Information on EC 1.3.1.10 - enoyl-[acyl-carrier-protein] reductase (NADPH, Si-specific)

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

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EC NUMBER
COMMENTARY hide
1.3.1.10
-
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RECOMMENDED NAME
GeneOntology No.
enoyl-[acyl-carrier-protein] reductase (NADPH, Si-specific)
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
an acyl-[acyl-carrier protein] + NADP+ = a trans-2,3-dehydroacyl-[acyl-carrier protein] + NADPH + H+
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
palmitate biosynthesis I (animals and fungi)
-
-
stearate biosynthesis III (fungi)
-
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octanoyl-[acyl-carrier protein] biosynthesis (mitochondria, yeast)
-
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fatty acid elongation -- saturated
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lipid metabolism
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Fatty acid biosynthesis
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Biotin metabolism
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Metabolic pathways
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SYSTEMATIC NAME
IUBMB Comments
acyl-[acyl-carrier protein]:NADP+ oxidoreductase (Si-specific)
One of the activities of EC 2.3.1.86, fatty-acyl-CoA synthase, an enzyme found in yeasts (Ascomycota and the Basidiomycota). Catalyses the reduction of enoyl-acyl-[acyl-carrier protein] derivatives of carbon chain length from 4 to 16. The yeast enzyme is Si-specific with respect to NADP+. cf. EC 1.3.1.39, enoyl-[acyl-carrier-protein] reductase (NADPH, Re-specific) and EC 1.3.1.104, enoyl-[acyl-carrier-protein] reductase (NADPH), which describes enzymes whose stereo-specificity towards NADPH is not known. See also EC 1.3.1.9, enoyl-[acyl-carrier-protein] reductase (NADH).
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CAS REGISTRY NUMBER
COMMENTARY hide
37251-09-5
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37251-09-5
not distinguished from EC 1.3.1.39
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SwissProt
Manually annotated by BRENDA team
strain 168
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Manually annotated by BRENDA team
enzyme Etr1p
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Manually annotated by BRENDA team
safflower, enoyl-ACP reductase II, as there is no information concerning the stereochemistry of hydrogen transfer from NADPH to substrate an appointment to EC 1.3.1.10 or EC 1.3.1.39 is impossible
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Manually annotated by BRENDA team
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(2E)-but-2-enoyl-[acyl carrier protein] + NADPH + H+
butanoyl-[acyl-carrier protein] + NADP+
show the reaction diagram
1-cyclohexenylcarbonyl-CoA + NADPH
1-cyclohexylcarbonyl-CoA + NADP+
show the reaction diagram
-
reaction in ansatrienin biosynthesis out of shikimic acid
-
?
2-decenoyl-[acyl-carrier protein] + NADPH
decanoyl-[acyl-carrier protein] + NADP+
show the reaction diagram
-
syn addition of hydrogen via a 2-Re,3-Si attack on the double bond
-
?
2-hexenoyl-[acyl-carrier protein] + NADPH
hexanoyl-[acyl-carrier protein] + NADP+
show the reaction diagram
2-trans-hexenoyl-CoA + NADPH
?
show the reaction diagram
-
assay at pH 7.5, 23°C
-
-
?
5-hydroxycyclohex-1-enecarbonyl-CoA + NADPH
5-hydroxycyclohexylcarbonyl-CoA + NADP+
show the reaction diagram
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reaction in ansatrienin biosynthesis out of shikimic acid
-
?
acyl-[acyl-carrier protein] + NADP+
trans-2,3-dehydroacyl-[acyl-carrier protein] + NADPH + H+
show the reaction diagram
an acyl-[acyl-carrier protein] + NADP+
a trans-2,3-dehydroacyl-[acyl-carrier protein] + NADPH + H+
show the reaction diagram
beta-ketoacyl-[acyl-carrier protein] + NADH + H+
beta-hydroxyacyl-[acyl-carrier protein] + NAD+
show the reaction diagram
-
-
-
-
?
crotonyl-CoA + NADPH + H+
?
show the reaction diagram
crotonyl-N-acetyl-cysteamine + NADPH
butyryl-N-acetyl-cysteamine + NADP+
show the reaction diagram
crotonyl-N-acetyl-cysteamine + NADPH + H+
butyryl-N-acetyl-cysteamine + NADP+
show the reaction diagram
-
-
-
-
?
crotonyl-[acyl-carrier protein] + NADPH
butyryl-[acyl-carrier protein] + NADP+
show the reaction diagram
crotonyl-[acyl-carrier protein] + NADPH + H+
?
show the reaction diagram
crotonyl-[acyl-carrier protein] + NADPH + H+
butyryl-[acyl-carrier protein] + NADP+
show the reaction diagram
crotonyl-[Staphylococcus aureus acyl carrier protein] + NADPH + H+
butyryl-[Staphylococcus aureus acyl carrier protein] + NADP+
show the reaction diagram
-
-
-
-
?
dodecenoyl-CoA + NADPH + H+
dodecanoyl-CoA + NADP+
show the reaction diagram
-
-
-
-
?
dodecenoyl-N-acetyl-cysteamine + NADPH + H+
dodecanoyl-N-acetyl-cysteamine + NADP+
show the reaction diagram
-
-
-
-
?
dodecenoyl-[Staphylococcus aureus acyl carrier protein] + NADPH + H+
dodecanoyl-[Staphylococcus aureus acyl carrier protein] + NADP+
show the reaction diagram
-
-
-
-
?
hexanoyl-CoA + NADH + H+
?
show the reaction diagram
-
-
-
-
?
hexanoyl-[acyl-carrier protein] + NADH + H+
?
show the reaction diagram
-
-
-
-
?
octenoyl-N-acetyl-cysteamine + NADPH
octanoyl-N-acetyl-cysteamine + NADP+
show the reaction diagram
S-((2E)-oct-2-enoyl)-N-acetylcysteamine + NADPH + H+
S-octanoyl-N-acetylcysteamine + NADP+
show the reaction diagram
trans-2,3-dehydroacyl-[acyl-carrier protein] + NADPH
acyl-[acyl-carrier protein] + NADP+
show the reaction diagram
trans-2,3-dehydroacyl-[acyl-carrier protein] + NADPH + H+
acyl-[acyl-carrier protein] + NADP+
show the reaction diagram
-
prefers acyl carrier protein substrates carrying fatty acids with long acyl chains
-
-
?
trans-2-hexenoyl-CoA + NADPH
hexanoyl-CoA + NADP+
show the reaction diagram
-
-
-
-
?
trans-3,4-dihydroxycyclohexa-1,5-dienecarbonyl-CoA + NADPH
trans-4,5-dihydroxycyclohexa-2-enecarbonyl-CoA + NADP+
show the reaction diagram
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reaction in ansatrienin biosynthesis out of shikimic acid
-
?
additional information
?
-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
1-cyclohexenylcarbonyl-CoA + NADPH
1-cyclohexylcarbonyl-CoA + NADP+
show the reaction diagram
-
reaction in ansatrienin biosynthesis out of shikimic acid
-
?
5-hydroxycyclohex-1-enecarbonyl-CoA + NADPH
5-hydroxycyclohexylcarbonyl-CoA + NADP+
show the reaction diagram
-
reaction in ansatrienin biosynthesis out of shikimic acid
-
?
an acyl-[acyl-carrier protein] + NADP+
a trans-2,3-dehydroacyl-[acyl-carrier protein] + NADPH + H+
show the reaction diagram
beta-ketoacyl-[acyl-carrier protein] + NADH + H+
beta-hydroxyacyl-[acyl-carrier protein] + NAD+
show the reaction diagram
-
-
-
-
?
trans-2,3-dehydroacyl-[acyl-carrier protein] + NADPH
acyl-[acyl-carrier protein] + NADP+
show the reaction diagram
trans-3,4-dihydroxycyclohexa-1,5-dienecarbonyl-CoA + NADPH
trans-4,5-dihydroxycyclohexa-2-enecarbonyl-CoA + NADP+
show the reaction diagram
-
reaction in ansatrienin biosynthesis out of shikimic acid
-
?
additional information
?
-
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
FAD
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enzyme contains 0.8 mol FAD/enzyme, but functional role is not investigated
NADP+
additional information
-
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(E)-N-(1,2-dimethyl-1-H-indol-3-ylmethyl)-N-methyl-3-(7-oxo-5,6,7,8-tetrahydro-1,8-naphthyridin-3-yl) acrylamide
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5-chloro-2-phenoxyphenol
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5-ethyl-2-phenoxyphenol
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6-methyl-2-(propane-1-sulfonyl)-4a,7a-dihydro-2H-thieno[3,2-d][1,2,3]diazaborinin-1-ol
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diazaborine derivative 2b18, binds only in presence of NADH or NADPH, non-competitive inhibition, 0.2 mM lead to 25% inhibition, 0.52 mM to 50%, 1.56 mM to 80%. Increasing the inhibitor concentrations lead to preference for shorter acyl chain lengths
aquastatin A
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a natural inhibitor from the fungus Sporothrix sp. strain FN611, mixed-type inhibition against FabI with respect to the substrate trans-2-octenoyl N-acetylcysteamine and NADPH, prevents the growth of Staphylococcus aureus and methicillin-resistant Staphylococcus aureus with minimum inhibitory concentration of 0.016-0.032 mg/ml, overview
degalactosylated aquastatin A
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a natural inhibitor from the fungus Sporothrix sp. strain FN611
Hexachlorophene
half-maximal inhibition at 0.004 mM
iodoacetate
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N-ethylmaleimide
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p-hydroxymercuribenzoate
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palmitoyl-CoA
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0.0016 mM lead to 50% inhibition, 0.002 mM to 60%, 0.005 mM to 20%, 0.01 mM to nearly total inhibition
triclosan
additional information
-
not inhibited by: triclosan
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NH4Cl
required for stability and activity. Assay in presence of 0.1 M NH4Cl
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.025
1-cyclohexenylcarbonyl-CoA
-
vmax 0.0075 mmol/mg/min
0.03
5-hydroxycyclohex-1-enecarbonyl-CoA
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vmax 0.0053 mmol/mg/min
0.008 - 8
Crotonyl-N-acetyl-cysteamine
0.0478
crotonyl-[acyl-carrier protein]
pH 7.5, 25°C
0.0115
crotonyl-[Staphylococcus aureus acyl carrier protein]
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wild type enzyme, at 25°C, in 100 mM Na2HPO4 buffer (pH 7.8)
0.0241
dodec-2-enoyl-CoA
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wild type enzyme, at 25°C, in 100 mM Na2HPO4 buffer (pH 7.8)
0.0233
dodecenoyl-N-acetyl-cysteamine
-
wild type enzyme, at 25°C, in 100 mM Na2HPO4 buffer (pH 7.8)
0.0045 - 0.0184
dodecenoyl-[Staphylococcus aureus acyl carrier protein]
0.016 - 1
NADPH
additional information
NADPH
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.5
Crotonyl-N-acetyl-cysteamine
-
wild type enzyme, at 25°C, in 100 mM Na2HPO4 buffer (pH 7.8)
0.038 - 0.51
crotonyl-[acyl-carrier protein]
11.6
crotonyl-[Staphylococcus aureus acyl carrier protein]
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wild type enzyme, at 25°C, in 100 mM Na2HPO4 buffer (pH 7.8)
18
dodec-2-enoyl-CoA
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wild type enzyme, at 25°C, in 100 mM Na2HPO4 buffer (pH 7.8)
30.4
dodecenoyl-N-acetyl-cysteamine
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wild type enzyme, at 25°C, in 100 mM Na2HPO4 buffer (pH 7.8)
18.4 - 157.3
dodecenoyl-[Staphylococcus aureus acyl carrier protein]
130.2
NADPH
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wild type enzyme, at 25°C, in 100 mM Na2HPO4 buffer (pH 7.8)
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00006
(E)-N-(1,2-dimethyl-1-H-indol-3-ylmethyl)-N-methyl-3-(7-oxo-5,6,7,8-tetrahydro-1,8-naphthyridin-3-yl) acrylamide
pH 7.0, 30°C
-
0.000004 - 0.000069
AFN-1252
0.0014 - 0.00161
aquastatin A
0.109
NADPH
pH 7.5, 25°C
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0032
aquastatin A
Staphylococcus aureus
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FabI, pH 6.5, 30°C
0.0034
degalactosylated aquastatin A
Staphylococcus aureus
-
FabI, pH 6.5, 30°C
0.016
triclosan
Bacillus subtilis
P71079
-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.008
-
crude cell extract
0.18
spectrophotometric assay, S-((2E)-oct-2-enoyl)-N-acetylcysteamine as a substrate; with octenyl-N-acetyl-cysteamine
0.2
-
purified recombinant mutant Y79N
0.3
spectrophotometric assay, (2E)-but-2-enoyl-[acyl carrier protein] as a substrate; with crotonyl-[acyl-carrier-protein]
0.4
-
purified by chromatography on DEAE-cellulose and Blue sepharose
0.882
-
crude Escherichia coli cell extract after overexpression
3.667
-
purified, overexpressed enzyme
20
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purified recombinant wild-type enzyme
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5
-
assay at
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
29700
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ChcA, gene sequence
30000
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SDS-PAGE
33000
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FabI, SDS-PAGE
33090
x * 33090, calculated
34000
-
FabK, gene sequence
37000
-
ChcA, SDS-PAGE, +/-2000
75000
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ChcA, gel filtration on superose 12, +/-10000
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
FabL in apo form and in the ternary complex with NADP+ and an indole naphthyridinone inhibitor, X-ray diffraction structure determination and analysis; FabL in apo form and in the ternary complex with NADP+ and inhibitor (E)-N-(1,2-dimethyl-1-H-indol-3-ylmethyl)-N-methyl-3-(7-oxo-5,6,7,8-tetrahydro-1,8-naphthyridin-3-yl) acrylamide, 8 mg/ml protein in 20 mM Tris, pH 8.0, 100 mM NaCl, and 1 mM DTT, is mixed with an equal volume of reservoir solution containing 0.1 M sodium citrate pH 5.6, 8% w/v PEG 10,000 and 0.4 M magnesium acetate, hanging-drop methods, for the ternary BcFabL-NADP+-INH complex, NADP+ and inhibitor are added at the molar ratio of 1:1.5 and 1:5, respectively, equilibration in a stabilizing solution containing 0.1 M sodium citrate, pH 5.6, 8% w/v PEG 10,000, 0.4 M magnesium acetate with 30% v/v ethylene glycol as the cryoprotectant, X-ray diffraction structure determination and analysis at 2.2-3.0 A resolution
hanging drop vapour diffusion method with 0.04 M MgCl2, 0.05 M sodium cacodylate pH 6.0 and 11% (v/v) 2-methyl-2,4-pentanediol at 4°C
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purified recombinant wild-type enzyme free and in complex with NADPH, mutant enzyme Y79N, hanging drop vapour diffusion method, 22°C, 15-25 mg/ml free enzyme in 50 mM sodium phosphate, pH 7.0, 150 mM NaCl with or without 10 mM NADPH, in a 1:1 ratio with reservoir solution containing 1.9 M ammonium sulfate, and 0.1 M N-(2-acetamido)-2-iminodiacetic acid/NaOH, at pH 6.5 for the free enzyme and pH 7.0 for the cofactor-complexed enzyme, mutant Y79N is crystallized using 15 mg/ml protein and reservoir solution at pH 7.0, labeling by soaking in heavy-atom-solutions, X-ray diffraction structure determination and analysis at 1.7 A, 2.25 A, and 2.6 A, respectively
-
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.6
-
unstable at
390499, 390500
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
55
-
5 min stable
60
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5 min, inactivation
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
enzyme can be concentrated to 20 mg/ml without precipitation
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimethyl sulfoxide
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 10 mM phosphate buffer, pH 6.5, 5 mM 2-mercaptoethanol, inactivation in 2-3 months
-
-20°C, 30% glycerol, no significant loss of activity for at least 1 month
-20°C, rapidly inactivated
-
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
chromatography of protein overexpressed in Escherichia coli by using Sephadex G-100, DEAE, Mono-Q HR 5/5
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in BisTris puffer pH 6.5 in order to retain NADPH dependent activity which is lost at pH 7.5
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Ni-NTA column chromatography and Superdex 200 gel filtration
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Ni2+ affinity chromatography on his-tagged protein
Ni2+ affinity chromatography on his-tagged protein; Ni2+ chelation chromatography
Ni2+-NTA resin chromatography
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nickel-chelated Hi-Trap column chromatography, Hi-Trap Blue HP column chromatography, Q-Sepharose column chromatography, and Superdex-75 gel filtration
-
no separation from NADH specific enzyme
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no separation from NADH specific enzyme; sonification and chromatography using DEAE-Cellulose, Sephadex G-100, Hydroxylapatite
-
recombinant His6-tagged BcFabL from Escherichia coli strain BL21(DE3) by nickel affinity and adsorption chromatography and gel filtration
recombinant protein
recombinant wild-type enzyme and mutant Y73N from mutant strain BJ1991 mrf1DELTA
recombinant wild-type enzyme and mutant Y79N from Saccharomyces cerevisiae mutant strain BJ1991 mrf1DELTA
-
which also catalyzes the reduction of enoyl-CoA substrates
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
BcFabL from strain 6A5 is expressed in Escherichia coli strain BL21(DE3) as His6-tagged protein
chcA in pUC18 and pET3C
-
envM in bacteriophage P1
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expressed in Escherichia coli BL21(DE3) cells
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expressed in Escherichia coli BL21(DE3)pLysS cells
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expressed in Escherichia coli JP1111 cells
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expression in Escherichia coli
expression in Escherichia coli; fabL in pET15b for his-tagged overexpression
fabI in pUC118
-
fabI of strain RN4220 found by homology and cloned into pET15b for his-tagged overexpression
fabK in expression plasmid
-
overexpression of wild-type enzyme and mutant Y73N in enzyme-deficient mutant strain BJ1991 mrf1DELTA, using the catalase 1 promotor
overexpression of wild-type enzyme and mutant Y79N in enzyme-deficient Saccharomyces cerevisiae mutant strain BJ1991 mrf1DELTA, using the catalase 1 promotor
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
transcription factor Adr1p influences transcription levels of ETR1 promoter, which controls the expression of 2-trans-enoyl-ACP reductase
-
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Y79N
-
site-directed mutagenesis, mutant shows native fold, but only 0.1% of the wild-type enzyme activity, no rescue of the enzyme-deficient mutant strain mrf1DELTA
G93S
-
leads to diazaborine resistance
G93V
-
leads to triclosan resistance
S241F
-
leads to temperature sensitive growth and abolished activity
Y73N
site-directed mutagenesis, mutant shows native fold, but only residual wild-type enzyme activity, no rescue of the enzyme-deficient mutant strain mrf1DELTA
A95V
-
the mutant correlates with resistance to diphenyl ethers and causes a significant reduction in the affinity of the inhibitors for the enzyme
F204S
-
inactive, the mutant correlates with resistance to diphenyl ethers and causes a significant reduction in the affinity of the inhibitors for the enzyme
I193S
-
the mutant correlates with resistance to diphenyl ethers and causes a significant reduction in the affinity of the inhibitors for the enzyme
K41N
-
strongly decreased activity for NADPH and increased activity with NADH
M99T
-
the mutant is resistant toward inhibition by AFN-1252
R40Q
-
strongly decreased activity for NADPH and increased activity with NADH
R40Q/K41N
-
strongly decreased activity for NADPH and increased activity with NADH
Y147F
-
the mutant is catalytically defective but retains its sensitivity to inhibitor AFN-1252
Y147H
-
the mutant is catalytically defective but retains its sensitivity to inhibitor AFN-1252
M99T
-
the mutant is resistant toward inhibition by AFN-1252
-
Y147F
-
the mutant is catalytically defective but retains its sensitivity to inhibitor AFN-1252
-
Y147H
-
the mutant is catalytically defective but retains its sensitivity to inhibitor AFN-1252
-
additional information
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
drug development
-
the bacterial enoyl-ACP reductase is a target for antibacterial drug development
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Show AA Sequence (372 entries)
Please use the Sequence Search for a specific query.
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LINKS TO OTHER DATABASES (specific for EC-Number 1.3.1.10)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
InterPro (database of protein families, domains and functional sites)