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Information on EC 1.3.1.10 - enoyl-[acyl-carrier-protein] reductase (NADPH, Si-specific) and Organism(s) Bacillus subtilis and UniProt Accession P71079
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1.3.1.10 enoyl-[acyl-carrier-protein] reductase (NADPH, Si-specific)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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Word Map
- 1.3.1.10
- tuberculosis
- mycobacterium
- triclosan
- isoniazid
- aureus
- falciparum
-
antitubercular
- polyketide
-
mycolic
-
beta-ketoacyl
-
thioesterase
- pfenr
-
antimycobacterial
-
diphenyl
-
antituberculosis
- diazaborine
- fas-ii
-
ketoacyl
-
dehydrase
-
biocide
-
anti-tb
-
malonyl
- ketoreductase
-
transacylase
-
beta-ketoacyl-acp
- catalase-peroxidase
-
mdr-tb
- drug development
The taxonomic range for the selected organisms is: Bacillus subtilis
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Reaction Schemes
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
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acyl-ACP dehydrogenase
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-
-
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enoyl acyl-carrier-protein reductase
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-
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enoyl-ACP reductase
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-
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NADPH 2-enoyl Co A reductase
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-
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reductase, enoyl-[acyl carrier protein] (reduced nicotinamide adenine dinucleotide phosphate)
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
-
-
-
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oxidation
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-
-
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reduction
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-
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PATHWAY SOURCE
PATHWAYS
BRENDA
-
-, -, -, -, -, -, -
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
37251-09-5
-
37251-09-5
not distinguished from EC 1.3.1.39
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(2E)-but-2-enoyl-[acyl carrier protein] + NADPH + H+
butanoyl-[acyl-carrier protein] + NADP+
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-
-
?
S-((2E)-oct-2-enoyl)-N-acetylcysteamine + NADPH + H+
S-octanoyl-N-acetylcysteamine + NADP+
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-
-
?
acyl-[acyl-carrier protein] + NADP+
trans-2,3-dehydroacyl-[acyl-carrier protein] + NADPH + H+
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-
-
-
?
crotonyl-[acyl-carrier protein] + NADPH
butyryl-[acyl-carrier protein] + NADP+
-
-
?
octenoyl-N-acetyl-cysteamine + NADPH
octanoyl-N-acetyl-cysteamine + NADP+
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-
?
additional information
?
-
-
catalyzes the NADPH-dependent reduction of trans-2-enoyl thioesters of both N-acetylcysteamine and acyl-carrier protein
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-
?
additional information
?
-
catalyzes the NADPH-dependent reduction of trans-2-enoyl thioesters of both N-acetylcysteamine and acyl-carrier protein
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?
additional information
?
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part of fatty acid synthesis reducing double bonds of a great varity of acyl thioesters
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-
?
additional information
?
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part of fatty acid synthesis reducing double bonds of a great varity of acyl thioesters
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-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
catalyzes the NADPH-dependent reduction of trans-2-enoyl thioesters of both N-acetylcysteamine and acyl-carrier protein
-
-
?
additional information
?
-
catalyzes the NADPH-dependent reduction of trans-2-enoyl thioesters of both N-acetylcysteamine and acyl-carrier protein
-
-
?
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
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
triclosan
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
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.18
spectrophotometric assay, S-((2E)-oct-2-enoyl)-N-acetylcysteamine as a substrate
0.3
spectrophotometric assay, (2E)-but-2-enoyl-[acyl carrier protein] as a substrate
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
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
PDB
SCOP
CATH
UNIPROT
ORGANISM
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
the ygaA knockout is 250fold more sensitive to the inhibitor triclosan
additional information
the ygaA knockout is 250fold more sensitive to the inhibitor triclosan
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Heath, R.J.; Su, N.; Murphy, C.K.; Rock, C.O.
The enoyl-[acyl-carrier-protein] reductases FabI and FabL from Bacillus subtilis
J. Biol. Chem.
275
40128-40133
2000
Bacillus subtilis, Bacillus subtilis (P71079)
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Release 2023.1 (January 2023)
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