Entry
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
Orthology
K10780 enoyl-[acyl-carrier protein] reductase III
Genes
LLG : 44548918_00264(fabL)
LJR : NCTC11533_00288(fabL)
LCJ : NCTC11976_01126(fabL) NCTC11976_02509(phaB_4)
LWA : SAMEA4504053_0677(fabL)
LSS : NCTC12082_02402(fabL)
RBS : RHODOSMS8_02171(fabL)
SUR : STAUR_4694 STAUR_7038
AGE : AA314_01964 AA314_07156
MRM : A7982_00886 A7982_02081
LCRE : Pla8534_03000(fabL_1) Pla8534_16180(fabL_2)
SMAM : Mal15_43370(fabL_1)
SNEP : Enr13x_06110(fabL_1)
KAN : IMCC3317_45070(fabL)
SPON : HME9304_03191(fabI)
CJG : NCTC13459_00416(fabL)
CANT : NCTC13489_01022(fabL)
BAZ : BAMTA208_03980(fabL)
BSON : S101395_01084(phbB)
BFD : NCTC4823_02971(fabL)
BLEN : NCTC4824_03129(fabL)
PARG : PspKH34_32790(fabL)
PUK : PU629_11165 PU629_12465(fabL) PU629_17860(fabL)
LMOC : LMOSLCC5850_1751(fabL)
LMW : LMOSLCC2755_1700(fabL)
LMX : LMOSLCC2372_1754(fabL)
LMZ : LMOSLCC2482_1752(fabL)
LMON : LMOSLCC2376_1647(fabL)
LMOS : LMOSLCC7179_1662(fabL)
LMOO : LMOSLCC2378_1709(fabL)
LMOY : LMOSLCC2479_1752(fabL)
LMOT : LMOSLCC2540_1771(fabL)
LMOA : LMOATCC19117_1703(fabL)
LGZ : NCTC10812_01163(fabL)
BAYD : BSPP4475_16895(fabL)
AAD : TC41_2687(fabG) TC41_2700(fabL)
AFX : JZ786_19250(fabL) JZ786_19315
AACO : K1I37_18445 K1I37_18565(fabL)
ADAU : NZD86_04905(fabL) NZD86_04985
AFAS : NZD89_04880(fabL) NZD89_04935
ACYC : JI721_14715 JI721_16895(fabL)
ALIC : GI364_00850 GI364_05075 GI364_12615(fabL)
SAY : TPY_3095 TPY_3240(fabL)
SAP : Sulac_0799 Sulac_1673
SLE : sle_01250(sle_01250)
AWN : NQV15_07675 NQV15_14330
KUT : JJ691_15740 JJ691_19750
» show all
Taxonomy
Reference
Authors
Heath RJ, Su N, Murphy CK, Rock CO
Title
The enoyl-[acyl-carrier-protein] reductases FabI and FabL from Bacillus subtilis.
Journal
Sequence
Reference
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
Reference
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
Other DBs
ExPASy - ENZYME nomenclature database: 1.3.1.104
LinkDB
All DBs