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
1.3.1.10
-
RECOMMENDED NAME
GeneOntology No.
enoyl-[acyl-carrier-protein] reductase (NADPH, Si-specific)
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
an acyl-[acyl-carrier protein] + NADP+ = a 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
syn addition via 2Re,3Si attack on double bond
-
an acyl-[acyl-carrier protein] + NADP+ = a trans-2,3-dehydroacyl-[acyl-carrier protein] + NADPH + H+
show the reaction diagram
anti addition via 2Si,3Si attack on double bond
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
Biotin metabolism
-
fatty acid elongation -- saturated
-
Metabolic pathways
-
octanoyl-ACP biosynthesis (mitochondria, yeast)
-
palmitate biosynthesis I (animals and fungi)
-
stearate biosynthesis III (fungi)
-
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 1.3.1.9, enoyl-[acyl-carrier-protein] reductase (NADH).
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
1-cyclohexenylcarbonyl coenzyme A reductase
-
-
2-enoyl thioester reductase
-
-
2-enoyl thioester reductase
P38071
-
2-trans-enoyl-ACP reductase
-
-
acyl-ACP dehydrogenase
-
-
-
-
enoyl acyl-carrier-protein reductase
-
-
-
-
enoyl reductase
-
-
enoyl thioester reductase
-
-
enoyl thioester reductase
P38071
-
enoyl-ACP reductase
-
-
-
-
enoyl-ACP reductase
P71079
-
enoyl-ACP reductase
Bacillus subtilis 168
P71079
-
-
enoyl-ACP reductase
-
-
enoyl-ACP reductase III
-
-
enoyl-ACP reductase III
Bacillus subtilis 168
-
-
-
enoyl-ACP-reductase II
Q7MAW0
-
enoyl-ACP-reductase II
Q7MAW0
-
-
enoyl-acyl carrier protein reductase
-
-
enoyl-[acyl carrier protein] reductase
-, Q81GI3
-
enoyl-[acyl carrier protein] reductase
Bacillus cereus 6A5
-, Q81GI3
-
-
enoyl-[acyl carrier protein] reductase
Bacillus cereus DSM31
Q81GI3
-
-
ENR
-, Q81GI3
-
ENR
Bacillus cereus 6A5
-, Q81GI3
-
-
ENR
Bacillus cereus DSM31
Q81GI3
-
-
FabL
-, Q81GI3
-
FabL
Bacillus cereus 6A5
-, Q81GI3
-
-
FabL
Bacillus cereus DSM31
Q81GI3
-
-
FabL
P71079
-
NADPH 2-enoyl Co A reductase
-
-
-
-
reductase, enoyl-[acyl carrier protein] (reduced nicotinamide adenine dinucleotide phosphate)
-
-
-
-
trans-enoyl-[acyl-carrier-protein] reductase
-
-
trans-enoyl-[acyl-carrier-protein] reductase
Bacillus subtilis 168
-
-
-
YgaA
P71079
-
YgaA
Bacillus subtilis 168
P71079
-
-
FabL
Bacillus subtilis 168
-, P71079
-
-
additional information
-
enzyme belongs to the medium-chain dehydrogenase/reductase superfamily of enzymes
additional information
-
NADPH dependent acyl-ACP reductase and NADH dependent acyl-ACP/acyl-CoA reductase activity reside on the same protein
additional information
P38071
enzyme belongs to the medium-chain dehydrogenase/reductase superfamily of enzymes
CAS REGISTRY NUMBER
COMMENTARY
37251-09-5
-, not distinguished from EC 1.3.1.39
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
Bacillus cereus 6A5
-
-
-
Manually annotated by BRENDA team
Bacillus cereus DSM31
-
SwissProt
Manually annotated by BRENDA team
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
-
-
Manually annotated by BRENDA team
strain 168
-
-
Manually annotated by BRENDA team
Bacillus subtilis 168
strain 168
-
-
Manually annotated by BRENDA team
enzyme Etr1p
-
-
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
-
-
Manually annotated by BRENDA team
enzyme Mrf1p
SwissProt
Manually annotated by BRENDA team
Saccharomyces cerevisiae
-
-
Manually annotated by BRENDA team
scientific name not stated
-
-
Manually annotated by BRENDA team
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
-
-
Manually annotated by BRENDA team
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
Uniprot
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
malfunction
-, P71079
physiological function of the enzyme is examined by knocking out the gene and determining the effect of the gene disruptions on cell growth and triclosan sensitivity, the gene is not essential
malfunction
Bacillus subtilis 168
-
physiological function of the enzyme is examined by knocking out the gene and determining the effect of the gene disruptions on cell growth and triclosan sensitivity, the gene is not essential
-
metabolism
-, Q81GI3
ENR is an essential enzyme in type II fatty-acid synthesis that catalyzes the last step in each elongation cycle; ENR is an essential enzyme in type II fatty-acid synthesis that catalyzes the last step in each elongation cycle
metabolism
Bacillus cereus 6A5
-
ENR is an essential enzyme in type II fatty-acid synthesis that catalyzes the last step in each elongation cycle; ENR is an essential enzyme in type II fatty-acid synthesis that catalyzes the last step in each elongation cycle
-
metabolism
Bacillus cereus DSM31
-
ENR is an essential enzyme in type II fatty-acid synthesis that catalyzes the last step in each elongation cycle
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
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
-, P71079
-
-
-
?
(2E)-but-2-enoyl-[acyl carrier protein] + NADPH + H+
butanoyl-[acyl-carrier protein] + NADP+
show the reaction diagram
Bacillus subtilis 168
-
-
-
-
?
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-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
-
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
Bacillus subtilis, Bacillus subtilis 168
-
-
-
-
?
an acyl-[acyl-carrier protein] + NADP+
a trans-2,3-dehydroacyl-[acyl-carrier protein] + NADPH + H+
show the reaction diagram
-, Q81GI3
-
-
-
?
an acyl-[acyl-carrier protein] + NADP+
a trans-2,3-dehydroacyl-[acyl-carrier protein] + NADPH + H+
show the reaction diagram
-, Q81GI3
assay method by consumption of beta-nicotinamide adenine dinucleotide phosphate during reduction of trans-2-octenoyl-N-acetylcysteamine as the substrate
-
-
?
an acyl-[acyl-carrier protein] + NADP+
a trans-2,3-dehydroacyl-[acyl-carrier protein] + NADPH + H+
show the reaction diagram
Bacillus cereus 6A5
-
-, assay method by consumption of beta-nicotinamide adenine dinucleotide phosphate during reduction of trans-2-octenoyl-N-acetylcysteamine as the substrate
-
-
?
an acyl-[acyl-carrier protein] + NADP+
a trans-2,3-dehydroacyl-[acyl-carrier protein] + NADPH + H+
show the reaction diagram
Bacillus cereus DSM31
Q81GI3
-
-
-
?
crotonyl-N-acetyl-cysteamine + NADPH
butyryl-N-acetyl-cysteamine + NADP+
show the reaction diagram
Q9RMI3
-
-
?
crotonyl-N-acetyl-cysteamine + NADPH
butyryl-N-acetyl-cysteamine + NADP+
show the reaction diagram
-
stereochemistry
-
?
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
-, P71079
-
-
?
crotonyl-[acyl-carrier protein] + NADPH
butyryl-[acyl-carrier protein] + NADP+
show the reaction diagram
-
-
-
?
crotonyl-[acyl-carrier protein] + NADPH
butyryl-[acyl-carrier protein] + NADP+
show the reaction diagram
-
-
-
?
crotonyl-[acyl-carrier protein] + NADPH
butyryl-[acyl-carrier protein] + NADP+
show the reaction diagram
-
-
-
?
crotonyl-[acyl-carrier protein] + NADPH
butyryl-[acyl-carrier protein] + NADP+
show the reaction diagram
-
substrate created by E. coli enzymes during assay
-
-
crotonyl-[acyl-carrier protein] + NADPH
butyryl-[acyl-carrier protein] + NADP+
show the reaction diagram
-
anti addition of hydrogen via a 2-Si,3-Si attack on the double bond
-
?
crotonyl-[acyl-carrier protein] + NADPH
butyryl-[acyl-carrier protein] + NADP+
show the reaction diagram
-
anti addition of hydrogen via a 2-Si,3-Si attack on the double bond
-
?
crotonyl-[acyl-carrier protein] + NADPH + H+
butyryl-[acyl-carrier protein] + NADP+
show the reaction diagram
-, Q7MAW0
-
-
-
?
crotonyl-[acyl-carrier protein] + NADPH + H+
butyryl-[acyl-carrier protein] + NADP+
show the reaction diagram
Q7MAW0
-
-
-
?
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
-
-
-
-
?
octenoyl-N-acetyl-cysteamine + NADPH
octanoyl-N-acetyl-cysteamine + NADP+
show the reaction diagram
Q9RMI3
-
-
?
octenoyl-N-acetyl-cysteamine + NADPH
octanoyl-N-acetyl-cysteamine + NADP+
show the reaction diagram
-, P71079
-
-
?
S-((2E)-oct-2-enoyl)-N-acetylcysteamine + NADPH + H+
S-octanoyl-N-acetylcysteamine + NADP+
show the reaction diagram
-, P71079
-
-
-
?
S-((2E)-oct-2-enoyl)-N-acetylcysteamine + NADPH + H+
S-octanoyl-N-acetylcysteamine + NADP+
show the reaction diagram
Bacillus subtilis 168
-
-
-
-
?
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
acyl-[acyl-carrier protein] + NADP+
show the reaction diagram
P38071
-
-
-
?
trans-2,3-dehydroacyl-[acyl-carrier protein] + NADPH
acyl-[acyl-carrier protein] + NADP+
show the reaction diagram
-
reaction within the fatty acid synthase complex, indispensable for respiratory function in mitochondria
-
-
?
trans-2,3-dehydroacyl-[acyl-carrier protein] + NADPH
acyl-[acyl-carrier protein] + NADP+
show the reaction diagram
P38071
reaction within the fatty acid synthase complex, indispensable for respiratory function in mitochondria
-
-
?
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
-
reaction in ansatrienin biosynthesis out of shikimic acid
-
?
dodecenoyl-[Staphylococcus aureus acyl carrier protein] + NADPH + H+
dodecanoyl-[Staphylococcus aureus acyl carrier protein] + NADP+
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
active on substrates with acyl chain length C4-C16
-
-
-
additional information
?
-
-
inactive with enoyl-CoA substrates
-
-
-
additional information
?
-
-
part of fatty acid synthesis reducing double bonds of a great varity of acyl thioesters
-
-
-
additional information
?
-
Q9RMI3
part of fatty acid synthesis reducing double bonds of a great varity of acyl thioesters
-
-
-
additional information
?
-
-, P71079
part of fatty acid synthesis reducing double bonds of a great varity of acyl thioesters
-
-
-
additional information
?
-
-
part of fatty acid synthesis reducing double bonds of a great varity of acyl thioesters
-
-
-
additional information
?
-
-
part of fatty acid synthesis reducing double bonds of a great varity of acyl thioesters
-
-
-
additional information
?
-
-
part of fatty acid synthesis reducing double bonds of a great varity of acyl thioesters
-
-
-
additional information
?
-
-
part of fatty acid synthesis reducing double bonds of a great varity of acyl thioesters
-
-
-
additional information
?
-
-
no activity with crotonyl-CoA and NADH
-
-
-
additional information
?
-
-, P71079
catalyzes the NADPH-dependent reduction of trans-2-enoyl thioesters of both N-acetylcysteamine and acyl-carrier protein
-
-
-
additional information
?
-
-
activity measurement by reduction of the trans-2-octenoyl N-acetylcysteamine as substrate and NADPH as cofactor
-
-
-
additional information
?
-
-, Q7MAW0
enzyme possesses intrinsic NADPH oxidase activity in the absence of the crotonyl-CoA substrate
-
-
-
additional information
?
-
Bacillus subtilis 168
-
catalyzes the NADPH-dependent reduction of trans-2-enoyl thioesters of both N-acetylcysteamine and acyl-carrier protein
-
-
-
additional information
?
-
Q7MAW0
enzyme possesses intrinsic NADPH oxidase activity in the absence of the crotonyl-CoA substrate
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
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
-, Q81GI3
-
-
-
?
an acyl-[acyl-carrier protein] + NADP+
a trans-2,3-dehydroacyl-[acyl-carrier protein] + NADPH + H+
show the reaction diagram
Bacillus cereus 6A5
-
-
-
-
?
trans-2,3-dehydroacyl-[acyl-carrier protein] + NADPH
acyl-[acyl-carrier protein] + NADP+
show the reaction diagram
-
reaction within the fatty acid synthase complex, indispensable for respiratory function in mitochondria
-
-
?
trans-2,3-dehydroacyl-[acyl-carrier protein] + NADPH
acyl-[acyl-carrier protein] + NADP+
show the reaction diagram
P38071
reaction within the fatty acid synthase complex, indispensable for respiratory function in mitochondria
-
-
?
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
-
?
an acyl-[acyl-carrier protein] + NADP+
a trans-2,3-dehydroacyl-[acyl-carrier protein] + NADPH + H+
show the reaction diagram
Bacillus cereus DSM31
Q81GI3
-
-
-
?
additional information
?
-
-
part of fatty acid synthesis reducing double bonds of a great varity of acyl thioesters
-
-
-
additional information
?
-
Q9RMI3
part of fatty acid synthesis reducing double bonds of a great varity of acyl thioesters
-
-
-
additional information
?
-
-, P71079
part of fatty acid synthesis reducing double bonds of a great varity of acyl thioesters
-
-
-
additional information
?
-
-
part of fatty acid synthesis reducing double bonds of a great varity of acyl thioesters
-
-
-
additional information
?
-
-
part of fatty acid synthesis reducing double bonds of a great varity of acyl thioesters
-
-
-
additional information
?
-
-
part of fatty acid synthesis reducing double bonds of a great varity of acyl thioesters
-
-
-
additional information
?
-
-
part of fatty acid synthesis reducing double bonds of a great varity of acyl thioesters
-
-
-
additional information
?
-
-, P71079
catalyzes the NADPH-dependent reduction of trans-2-enoyl thioesters of both N-acetylcysteamine and acyl-carrier protein
-
-
-
additional information
?
-
Bacillus subtilis 168
-
catalyzes the NADPH-dependent reduction of trans-2-enoyl thioesters of both N-acetylcysteamine and acyl-carrier protein
-
-
-
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
FAD
-
enzyme contains 0.8 mol FAD/enzyme, but functional role is not investigated
NADH
-
also essential for activity, article leaves doubtful whether NADH or NADPH or both are cofactors
NADH
-, Q7MAW0
poor cofactor
NADP+
-
dependent
NADP+
-, Q81GI3
FabL is NADP+-dependent, the side chain of Lys164 of the Tyr-(Xaa)6-Lys dyad at the active site forms a hydrogen bond with the hydroxyl group of the nicotinamide ribose moiety, binding structure, overview; the side chain of Lys164 of the Tyr-(Xaa)6-Lys dyad at the active site forms a hydrogen bond with the hydroxyl group of the nicotinamide ribose moiety, binding structure, overview
NADPH
-
stereospecificity of NADPH is pro-4S
NADPH
-
specific for form B, i.e. hydrogen in position HB is transferred to substrate
NADPH
-
specific for form B, i.e. hydrogen in position HB is transferred to substrate
NADPH
-, P71079
inactive with NADH
NADPH
-
dependent on, tyrosine in the binding cleft is critical for enzyme activity, NADPH binding induces conformational changes in the enzyme, overview
NADPH
P38071
dependent on
NADPH
-, Q7MAW0
inhibitory at high concentration
additional information
-
enzyme also exhibits NADPH dependent activity, if isolated at pH 6.5
-
additional information
-
enzyme is highly specific for NADH, even if isolated at pH 6.5
-
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
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
-, Q81GI3
-
-
5-chloro-2-phenoxyphenol
-
-
5-ethyl-2-phenoxyphenol
-
-
6-methyl-2-(propane-1-sulfonyl)-4a,7a-dihydro-2H-thieno[3,2-d][1,2,3]diazaborinin-1-ol
-
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
-
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
-
a natural inhibitor from the fungus Sporothrix sp. strain FN611
Hexachlorophene
Q9RMI3
half-maximal inhibition at 0.004 mM
N-ethylmaleimide
-
-
p-hydroxymercuribenzoate
-
-
palmitoyl-CoA
-
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
Q9RMI3
half-maximal inhibition at 0.003 mM; slow-binding inhibitor forms a stable, ternary complex with enzyme and NADP+
triclosan
-, P71079
half-maximal inhibition at 0.016 mM; reversible inhibitor that does not form a ternary complex; reversibly inhibited by, does not form the stable ternary complex characteristic of the FabI proteins. Expression of YgaA complements the fabI(ts) defect in Escherichia coli and conferrs complete triclosan resistance
triclosan
-, Q81GI3
;
iodoacetate
-
-
additional information
-
not inhibited by: triclosan
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
NH4Cl
-, Q7MAW0
required for stability and activity. Assay in presence of 0.1 M NH4Cl
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.025
-
1-cyclohexenylcarbonyl-CoA
-
vmax 0.0075 mmol/mg/min
0.03
-
5-hydroxycyclohex-1-enecarbonyl-CoA
-
vmax 0.0053 mmol/mg/min
0.008
-
Crotonyl-N-acetyl-cysteamine
-
wild type enzyme, at 25C, in 100 mM Na2HPO4 buffer (pH 7.8)
8
-
Crotonyl-N-acetyl-cysteamine
Q9RMI3
Vmax 0.0003 nmol/min/mg
0.0478
-
crotonyl-[acyl-carrier protein]
-, Q7MAW0
pH 7.5, 25C
0.0115
-
crotonyl-[Staphylococcus aureus acyl carrier protein]
-
wild type enzyme, at 25C, in 100 mM Na2HPO4 buffer (pH 7.8)
0.0241
-
dodecenoyl-CoA
-
wild type enzyme, at 25C, in 100 mM Na2HPO4 buffer (pH 7.8)
-
0.0233
-
dodecenoyl-N-acetyl-cysteamine
-
wild type enzyme, at 25C, in 100 mM Na2HPO4 buffer (pH 7.8)
0.0045
-
dodecenoyl-[Staphylococcus aureus acyl carrier protein]
-
wild type enzyme, at 25C, in 100 mM Na2HPO4 buffer (pH 7.8)
0.0114
-
dodecenoyl-[Staphylococcus aureus acyl carrier protein]
-
mutant enzyme A95V, at 25C, in 100 mM Na2HPO4 buffer (pH 7.8)
0.016
-
NADPH
-, P71079
; no cooperativity in binding NADPH
0.0171
-
NADPH
-, Q7MAW0
pH 7.5, 25C
0.2694
-
NADPH
-
mutant enzyme A95V, at 25C, in 100 mM Na2HPO4 buffer (pH 7.8)
0.4296
-
NADPH
-
mutant enzyme F204S, at 25C, in 100 mM Na2HPO4 buffer (pH 7.8)
0.0184
-
dodecenoyl-[Staphylococcus aureus acyl carrier protein]
-
mutant enzyme F204S, at 25C, in 100 mM Na2HPO4 buffer (pH 7.8)
additional information
-
NADPH
-
value above 2 mM
additional information
-
NADPH
Q9RMI3
cooperative binding with Hill coefficient 2.2; half-maximal rate at 0.065 mM NADPH
1
-
NADPH
-
Km above 1 mM, mutant enzyme I193S, at 25C, in 100 mM Na2HPO4 buffer (pH 7.8)
additional information
-
trans-3,4-dihydroxycyclohexa-1,5-dienecarbonyl-CoA
-
only impure solution available, KM and vmax in same order of magnitude as with 1-cyclohexenylcarbonyl-CoA
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1.5
-
Crotonyl-N-acetyl-cysteamine
-
wild type enzyme, at 25C, in 100 mM Na2HPO4 buffer (pH 7.8)
11.6
-
crotonyl-[Staphylococcus aureus acyl carrier protein]
-
wild type enzyme, at 25C, in 100 mM Na2HPO4 buffer (pH 7.8)
18
-
dodecenoyl-CoA
-
wild type enzyme, at 25C, in 100 mM Na2HPO4 buffer (pH 7.8)
-
30.4
-
dodecenoyl-N-acetyl-cysteamine
-
wild type enzyme, at 25C, in 100 mM Na2HPO4 buffer (pH 7.8)
18.4
-
dodecenoyl-[Staphylococcus aureus acyl carrier protein]
-
mutant enzyme A95V, at 25C, in 100 mM Na2HPO4 buffer (pH 7.8)
130.2
-
dodecenoyl-[Staphylococcus aureus acyl carrier protein]
-
wild type enzyme, at 25C, in 100 mM Na2HPO4 buffer (pH 7.8)
157.3
-
dodecenoyl-[Staphylococcus aureus acyl carrier protein]
-
mutant enzyme F204S, at 25C, in 100 mM Na2HPO4 buffer (pH 7.8)
130.2
-
NADPH
-
wild type enzyme, at 25C, in 100 mM Na2HPO4 buffer (pH 7.8)
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
6e-05
-
(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
-, Q81GI3
pH 7.0, 30C
-
0.0014
-
aquastatin A
-
pH 6.5, 30C, versus NADPH
0.00161
-
aquastatin A
-
pH 6.5, 30C, versus trans-2-octenoyl N-acetylcysteamine
0.109
-
NADPH
-, Q7MAW0
pH 7.5, 25C
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0032
-
aquastatin A
-
FabI, pH 6.5, 30C
0.0034
-
degalactosylated aquastatin A
-
FabI, pH 6.5, 30C
0.016
-
triclosan
-, P71079
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.008
-
-
crude cell extract
0.18
-
-, P71079
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
-
-, P71079
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
-
-
purified recombinant wild-type enzyme
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6
-
-
no measurements below pH 6 carried out
6.5
-
-
assay at
7.5
-
-
assay at
7.5
-
-, Q7MAW0
-
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6
-
-
inactive above pH 8, no measurement below pH 6
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
-
-, P71079
assay at
30
-
-
assay at
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
29700
-
-
ChcA, gene sequence
30000
-
-
SDS-PAGE
33000
-
-
FabI, SDS-PAGE
34000
-
-
FabK, gene sequence
37000
-
-
ChcA, SDS-PAGE, +/-2000
75000
-
-
ChcA, gel filtration on superose 12, +/-10000
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-, Q7MAW0
x * 33090, calculated
?
-
x * 33090, calculated
-
dimer
-
2 * 37000, homodimer, comparison molecular weight SDS-PAGE versus gel filtration
dimer
-, Q81GI3
the FabL apo form exists as a homodimer in both crystal and solution; the FabL apo form exists as a homodimer in both crystal and solution
dimer
Bacillus cereus 6A5
-
the FabL apo form exists as a homodimer in both crystal and solution; the FabL apo form exists as a homodimer in both crystal and solution
-
dimer
Bacillus cereus DSM31
-
the FabL apo form exists as a homodimer in both crystal and solution
-
tetramer
-, Q81GI3
the ternary complex of FabL with NADP+ or an indole naphthyridinone inhibitor forms a homotetramer; the ternary complex of FabL with NADP+ or the indole naphthyridinone 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 forms a homotetramer
tetramer
Bacillus cereus 6A5
-
the ternary complex of FabL with NADP+ or an indole naphthyridinone inhibitor forms a homotetramer; the ternary complex of FabL with NADP+ or the indole naphthyridinone 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 forms a homotetramer
-
tetramer
Bacillus cereus DSM31
-
the ternary complex of FabL with NADP+ or an indole naphthyridinone inhibitor forms a homotetramer
-
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
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
-, Q81GI3
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
-
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
-
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7.6
-
-
unstable at
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
55
-
-
5 min stable
60
-
-
5 min, inactivation
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
enzyme can be concentrated to 20 mg/ml without precipitation
-, Q7MAW0
ORGANIC SOLVENT
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
dimethyl sulfoxide
-, Q7MAW0
up to 10%, no loss of activity
dimethyl sulfoxide
-
up to 10%, no loss of activity
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-20C, 10 mM phosphate buffer, pH 6.5, 5 mM 2-mercaptoethanol, inactivation in 2-3 months
-
-20C, rapidly inactivated
-
-20C, 30% glycerol, no significant loss of activity for at least 1 month
-, Q7MAW0
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
recombinant His6-tagged BcFabL from Escherichia coli strain BL21(DE3) by nickel affinity and adsorption chromatography and gel filtration
-, Q81GI3
Ni2+ affinity chromatography on his-tagged protein; Ni2+ chelation chromatography
-, P71079
nickel-chelated Hi-Trap column chromatography, Hi-Trap Blue HP column chromatography, Q-Sepharose column chromatography, and Superdex-75 gel filtration
-
recombinant wild-type enzyme and mutant Y79N from Saccharomyces cerevisiae mutant strain BJ1991 mrf1DELTA
-
in BisTris puffer pH 6.5 in order to retain NADPH dependent activity which is lost at pH 7.5
-
no separation from NADH specific enzyme
-
no separation from NADH specific enzyme; sonification and chromatography using DEAE-Cellulose, Sephadex G-100, Hydroxylapatite
-
which also catalyzes the reduction of enoyl-CoA substrates
-
recombinant protein
-, Q7MAW0
recombinant wild-type enzyme and mutant Y73N from mutant strain BJ1991 mrf1DELTA
P38071
Ni2+ affinity chromatography on his-tagged protein
Q9RMI3
Ni2+-NTA resin chromatography
-
chromatography of protein overexpressed in Escherichia coli by using Sephadex G-100, DEAE, Mono-Q HR 5/5
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
BcFabL from strain 6A5 is expressed in Escherichia coli strain BL21(DE3) as His6-tagged protein
-, Q81GI3
expressed in Escherichia coli BL21(DE3) cells
-
expression in Escherichia coli; fabL in pET15b for his-tagged overexpression
-, P71079
overexpression of wild-type enzyme and mutant Y79N in enzyme-deficient Saccharomyces cerevisiae mutant strain BJ1991 mrf1DELTA, using the catalase 1 promotor
-
envM in bacteriophage P1
-
fabI in pUC118
-
expression in Escherichia coli
-, Q7MAW0
overexpression of wild-type enzyme and mutant Y73N in enzyme-deficient mutant strain BJ1991 mrf1DELTA, using the catalase 1 promotor
P38071
expressed in Escherichia coli BL21(DE3)pLysS cells
-
fabI of strain RN4220 found by homology and cloned into pET15b for his-tagged overexpression
Q9RMI3
fabK in expression plasmid
-
chcA in pUC18 and pET3C
-
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
transcription factor Adr1p influences transcription levels of ETR1 promoter, which controls the expression of 2-trans-enoyl-ACP reductase
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
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
P38071
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
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
-, P71079
the ygaA knockout is 250fold more sensitive to the inhibitor triclosan
additional information
Bacillus subtilis 168
-
the ygaA knockout is 250fold more sensitive to the inhibitor triclosan
-
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
drug development
-
the bacterial enoyl-ACP reductase is a target for antibacterial drug development