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Enzyme Nomenclature
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
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EC NUMBER 
COMMENTARY 
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
ORGANISM
UNIPROT
LITERATURE
an acyl-[acyl-carrier protein] + NADP+ = a trans-2,3-dehydroacyl-[acyl-carrier protein] + NADPH + H+
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-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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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)].
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
expression complements the Escherichia coli fabI temperature-sensitive mutant
physiological function
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expression of isoform FabL complements the temperature-sensitive fabI defect in Escherichia coli and confers complete triclosan resistance. Knockouts of the FabL gene in Bacillus subtilis are viable, but double knockouts of isoforms FabI and FabL are not obtained. The ygaA knockout is 250fold more sensitive to triclosan than wild-type
physiological function
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expression of isoform FabL complements the temperature-sensitive fabI defect in Escherichia coli and confers complete triclosan resistance. Knockouts of the FabL gene in Bacillus subtilis are viable, but double knockouts of isoforms FabI and FabL are not obtained. The ygaA knockout is 250fold more sensitive to triclosan than wild-type
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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
crotonyl-N-acetylcysteamine + NADPH + H+
butyryl-N-acetylcysteamine + NADP+
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-
-
?
trans-2-octenoyl-N-acetylcysteamine + NADPH + H+
octanoyl-N-acetylcysteamine + NADP+
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-
-
?
trans-2-octenoyl-N-acetylcysteamine + NADPH + H+
octanoyl-N-acetylcysteamine + NADP+
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-
-
?
trans-2-octenoyl-N-acetylcysteamine + NADPH + H+
octanoyl-N-acetylcysteamine + NADP+
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-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADPH
exhibits specific and positive cooperative binding of NADPH. The cofactor concentration that yields 50% of the maximal rate is 65 microM
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
triclosan
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enzyme is reversibly inhibited by triclosan, but does not form a stable ternary complex
triclosan
the introduction of a plasmid expressing the enzyme gene leads to triclosan resistance
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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PDB
SCOP
CATH
ORGANISM
UNIPROT
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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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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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
G23S
mutation increases the resistance of Staphylococcus aureus to triclosan by an order of magnitude
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LINKS TO OTHER DATABASES (specific for EC-Number 1.3.1.104)
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