	VSAL_II0964(luxC)

SWD:

Swoo_3633

IOD:	EJO50_06695

UPI:	EJG51_013270

SPLB:

SFPGR_03580(luxC)

» 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

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