Information on EC 1.3.1.39 - enoyl-[acyl-carrier-protein] reductase (NADPH, Re-specific)

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY hide
1.3.1.39
-
RECOMMENDED NAME
GeneOntology No.
enoyl-[acyl-carrier-protein] reductase (NADPH, Re-specific)
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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-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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-
-
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redox reaction
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-
-
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reduction
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-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
fatty acid elongation -- saturated
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octanoyl-[acyl-carrier protein] biosynthesis (mitochondria, yeast)
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palmitate biosynthesis I (animals and fungi)
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SYSTEMATIC NAME
IUBMB Comments
acyl-[acyl-carrier protein]:NADP+ oxidoreductase (Re-specific)
This 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 an acyl-carrier protein. It is one of the activities of EC 2.3.1.85, animal fatty-acid synthase. The mammalian enzyme is Re-specific with respect to NADP+. cf. EC 1.3.1.10, enoyl-[acyl-carrier-protein] reductase (NADPH, Si-specific) and EC 1.3.1.104, enoyl-[acyl-carrier-protein] reductase (NADPH).
CAS REGISTRY NUMBER
COMMENTARY hide
37251-09-5
not distinguished from EC 1.3.1.10
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
isoform FabL
UniProt
Manually annotated by BRENDA team
isoform FabL
UniProt
Manually annotated by BRENDA team
guinea pig
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-
Manually annotated by BRENDA team
chicken
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-
Manually annotated by BRENDA team
Pigeon
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-
-
Manually annotated by BRENDA team
rat
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-
Manually annotated by BRENDA team
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+
butyryl-CoA + NADP+
show the reaction diagram
crotonyl-N-acetyl-cysteamine + NADPH
butyryl-N-acetyl-cysteamine + NADP+
show the reaction diagram
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
panosialin A
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acylbenzenediol sulfate metabolites from Streptomyces sp. AN1761, potently inhibits bacterial enoyl-ACP reductases of Staphylococcus aureus, Streptococcus pneumoniae, and Mycobacterium tuberculosis
panosialin B
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acylbenzenediol sulfate metabolites from Streptomyces sp. AN1761, potently inhibits bacterial enoyl-ACP reductases of Staphylococcus aureus, Streptococcus pneumoniae, and Mycobacterium tuberculosis
panosialin wA
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acylbenzenediol sulfate metabolites from Streptomyces sp. AN1761, potently inhibits bacterial enoyl-ACP reductases of Staphylococcus aureus, Streptococcus pneumoniae, and Mycobacterium tuberculosis
panosialin wB
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acylbenzenediol sulfate metabolites from Streptomyces sp. AN1761, potently inhibits bacterial enoyl-ACP reductases of Staphylococcus aureus, Streptococcus pneumoniae, and Mycobacterium tuberculosis
pyridoxal 5'-phosphate
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4 mM at 30C for 15 min on complete fatty acid synthase selectively and completely inactivates
triclosan
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0478
crotonyl-CoA
pH 7.5, 25C
0.017
NADPH
pH 7.5, 25C
additional information
additional information
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NADP+ binds to enzyme in anti conformation both between nicotinamide-ribose and adenine-ribose
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0043
panosialin A
Staphylococcus aureus
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pH 6.5, temperature not specified in the publication
0.0053
panosialin B
Staphylococcus aureus
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pH 6.5, temperature not specified in the publication
0.003
panosialin wA
Staphylococcus aureus
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pH 6.5, temperature not specified in the publication
0.0046
panosialin wB
Staphylococcus aureus
-
pH 6.5, temperature not specified in the publication
0.00066
triclosan
Staphylococcus aureus
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pH 6.5, temperature not specified in the publication
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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prepared of particle-free supernatant
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
Staphylococcus aureus (strain MRSA252)
Staphylococcus aureus (strain MRSA252)
Staphylococcus aureus (strain MRSA252)
Staphylococcus aureus (strain MRSA252)
Staphylococcus aureus (strain N315)
Staphylococcus aureus (strain N315)
Staphylococcus aureus (strain N315)
Staphylococcus aureus (strain N315)
Staphylococcus aureus (strain N315)
Staphylococcus aureus (strain N315)
Staphylococcus aureus (strain N315)
Staphylococcus aureus (strain N315)
Staphylococcus aureus (strain N315)
Staphylococcus aureus (strain N315)
Staphylococcus aureus (strain N315)
Staphylococcus aureus (strain N315)
Staphylococcus aureus (strain N315)
Staphylococcus aureus (strain N315)
Staphylococcus aureus (strain N315)
Staphylococcus aureus (strain N315)
Staphylococcus aureus (strain N315)
Staphylococcus aureus (strain N315)
Staphylococcus aureus (strain USA300)
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
native enzyme and in complex with NADPH and inhibitor triclosan, to 2.8 A and 1.8 A resolution, respectively
apo-enzyme and complex with NADPH and inhibitor triclosan. Enzyme is a tetramer. In the apo-form of the SaFabI structure, residues Ile193 to Leu196 form part of a flexible loop adjacent to the active site. In the open conformation, the loop is on the surface of the protein, and does not form any secondary structure or contribute to inhibitor or cofactor binding. The substrate-binding loop of the holo-enzyme containing Ser197, Val201 and Phe204 has a closed conformation
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.2
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activity of entire fatty acid synthase declined no more than 15% in 24 h at pH 7.2 in phosphate puffer
390763
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, 10 mM DTT
-20C, 5 mg/ml concentration, 30% glycerol stock, stable for at least 1 month
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis