BRENDA - Enzyme Database show
show all sequences of 1.3.1.10

Aquastatin A, a new inhibitor of enoyl-acyl carrier protein reductase from Sporothrix sp. FN611

Kwon, Y.J.; Fang, Y.; Xu, G.H.; Kim, W.G.; Biol. Pharm. Bull. 32, 2061-2064 (2009)

Data extracted from this reference:

Application
Application
Commentary
Organism
drug development
the bacterial enoyl-ACP reductase is a target for antibacterial drug development
Staphylococcus aureus
Inhibitors
Inhibitors
Commentary
Organism
Structure
aquastatin A
a natural inhibitor from the fungus Sporothrix sp. strain FN611, mixed-type inhibition against FabI with respect to the substrate trans-2-octenoyl N-acetylcysteamine and NADPH, prevents the growth of Staphylococcus aureus and methicillin-resistant Staphylococcus aureus with minimum inhibitory concentration of 0.016-0.032 mg/ml, overview
Staphylococcus aureus
degalactosylated aquastatin A
a natural inhibitor from the fungus Sporothrix sp. strain FN611
Staphylococcus aureus
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Staphylococcus aureus
-
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
activity measurement by reduction of the trans-2-octenoyl N-acetylcysteamine as substrate and NADPH as cofactor
711351
Staphylococcus aureus
?
-
-
-
-
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
30
-
assay at
Staphylococcus aureus
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6.5
-
assay at
Staphylococcus aureus
Cofactor
Cofactor
Commentary
Organism
Structure
NADPH
-
Staphylococcus aureus
Ki Value [mM]
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
0.0014
-
aquastatin A
pH 6.5, 30°C, versus NADPH
Staphylococcus aureus
0.00161
-
aquastatin A
pH 6.5, 30°C, versus trans-2-octenoyl N-acetylcysteamine
Staphylococcus aureus
IC50 Value
IC50 Value
IC50 Value Maximum
Commentary
Organism
Inhibitor
Structure
0.0032
-
FabI, pH 6.5, 30°C
Staphylococcus aureus
aquastatin A
0.0034
-
FabI, pH 6.5, 30°C
Staphylococcus aureus
degalactosylated aquastatin A
Application (protein specific)
Application
Commentary
Organism
drug development
the bacterial enoyl-ACP reductase is a target for antibacterial drug development
Staphylococcus aureus
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NADPH
-
Staphylococcus aureus
IC50 Value (protein specific)
IC50 Value
IC50 Value Maximum
Commentary
Organism
Inhibitor
Structure
0.0032
-
FabI, pH 6.5, 30°C
Staphylococcus aureus
aquastatin A
0.0034
-
FabI, pH 6.5, 30°C
Staphylococcus aureus
degalactosylated aquastatin A
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
aquastatin A
a natural inhibitor from the fungus Sporothrix sp. strain FN611, mixed-type inhibition against FabI with respect to the substrate trans-2-octenoyl N-acetylcysteamine and NADPH, prevents the growth of Staphylococcus aureus and methicillin-resistant Staphylococcus aureus with minimum inhibitory concentration of 0.016-0.032 mg/ml, overview
Staphylococcus aureus
degalactosylated aquastatin A
a natural inhibitor from the fungus Sporothrix sp. strain FN611
Staphylococcus aureus
Ki Value [mM] (protein specific)
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
0.0014
-
aquastatin A
pH 6.5, 30°C, versus NADPH
Staphylococcus aureus
0.00161
-
aquastatin A
pH 6.5, 30°C, versus trans-2-octenoyl N-acetylcysteamine
Staphylococcus aureus
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
activity measurement by reduction of the trans-2-octenoyl N-acetylcysteamine as substrate and NADPH as cofactor
711351
Staphylococcus aureus
?
-
-
-
-
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
30
-
assay at
Staphylococcus aureus
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6.5
-
assay at
Staphylococcus aureus
Other publictions for EC 1.3.1.10
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
740013
Dutta
Crystal structure of hexanoyl- ...
Mycobacterium tuberculosis
Biochem. J.
450
127-139
2013
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740716
Yao
Resistance to AFN-1252 arises ...
Staphylococcus aureus, Staphylococcus aureus RN4220
J. Biol. Chem.
288
36261-36271
2013
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726431
Hevener
Expression, purification and c ...
Porphyromonas gingivalis, Porphyromonas gingivalis W83
Protein Expr. Purif.
85
100-108
2012
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711113
Kim
Dimeric and tetrameric forms o ...
Bacillus cereus, Bacillus cereus 6A5, Bacillus cereus DSM 31
Biochem. Biophys. Res. Commun.
400
517-522
2010
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703756
Gurvitz
A novel circuit overrides Adr1 ...
Saccharomyces cerevisiae
FEMS Microbiol. Lett.
297
255-260
2009
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711351
Kwon
Aquastatin A, a new inhibitor ...
Staphylococcus aureus
Biol. Pharm. Bull.
32
2061-2064
2009
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685233
Xu
Mechanism and inhibition of sa ...
Staphylococcus aureus
Biochemistry
47
4228-4236
2008
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10
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8
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684170
Kim
Crystallization and preliminar ...
Bacillus subtilis 168, Bacillus subtilis
Acta Crystallogr. Sect. F
63
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2007
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1
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656515
Airenne
Structure-function analysis of ...
Candida tropicalis, Saccharomyces cerevisiae
J. Mol. Biol.
327
47-59
2003
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390504
Heath
Inhibition of the Staphylococc ...
Escherichia coli, Staphylococcus aureus
J. Biol. Chem.
275
4654-4659
2000
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390505
Heath
The enoyl-[acyl-carrier-protei ...
Bacillus subtilis
J. Biol. Chem.
275
40128-40133
2000
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1
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390508
Heath
A triclosan-resistant bacteria ...
Streptococcus pneumoniae
Nature
406
145-146
2000
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1
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390503
Bergler
The enoyl-[acyl-carrier-protei ...
Escherichia coli, Salmonella enterica subsp. enterica serovar Typhimurium
Eur. J. Biochem.
242
689-694
1996
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390509
Wang
Cloning and characterization o ...
Streptomyces collinus
J. Bacteriol.
178
6873-6881
1996
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390507
Bergler
Sequences of the envM gene and ...
Escherichia coli
J. Gen. Microbiol.
138
2093-2100
1992
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Turnowsky
EnvM genes of Salmonella typhi ...
Escherichia coli, Salmonella enterica subsp. enterica serovar Typhimurium
J. Bacteriol.
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6555-6565
1989
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285669
Shimakata
The procaryotic nature of the ...
Carthamus tinctorius
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217
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1982
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390496
Saito
Steric course of reaction cata ...
Escherichia coli
Eur. J. Biochem.
116
581-586
1981
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390497
Sedgwick
-
Stereochemical course of hydro ...
Saccharomyces cerevisiae
J. Chem. Soc. Chem. Commun.
1980
96-97
1980
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390501
Saito
Incorporation of hydrogen atom ...
Escherichia coli
Biochim. Biophys. Acta
618
202-213
1980
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390498
Seyama
Origin of hydrogen atoms in th ...
Escherichia coli, Saccharomyces cerevisiae
J. Biochem.
82
1325-1329
1977
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390499
Weeks
-
Enoyl acyl carrier protein red ...
Escherichia coli
Methods Enzymol.
14
66-73
1969
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5
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5
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390500
Weeks
Studies on the mechanism of fa ...
Escherichia coli
J. Biol. Chem.
243
1180-1189
1968
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