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Information on EC 1.3.1.10 - enoyl-[acyl-carrier-protein] reductase (NADPH, Si-specific) and Organism(s) Bacillus cereus and UniProt Accession Q81GI3

for references in articles please use BRENDA:EC1.3.1.10
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IUBMB Comments
One of the activities of EC 2.3.1.86, fatty-acyl-CoA synthase system, an enzyme found in yeasts (Ascomycota and 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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Bacillus cereus
UNIPROT: Q81GI3
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The taxonomic range for the selected organisms is: Bacillus cereus
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
enoyl reductase, enoyl-acp reductase, enoyl-acyl carrier protein reductase, etr1p, fabl2, mrf1p, enoyl-[acyl-carrier-protein] reductase, enoyl acyl-carrier-protein reductase, 2-enoyl thioester reductase, 2-trans-enoyl-acp reductase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
enoyl-[acyl carrier protein] reductase
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acyl-ACP dehydrogenase
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enoyl acyl-carrier-protein reductase
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enoyl-ACP reductase
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enoyl-[acyl carrier protein] reductase
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NADPH 2-enoyl Co A reductase
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reductase, enoyl-[acyl carrier protein] (reduced nicotinamide adenine dinucleotide phosphate)
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
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oxidation
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reduction
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PATHWAY SOURCE
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 system, an enzyme found in yeasts (Ascomycota and 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
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
an acyl-[acyl-carrier protein] + NADP+
a trans-2,3-dehydroacyl-[acyl-carrier protein] + NADPH + H+
show the reaction diagram
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-
-
?
an acyl-[acyl-carrier protein] + NADP+
a trans-2,3-dehydroacyl-[acyl-carrier protein] + NADPH + H+
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
an acyl-[acyl-carrier protein] + NADP+
a trans-2,3-dehydroacyl-[acyl-carrier protein] + NADPH + H+
show the reaction diagram
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-
?
an acyl-[acyl-carrier protein] + NADP+
a trans-2,3-dehydroacyl-[acyl-carrier protein] + NADPH + H+
show the reaction diagram
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?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADP+
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
NADP+
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
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(E)-N-(1,2-dimethyl-1H-indol-3-ylmethyl)-N-methyl-3-(7-oxo-5,6,7,8-tetrahydro-1,8-naphthyridin-3-yl)acrylamide
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00006
(E)-N-(1,2-dimethyl-1H-indol-3-ylmethyl)-N-methyl-3-(7-oxo-5,6,7,8-tetrahydro-1,8-naphthyridin-3-yl)acrylamide
pH 7.0, 30°C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
ENR is an essential enzyme in type II fatty-acid synthesis that catalyzes the last step in each elongation cycle
metabolism
ENR is an essential enzyme in type II fatty-acid synthesis that catalyzes the last step in each elongation cycle
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
the FabL apo form exists as a homodimer in both crystal and solution
tetramer
the ternary complex of FabL with NADP+ or an indole naphthyridinone inhibitor forms a homotetramer
dimer
the FabL apo form exists as a homodimer in both crystal and solution
tetramer
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
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His6-tagged BcFabL from Escherichia coli strain BL21(DE3) by nickel affinity and adsorption chromatography and gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
BcFabL from strain 6A5 is expressed in Escherichia coli strain BL21(DE3) as His6-tagged protein
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kim, S.J.; Ha, B.H.; Kim, K.H.; Hong, S.K.; Shin, K.J.; Suh, S.W.; Kim, E.E.
Dimeric and tetrameric forms of enoyl-acyl carrier protein reductase from Bacillus cereus
Biochem. Biophys. Res. Commun.
400
517-522
2010
Bacillus cereus, Bacillus cereus (Q81GI3), Bacillus cereus 6A5, Bacillus cereus DSM 31 (Q81GI3)
Manually annotated by BRENDA team