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

EC NUMBER
COMMENTARY hide
1.3.1.10
-
RECOMMENDED NAME
GeneOntology No.
enoyl-[acyl-carrier-protein] reductase (NADPH, Si-specific)
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
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
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redox reaction
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-
-
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reduction
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-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Biotin metabolism
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Fatty acid biosynthesis
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fatty acid elongation -- saturated
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lipid metabolism
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Metabolic pathways
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octanoyl-[acyl-carrier protein] biosynthesis (mitochondria, yeast)
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palmitate biosynthesis I (animals and fungi)
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stearate biosynthesis III (fungi)
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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).
CAS REGISTRY NUMBER
COMMENTARY hide
37251-09-5
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37251-09-5
not distinguished from EC 1.3.1.39
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
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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
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
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, 23C
-
-
?
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
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+
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
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-
-
-
?
dodecenoyl-CoA + NADPH + H+
dodecanoyl-CoA + NADP+
show the reaction diagram
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-
-
-
?
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
-
-
-
-
?
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
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prefers acyl carrier protein substrates carrying fatty acids with long acyl chains
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-
?
trans-2-hexenoyl-CoA + NADPH
hexanoyl-CoA + NADP+
show the reaction diagram
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-
-
-
?
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
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?
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
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
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?
additional information
?
-
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
additional information
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
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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
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.025
1-cyclohexenylcarbonyl-CoA
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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, 25C
0.0115
crotonyl-[Staphylococcus aureus acyl carrier protein]
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wild type enzyme, at 25C, in 100 mM Na2HPO4 buffer (pH 7.8)
0.0241
dodec-2-enoyl-CoA
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wild type enzyme, at 25C, in 100 mM Na2HPO4 buffer (pH 7.8)
0.0233
dodecenoyl-N-acetyl-cysteamine
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wild type enzyme, at 25C, 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
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.5
Crotonyl-N-acetyl-cysteamine
Staphylococcus aureus
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wild type enzyme, at 25C, in 100 mM Na2HPO4 buffer (pH 7.8)
11.6
crotonyl-[Staphylococcus aureus acyl carrier protein]
Staphylococcus aureus
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wild type enzyme, at 25C, in 100 mM Na2HPO4 buffer (pH 7.8)
18
dodec-2-enoyl-CoA
Staphylococcus aureus
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wild type enzyme, at 25C, in 100 mM Na2HPO4 buffer (pH 7.8)
30.4
dodecenoyl-N-acetyl-cysteamine
Staphylococcus aureus
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wild type enzyme, at 25C, in 100 mM Na2HPO4 buffer (pH 7.8)
18.4 - 157.3
dodecenoyl-[Staphylococcus aureus acyl carrier protein]
130.2
NADPH
Staphylococcus aureus
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wild type enzyme, at 25C, in 100 mM Na2HPO4 buffer (pH 7.8)
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, 30C
-
0.0014 - 0.00161
aquastatin A
0.109
NADPH
pH 7.5, 25C
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0032
aquastatin A
Staphylococcus aureus
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FabI, pH 6.5, 30C
0.0034
degalactosylated aquastatin A
Staphylococcus aureus
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FabI, pH 6.5, 30C
0.016
triclosan
Bacillus subtilis
P71079
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.008
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crude cell extract
0.18
spectrophotometric assay, S-((2E)-oct-2-enoyl)-N-acetylcysteamine as a substrate; with octenyl-N-acetyl-cysteamine
0.2
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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
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purified by chromatography on DEAE-cellulose and Blue sepharose
0.882
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crude Escherichia coli cell extract after overexpression
3.667
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purified, overexpressed enzyme
20
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purified recombinant wild-type enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5
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assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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
34000
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FabK, gene sequence
37000
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ChcA, SDS-PAGE, +/-2000
75000
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ChcA, gel filtration on superose 12, +/-10000
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
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 4C
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purified recombinant wild-type enzyme free and in complex with NADPH, mutant enzyme Y79N, hanging drop vapour diffusion method, 22C, 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
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unstable at
390499, 390500
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
55
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5 min stable
60
-
5 min, inactivation
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
enzyme can be concentrated to 20 mg/ml without precipitation
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimethyl sulfoxide
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, 10 mM phosphate buffer, pH 6.5, 5 mM 2-mercaptoethanol, inactivation in 2-3 months
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-20C, 30% glycerol, no significant loss of activity for at least 1 month
-20C, 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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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
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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
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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
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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
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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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expression in Escherichia coli
expression in Escherichia coli; fabL in pET15b for his-tagged overexpression
fabI in pUC118
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fabI of strain RN4220 found by homology and cloned into pET15b for his-tagged overexpression
fabK in expression plasmid
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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
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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
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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
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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
R40Q
-
strongly decreased activity for NADPH and increased activity with NADH
R40Q/K41N
-
strongly decreased activity for NADPH and increased activity with NADH
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
drug development
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the bacterial enoyl-ACP reductase is a target for antibacterial drug development
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