Information on EC 1.3.1.104 - enoyl-[acyl-carrier-protein] reductase (NADPH)

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.3.1.104
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RECOMMENDED NAME
GeneOntology No.
enoyl-[acyl-carrier-protein] reductase (NADPH)
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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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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
fatty acid elongation -- saturated
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Fatty acid biosynthesis
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Metabolic pathways
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SYSTEMATIC NAME
IUBMB Comments
acyl-[acyl-carrier protein]:NADP+ oxidoreductase
The enzyme completes each cycle of fatty acid elongation by catalysing the stereospecific reduction of the double bond at position 2 of a growing fatty acid chain, while linked to the acyl-carrier protein, in an NADPH-dependent manner. This entry stands for enzymes whose stereo-specificity with respect to NADP+ is not known. [cf. EC 1.3.1.39 enoyl-[acyl-carrier-protein] reductase (NADPH, Re-specific), EC 1.3.1.10, enoyl-[acyl-carrier-protein] reductase (NADPH, Si-specific) and EC 1.3.1.9, enoyl-[acyl-carrier-protein] reductase (NADH)].
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
crotonyl-CoA + NADPH + H+
butanoyl-CoA + NAP+
show the reaction diagram
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-
-
?
crotonyl-N-acetylcysteamine + NADPH + H+
butyryl-N-acetylcysteamine + NADP+
show the reaction diagram
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-
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?
crotonyl-[acyl-carrier-protein] + NADPH + H+
butyryl-[acyl-carrier-protein] + NADP+
show the reaction diagram
gama-chloro-beta-methylcrotonyl-[acyl-carrier-protein] + NADPH + H+
gama-chloro-beta-methylbutanoyl-[acyl-carrier-protein] + NADP+
show the reaction diagram
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-
-
?
trans-2-octenoyl-N-acetylcysteamine + NADPH + H+
octanoyl-N-acetylcysteamine + NADP+
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADPH
additional information
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no cofactor: NADH
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
AFN-1252
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antibiotic AFN-1252, i.e. (2E)-N-methyl-N-[(3-methyl-1-benzofuran-2-yl)methyl]-3-(7-oxo-5,6,7,8-tetrahydro-1,8-naphthyridin-3-yl)prop-2-enamide, only binds to the NADPH form of FabI
Hexachlorophene
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triclosan
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
8
crotonyl-N-acetylcysteamine
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pH 7.5, 25°C
0.016
NADPH
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pH 7.5, 25°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.004 - 0.069
AFN-1252
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.003
triclosan
Staphylococcus aureus
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pH 7.5, 25°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.66
pH not specified in the publication, 25°C
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
27100
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x * 27100, calculated
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
both free form and complexed with NADP+ and inhibitor triclosan, to 2.2 and 1.8 A resolution, respectively. The substrate-binding region in the apo-FabL structure is found in the open form. In addition, the beta4-alpha5 and beta5-alpha7 regions, which include the catalytic residues as well as the cofactor binding residues, get collapsed into the pocket. These differences result in a tetrameric arrangement totally different from NADH-dependent isoform FabI
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to 2.5 A resolution. Hexagonal space group P622, with unit-cell parameters a = b = 139.56, c = 62.75 A , alpha = beta = 90, gamma = 120°
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
39.4
mutant A95V, melting temperature
40.2
mutant M99T, melting temperature
40.5
wild-type, melting temperature
58.8
wild-type, melting temperature in presence of both triclosan and NADP+. Neither triclosan nor NADP+ alone increases the Tm value
60.2
mutant M99T, melting temperature in presence of both triclosan and NADP+
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D273A
about 55% of wild-type activity
D273N
about 70% of wild-type activity
K251A
activity similar to wild-type
K251R
activity similar to wild-type
A95V
about 15% of wild-type activtiy, no inhibition by triclosan and no shift in melting temperature in presence of both triclosan and NADP+
F204S
no shift in melting temperature in presence of both triclosan and NADP+
G23S
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mutation increases the resistance of Staphylococcus aureus to triclosan by an order of magnitude
I193S
no shift in melting temperature in presence of both triclosan and NADP+
Y147H
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mutant is resistant to antibiotic AFN-1252 and to triclosan, about 5% of wild-type catalytic activity. A strain expressing Y147H has a pronounced growth defect that is rescued by exogenous fatty acid supplementation
A95V
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about 15% of wild-type activtiy, no inhibition by triclosan and no shift in melting temperature in presence of both triclosan and NADP+
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F204S
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no shift in melting temperature in presence of both triclosan and NADP+
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I193S
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no shift in melting temperature in presence of both triclosan and NADP+
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Y147H
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mutant is resistant to antibiotic AFN-1252 and to triclosan, about 5% of wild-type catalytic activity. A strain expressing Y147H has a pronounced growth defect that is rescued by exogenous fatty acid supplementation
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additional information
replacement of amino acids 55-66 by CurF enoyl reductase cyclopropanase loop leads to gain-of-function activity as a cyclopropanase. With substrate 3-chloromethyl-crotonyl-[acyl-carrier-protein], the formation of both the reduced product and also the cyclopropanated productis detected at levels of about one-quarter of the total product
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
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