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Information on EC 1.3.1.39 - enoyl-[acyl-carrier-protein] reductase (NADPH, Re-specific) and Organism(s) Staphylococcus aureus and UniProt Accession Q6GI75

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IUBMB Comments
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, fatty-acid synthase system. 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).
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Staphylococcus aureus
UNIPROT: Q6GI75
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The taxonomic range for the selected organisms is: Staphylococcus aureus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
acyl-ACP dehydrogenase, enoyl-ACP reductase, enoyl-ACP reductase III, enoyl-[acyl carrier protein] (reduced nicotinamide adenine dinucleotide phosphate) reductase, FabI, FabK, FabL, NADPH 2-enoyl Co A reductase, PG1416, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
acyl-ACP dehydrogenase
-
-
-
-
enoyl-ACP reductase
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-
-
enoyl-[acyl carrier protein] (reduced nicotinamide adenine dinucleotide phosphate) reductase
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-
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NADPH 2-enoyl Co A reductase
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
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-
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oxidation
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reduction
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-
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -, -, -, -
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, fatty-acid synthase system. 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
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
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
triclosan
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0043
panosialin A
Staphylococcus aureus
pH 6.5, temperature not specified in the publication
0.0053
panosialin B
Staphylococcus aureus
pH 6.5, temperature not specified in the publication
0.003
panosialin wA
Staphylococcus aureus
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
pH 6.5, temperature not specified in the publication
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kwon, Y.J.; Sohn, M.J.; Oh, T.; Cho, S.N.; Kim, C.J.; Kim, W.G.
Panosialins, inhibitors of enoyl-ACP reductase from Streptomyces sp. AN1761
J. Microbiol. Biotechnol.
23
184-188
2013
Staphylococcus aureus (Q6GI75)
Manually annotated by BRENDA team
Priyadarshi, A.; Kim, E.; Hwang, K.
Structural insights into Staphylococcus aureus enoyl-ACP reductase (FabI), in complex with NADP end triclosan
Proteins Struct. Funct. Bioinform.
78
480-486
2010
Staphylococcus aureus (Q6GI75)
Manually annotated by BRENDA team