KEGG   ENZYME: 1.3.1.104Help
Entry
EC 1.3.1.104                Enzyme                                 

Name
enoyl-[acyl-carrier-protein] reductase (NADPH);
acyl-ACP dehydrogenase (ambiguous);
enoyl-[acyl carrier protein] (reduced nicotinamide adenine dinucleotide phosphate) reductase;
NADPH 2-enoyl Co A reductase;
enoyl-ACP reductase (ambiguous);
fabL (gene name)
Class
Oxidoreductases;
Acting on the CH-CH group of donors;
With NAD+ or NADP+ as acceptor
BRITE hierarchy
Sysname
acyl-[acyl-carrier protein]:NADP+ oxidoreductase
Reaction(IUBMB)
an acyl-[acyl-carrier protein] + NADP+ = a trans-2,3-dehydroacyl-[acyl-carrier protein] + NADPH + H+ [RN:R01404]
Reaction(KEGG)
Substrate
acyl-[acyl-carrier protein] [CPD:C00173];
NADP+ [CPD:C00006]
Product
trans-2,3-dehydroacyl-[acyl-carrier protein] [CPD:C00693];
NADPH [CPD:C00005];
H+ [CPD:C00080]
Comment
The enzyme completes each cycle of fatty acid elongation by catalysing the stereospecific reduction of the double bond at position 2 of a growing fatty acid chain, while linked to the acyl-carrier protein, in an NADPH-dependent manner. This entry stands for enzymes whose stereo-specificity with respect to NADP+ is not known. [cf. EC 1.3.1.39 enoyl-[acyl-carrier-protein] reductase (NADPH, Re-specific), EC 1.3.1.10, enoyl-[acyl-carrier-protein] reductase (NADPH, Si-specific) and EC 1.3.1.9, enoyl-[acyl-carrier-protein] reductase (NADH)].
History
EC 1.3.1.104 created 2013
Pathway
Fatty acid biosynthesis
Metabolic pathways
Orthology
K10780  
enoyl-[acyl-carrier protein] reductase III
Genes
SMAF: 
SFW: 
LPH: 
LPO: 
LPU: 
LPM: 
LP6_0350(fabL)
LPA: 
LPE: 
LLO: 
LFA: 
LFA_2780(fabL)
LHA: 
LHA_0370(fabL)
LOK: 
TMC: 
LMI_0465(fabL)
DPR: 
SUR: 
AGE: 
BSU: 
BSU08650(fabL)
BSR: 
BSL: 
BSH: 
BSY: 
BSUT: 
BSUL: 
BSUS: 
BSS: 
BST: 
BSO: 
BSN: 
BSQ: 
BSX: 
C663_0887(fabL)
BSP: 
BLI: 
BL03039(fabL)
BLD: 
BLi00887(fabL)
BLH: 
BAY: 
BAQ: 
BYA: 
BAMP: 
BAML: 
BAMA: 
RBAU_0847(fabL)
BAMN: 
BASU_0823(fabL)
BAMB: 
BAMT: 
BAMY: 
BMP: 
BAO: 
BAMF_0873(fabL)
BAZ: 
BQL: 
LL3_00935(fabL)
BXH: 
BQY: 
MUS_0887(fabL)
BAMI: 
BAMC: 
BAMF: 
BAE: 
BATR: 
BHA: 
BCL: 
ABC1313(fabL)
BPU: 
BPUM_0812(fabL)
BPUM: 
BPF: 
BMQ: 
BMD: 
BMH: 
BMEG: 
BG04_2695(fabL)
BCO: 
BCK: 
BAG: 
BCOA: 
BF29_1474(fabL)
BJS: 
BACI: 
BIF: 
BLE: 
BMET: 
GST: 
BACW: 
BACP: 
BACB: 
BACY: 
BACL: 
BALM: 
BEO: 
BSM: 
BSJ: 
GKA: 
GTN: 
GTNG_0470(fabI)
GTH: 
GTE: 
GWC: 
GYC: 
GYA: 
GCT: 
GMC: 
GGH: 
GJF: 
GEA: 
GEL: 
GSE: 
LMO: 
LMF: 
LMH: 
LMN: 
LMY: 
LMT: 
LMG: 
LMS: 
LMJ: 
LMQ: 
LMM7_1777(fabL)
LML: 
LMP: 
LMW: 
LMX: 
LMZ: 
LMON: 
LMOC: 
LMOS: 
LMOO: 
LMOY: 
LMOT: 
LMOA: 
LMOL: 
LMOG: 
LMOE: 
LMOB: 
LMOJ: 
LMOZ: 
LMOD: 
LMOW: 
LMOX: 
LMOQ: 
LMR: 
LMOK: 
LMV: 
LMOM: 
LIN: 
LWE: 
LSG: 
LIV: 
LII: 
LIW: 
LIA: 
LIO: 
BBE: 
BLR: 
PBJ: 
AAC: 
AAD: 
TC41_2687(fabG) TC41_2700(fabL)
BTS: 
PLN: 
PKU: 
PRT: 
JEO: 
SAY: 
TPY_3240(fabL)
SAP: 
LPIL: 
NBR: 
ROA: 
SFA: 
STRP: 
PDX: 
KAL: 
AFO: 
NON: 
ATM: 
CAP: 
TTR: 
PLM: 
CPH: 
 » show all
Taxonomy
Reference
1  [PMID:11007778]
  Authors
Heath RJ, Su N, Murphy CK, Rock CO
  Title
The enoyl-[acyl-carrier-protein] reductases FabI and FabL from Bacillus subtilis.
  Journal
J. Biol. Chem. 275 (2000) 40128-33.
  Sequence
[bsu:BSU08650]
Reference
2  [PMID:17329825]
  Authors
Kim KH, Park JK, Ha BH, Moon JH, Kim EE
  Title
Crystallization and preliminary X-ray crystallographic analysis of enoyl-ACP reductase III (FabL) from Bacillus subtilis.
  Journal
Acta. Crystallogr. Sect. F. Struct. Biol. Cryst. Commun. 63 (2007) 246-8.
Reference
3  [PMID:21185310]
  Authors
Kim KH, Ha BH, Kim SJ, Hong SK, Hwang KY, Kim EE
  Title
Crystal structures of Enoyl-ACP reductases I (FabI) and III (FabL) from B. subtilis.
  Journal
J. Mol. Biol. 406 (2011) 403-15.
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 

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