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
1.3.1.39
-
RECOMMENDED NAME
GeneOntology No.
enoyl-[acyl-carrier-protein] reductase (NADPH, Re-specific)
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
an acyl-[acyl-carrier protein] + NADP+ = a trans-2,3-dehydroacyl-[acyl-carrier protein] + NADPH + H+
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
fatty acid elongation -- saturated
-
octanoyl-ACP biosynthesis (mitochondria, yeast)
-
palmitate biosynthesis I (animals and fungi)
-
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).
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
acyl-ACP dehydrogenase
-
-
-
-
enoyl-ACP reductase
-
-
-
-
enoyl-ACP reductase III
P71079
-
enoyl-ACP reductase III
Bacillus subtilis 168
P71079
-
-
enoyl-[acyl carrier protein] (reduced nicotinamide adenine dinucleotide phosphate) reductase
-
-
-
-
FabL
P71079
-
FabL
Bacillus subtilis 168
P71079
-
-
NADPH 2-enoyl Co A reductase
-
-
-
-
PG1416
Q7MAW0
locus name
PG1416
Q7MAW0
locus name
-
CAS REGISTRY NUMBER
COMMENTARY
37251-09-5
not distinguished from EC 1.3.1.10
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
isoform FabL
UniProt
Manually annotated by BRENDA team
Bacillus subtilis 168
isoform FabL
UniProt
Manually annotated by BRENDA team
guinea pig
-
-
Manually annotated by BRENDA team
chicken
-
-
Manually annotated by BRENDA team
Pigeon
-
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
crotonyl-CoA + NADPH + H+
butyryl-CoA + NADP+
show the reaction diagram
Q7MAW0
-
-
-
?
crotonyl-N-acetyl-cysteamine + NADPH
butyryl-N-acetyl-cysteamine + NADP+
show the reaction diagram
-
-
-
?
crotonyl-N-acetyl-cysteamine + NADPH
butyryl-N-acetyl-cysteamine + NADP+
show the reaction diagram
-
-
-
?
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
-
-
-
additional information
?
-
-
part of fatty acid synthesis reducing double bonds of a great varity of acyl thioesters
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
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
-
-
-
additional information
?
-
-
part of fatty acid synthesis reducing double bonds of a great varity of acyl thioesters
-
-
-
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
NADPH
-
-
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
panosialin A
-
acylbenzenediol sulfate metabolites from Streptomyces sp. AN1761, potently inhibits bacterial enoyl-ACP reductases of Staphylococcus aureus, Streptococcus pneumoniae, and Mycobacterium tuberculosis
panosialin B
-
acylbenzenediol sulfate metabolites from Streptomyces sp. AN1761, potently inhibits bacterial enoyl-ACP reductases of Staphylococcus aureus, Streptococcus pneumoniae, and Mycobacterium tuberculosis
panosialin wA
-
acylbenzenediol sulfate metabolites from Streptomyces sp. AN1761, potently inhibits bacterial enoyl-ACP reductases of Staphylococcus aureus, Streptococcus pneumoniae, and Mycobacterium tuberculosis
panosialin wB
-
acylbenzenediol sulfate metabolites from Streptomyces sp. AN1761, potently inhibits bacterial enoyl-ACP reductases of Staphylococcus aureus, Streptococcus pneumoniae, and Mycobacterium tuberculosis
pyridoxal 5'-phosphate
-
4 mM at 30C for 15 min on complete fatty acid synthase selectively and completely inactivates
triclosan
-
affinity varies with pH-value
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.017
-
NADPH
Q7MAW0
pH 7.5, 25C
0.0478
-
crotonyl-CoA
Q7MAW0
pH 7.5, 25C
additional information
-
additional information
-
NADP+ binds to enzyme in anti conformation both between nicotinamide-ribose and adenine-ribose
-
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0043
-
panosialin A
-
pH 6.5, temperature not specified in the publication
0.0053
-
panosialin B
-
pH 6.5, temperature not specified in the publication
0.003
-
panosialin wA
-
pH 6.5, temperature not specified in the publication
0.0046
-
panosialin wB
-
pH 6.5, temperature not specified in the publication
0.00066
-
triclosan
-
pH 6.5, temperature not specified in the publication
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
as there is no information concerning the stereochemistry of hydrogen transfer from NADPH to substrate an appointment to EC 1.3.1.10 or EC 1.3.1.39 is impossible for the enzyme of this source
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
prepared of particle-free supernatant
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
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)
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
Q7MAW0
x * 33090, calculated
?
-
x * 33090, calculated
-
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
native enzyme and in complex with NADPH and inhibitor triclosan, to 2.8 A and 1.8 A resolution, respectively
P71079
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
-
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7.2
-
-
activity of entire fatty acid synthase declined no more than 15% in 24 h at pH 7.2 in phosphate puffer
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-20C, 10 mM DTT
Pigeon
-
-20C, 5 mg/ml concentration, 30% glycerol stock, stable for at least 1 month
Q7MAW0
-20C, 10 mM DTT
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expression in Escherichia coli
Q7MAW0
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
analysis
Q7MAW0
sensitive assay method measuring the fluorescence decrease of NADPH as it is converted to NADP+ during the reaction, optimized for high-throughput screening
analysis
-
sensitive assay method measuring the fluorescence decrease of NADPH as it is converted to NADP+ during the reaction, optimized for high-throughput screening
-