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1,1'-[6-(1-phenyl-1H-pyrrol-2-yl)-1,3,5-triazine-2,4-diyl]bis(azepane)
-
1,1'-[6-[1-(3,5-dimethylphenyl)-1H-pyrrol-2-yl]-1,3,5-triazine-2,4-diyl]bis(azepane)
-
1-(2-phenylethyl)-1H-pyrrole
-
1-(3,5-dimethylphenyl)-1H-pyrrole
-
1-(3-phenylpropyl)-1H-pyrrole
-
1-cyclohexyl-1H-pyrrole
-
1-[4-(1-benzyl-1H-tetrazol-5-yl)-4-[(prop-2-yn-1-yl)amino]piperidin-1-yl]-3-(3-methyl-3H-diazirin-3-yl)propan-1-one
-
1-[4-chloro-6-(1-phenyl-1H-pyrrol-2-yl)-1,3,5-triazin-2-yl]azepane
-
10-bromo-3-(butylsulfanyl)-6-(thiophen-2-yl)-6,7-dihydro[1,2,4]triazino[5,6-d][3,1]benzoxazepine
-
2,4-bis(aziridin-1-yl)-6-(1-phenyl-1H-pyrrol-2-yl)-1,3,5-triazine
-
2,4-bis(aziridin-1-yl)-6-(1-phenylpyrrol-2-yl)-S-triazine
allosteric inhibitor
2,4-bis(morpholin-4-yl)-6-(1-phenyl-1H-pyrrol-2-yl)-1,3,5-triazine
-
2,4-bis[(oxiran-2-yl)methoxy]-6-(1-phenyl-1H-pyrrol-2-yl)-1,3,5-triazine
-
2,4-dichloro-6-(1-cyclohexyl-1H-pyrrol-2-yl)-1,3,5-triazine
-
2,4-dichloro-6-(1-phenyl-1H-pyrrol-2-yl)-1,3,5-triazine
-
2,4-dichloro-6-[1-(2-phenylethyl)-1H-pyrrol-2-yl]-1,3,5-triazine
-
2,4-dichloro-6-[1-(3,5-dimethylphenyl)-1H-pyrrol-2-yl]-1,3,5-triazine
-
2,4-dichloro-6-[1-(3-phenylpropyl)-1H-pyrrol-2-yl]-1,3,5-triazine
-
2-(1-benzyl-1H-pyrrol-2-yl)-4,6-dichloro-1,3,5-triazine
-
2-(1-phenyl-1H-pyrrol-2-yl)-4,6-di(piperidin-1-yl)-1,3,5-triazine
-
2-(1-phenyl-1H-pyrrol-2-yl)-4,6-di(pyrrolidin-1-yl)-1,3,5-triazine
-
2-chloro-4-(methanesulfonyl)benzoic acid
-
2-methyl-4-(3-phenyl[1,2,4]triazolo[3,4-b][1,3,4]thiadiazol-6-yl)quinoline
-
2-[(5-cyanopyridin-2-yl)(methyl)amino]ethyl 4-methyl-1,2,3-thiadiazole-5-carboxylate
-
2-[2-[2-(2-aminoethoxy)ethoxy]ethoxy]ethyl 2-(4-methoxyphenyl)-3-methyl-4-oxo-1,2,3,3a,4,9b-hexahydro[1]benzopyrano[3,4-b]pyrrole-1-carboxylate
-
3-(butylsulfanyl)-6-(5-methylfuran-2-yl)-6,7-dihydro[1,2,4]triazino[5,6-d][3,1]benzoxazepine
-
4-(1-benzyl-1H-pyrrol-2-yl)-N,N-dibutyl-6-chloro-1,3,5-triazin-2-amine
-
4-(azepan-1-yl)-6-(1-benzyl-1H-pyrrol-2-yl)-N,N-dibutyl-1,3,5-triazin-2-amine
-
4-(azepan-1-yl)-N,N-dibutyl-6-(1-cyclohexyl-1H-pyrrol-2-yl)-1,3,5-triazin-2-amine
-
4-(azepan-1-yl)-N,N-dibutyl-6-(1-phenyl-1H-pyrrol-2-yl)-1,3,5-triazin-2-amine
-
4-(azepan-1-yl)-N,N-dibutyl-6-[1-(2-phenylethyl)-1H-pyrrol-2-yl]-1,3,5-triazin-2-amine
pecies-specific inhibitor
4-(azepan-1-yl)-N,N-dibutyl-6-[1-(3,5-dimethylphenyl)-1H-pyrrol-2-yl]-1,3,5-triazin-2-amine
-
4-(azepan-1-yl)-N,N-dibutyl-6-[1-(3-phenylpropyl)-1H-pyrrol-2-yl]-1,3,5-triazin-2-amine
-
4-(azepan-1-yl)-N,N-dihexyl-6-(1-phenyl-1H-pyrrol-2-yl)-1,3,5-triazin-2-amine
-
4-(azepan-1-yl)-N,N-dimethyl-6-(1-phenyl-1H-pyrrol-2-yl)-1,3,5-triazin-2-amine
-
4-chloro-N,N-dihexyl-6-(1-phenyl-1H-pyrrol-2-yl)-1,3,5-triazin-2-amine
-
5-bromo-1,3-dimethylpyrimidine-2,4(1H,3H)-dione
-
6-(1-benzyl-1H-pyrrol-2-yl)-N2,N2-dibutyl-N4,N4-dihexyl-1,3,5-triazine-2,4-diamine
-
6-(1-phenyl-1H-pyrrol-2-yl)-1,3,5-triazine-2,4-diamine
-
dipropan-2-yl [(E)-(2-benzoylhydrazinylidene)(hydroxyamino)methyl]phosphonate
-
methyl 2-(4-methoxyphenyl)-3-methyl-4-oxo-3,4-dihydro[1]benzopyrano[3,4-b]pyrrole-1-carboxylate
-
methyl 3-amino-4-(propane-2-sulfonyl)thiophene-2-carboxylate
-
methyl 3-benzyl-2-(4-methoxyphenyl)-4-oxo-3,4-dihydro[1]benzopyrano[3,4-b]pyrrole-1-carboxylate
-
N'-(2,4,5-trichlorobenzene-1-sulfonyl)pyridine-3-carbohydrazide
-
N'-(2,6-dichlorophenyl)-5-nitrofuran-2-carbohydrazide
-
N,N-dibutyl-4-chloro-6-(1-cyclohexyl-1H-pyrrol-2-yl)-1,3,5-triazin-2-amine
-
N,N-dibutyl-4-chloro-6-(1-phenyl-1H-pyrrol-2-yl)-1,3,5-triazin-2-amine
-
N,N-dibutyl-4-chloro-6-[1-(2-phenylethyl)-1H-pyrrol-2-yl]-1,3,5-triazin-2-amine
-
N,N-dibutyl-4-chloro-6-[1-(3,5-dimethylphenyl)-1H-pyrrol-2-yl]-1,3,5-triazin-2-amine
-
N,N-dibutyl-4-chloro-6-[1-(3-phenylpropyl)-1H-pyrrol-2-yl]-1,3,5-triazin-2-amine
-
N-(2-[[(4-chlorophenyl)methyl]sulfanyl]ethyl)-3-methylbut-2-enamide
-
N-(3-chlorophenyl)-N'-(5-[[(4-chlorophenyl)sulfanyl]methyl]furan-2-yl)urea
-
N-[4-[(3,5-dichlorophenyl)sulfamoyl]phenyl]acetamide
-
N2,N2,N4,N4-tetramethyl-6-(1-phenyl-1H-pyrrol-2-yl)-1,3,5-triazine-2,4-diamine
-
N2,N4-dimethyl-6-(1-phenyl-1H-pyrrol-2-yl)-1,3,5-triazine-2,4-diamine
-
[1,1'-biphenyl]-2,2'-dicarbonitrile
-
2,4,6-Trinitrobenzenesulfonic acid
-
-
ATP
-
competes with methylenediphosphonate and diphosphate for binding at the allosteric regulatory site involving Lys112
Ca2+-diphosphate
-
nonhydrolyzable substrate analogue
Diazonium-1H-tetrazole
-
-
diphosphate
-
competes with ATP and methylenediphosphonate for binding at the allosteric regulatory site involving Lys112
hydroxymethylbisphosphonate
-
competitive with diphosphate
methylene diphosphate-Mg complex
-
competitive inhibition of MgPPi hydrolysis, binds at the active site
Methylenediphosphonate
-
competes with ATP and diphosphate for binding at the allosteric regulatory site involving Lys112
additional information
discovery and synthesis of analogues of lead compound allosteric inhibitor (2,4-bis(aziridin-1-yl)-6-(1-phenylpyrrol-2-yl)-S-triazine) as inhibitors of bacterial PPiases
-
fluoride
-
fluoride
reversible inhibition, binds to the active site, binding structure, overview
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0.00001 - 1.8
diphosphate
0.00045 - 4.2
Mg-diphosphate
0.91
Triphosphate
-
at pH 9.1 and 25Ā°C
additional information
additional information
-
0.00001
diphosphate
-
at pH 9.1 and 25Ā°C
0.0016
diphosphate
-
pH 6.5, wild type, hydrolysis of diphosphate
0.0016
diphosphate
-
pH 7.2, E20D
0.0018
diphosphate
-
pH 7.2, D97E, hydrolysis of diphosphate
0.0024
diphosphate
-
pH 8, D97E, hydrolysis of diphosphate
0.0027
diphosphate
-
pH 7.5, 25Ā°C, mutant K112Q/K148Q
0.0032
diphosphate
-
pH 7.5, 25Ā°C, wild-type enzyme and mutant K112Q/K115A
0.0034
diphosphate
-
pH 8, wild type, hydrolysis of diphosphate
0.0035
diphosphate
-
pH 7.2, wild type, hydrolysis of diphosphate
0.0045
diphosphate
-
pH 7.5, 25Ā°C, mutant K112Q
0.0053
diphosphate
-
pH 7.5, 25Ā°C, trimeric mutant K112Q
0.13
diphosphate
-
wild type hexamer, pH 7.5
0.8
diphosphate
-
wild type dimer, pH 7.5
1.3
diphosphate
-
E145Q hexamer, pH 7.5
1.8
diphosphate
-
E145Q dimer, pH 7.5
0.00045
Mg-diphosphate
-
pH 7.2, 1 mM Mg2+, 0.1 M TES/KOH
0.00053
Mg-diphosphate
-
pH 7.2, 1 mM Mg2+, 0.1 M MOPS/KOH
0.00116
Mg-diphosphate
-
pH 7.2, 1 mM Mg2+, 0.08 M monoethalamine/HCl + 0.02 M Tes/KOH
0.00133
Mg-diphosphate
-
pH 7.2, 1 mM Mg2+, 0.1 M Tris-HCl + 0.05 M KCl
0.00144
Mg-diphosphate
-
pH 7.2, 1 mM Mg2+, 0.08 M Tes/Tris + 0.02 M Tes/KOH
0.00168
Mg-diphosphate
-
pH 7.2, 1 mM Mg2+, 0.2 M Tes/Tris
0.00196
Mg-diphosphate
-
pH 7.2, 1 mM Mg2+, 0.15 M Tris-HCl or 0.08 M 2-amino-2-methyl-1,3-propanediol/HCl + 0.02 M Tes/KOH
0.0023
Mg-diphosphate
-
pH 7.2, hexameric, H136Q enzyme
0.0027
Mg-diphosphate
-
pH 7.2, H140Q enzyme, hexameric
0.0034
Mg-diphosphate
-
pH 8, wild type enzyme
0.0055
Mg-diphosphate
-
pH 7.2, 1 mM Mg2+, 0.08 M NH4Cl + 0.02 M TES/KOH
0.008
Mg-diphosphate
-
pH 8, hexameric, H136Q enzyme
0.198
Mg-diphosphate
-
pH 7.2, H136Q enzyme, trimeric
0.44
Mg-diphosphate
-
pH 8, H140Q enzyme, trimeric
4.2
Mg-diphosphate
-
pH 7.2, H140Q enzyme, trimeric
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
detailed kinetics of hexameric, trimeric enzyme, and enzyme mutants, overview, the active trimeric enzyme, formed under acidic conditions, does not obey Michaelis-Menten kinetics, overview
-
additional information
additional information
-
kinetic analysis of wild-type and mutant enzymes with different substrates, detailed overview
-
additional information
additional information
-
kinetic analysis of wild-type and mutant enzymes, Mg2+ binding kinetics, overview
-
additional information
additional information
-
kinetic analysis of wild-type and mutant enzymes, Mg2+ binding kinetics, overview
-
additional information
additional information
-
kinetics and thermodynamics, detailed overview
-
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D102N
site-directed mutagenesis, the active site residue mutation does only marginally influence the pH-dependence of fluoride inhibition
D65N
site-directed mutagenesis, the active site residue mutation does only marginally influence the pH-dependence of fluoride inhibition
D67N
site-directed mutagenesis, the active site residue mutation does only marginally influence the pH-dependence of fluoride inhibition
D70N
site-directed mutagenesis, the active site residue mutation does only marginally influence the pH-dependence of fluoride inhibition
R43Q
site-directed mutagenesis, crystal structure determination and analysis and comparison to the wild-type structure
Y55F
site-directed mutagenesis, the active site residue mutation does only marginally influence the pH-dependence of fluoride inhibition
D102V
-
large decrease in metal binding affinity
D42E
-
site-directed mutagenesis, the mutant shows a decrease in affinity to the effector site and, as a consequence, kinetics of substrate hydrolysis that do not obey the Michaelis-Menten equation
D65E
-
large decrease in metal binding affinity
D70E
-
strongly decreased affinity for diphosphate
E31A
-
site-directed mutagenesis, the mutant shows a decrease in affinity to the effector site and, as a consequence, kinetics of substrate hydrolysis that do not obey the Michaelis-Menten equation
H110Q
-
catalytic activity unchanged compared to wild type enzyme
H119Q
-
catalytic activity unchanged compared to wild type enzyme
H140Q
-
variant can be dissociated in trimers, hydrolytic activity 110% of wild-type enzyme
H60Q
-
catalytic activity unchanged compared to wild type enzyme
K112Q/K115A
-
site-directed mutagenesis, the mutant shows altered kinetics and reduced activity compared to the wild-type enzyme
K112Q/K148Q
-
site-directed mutagenesis, the mutant shows altered kinetics and reduced activity compared to the wild-type enzyme
K29R
-
strongly decreased affinity for diphosphate
R43K
-
strongly decreased affinity for diphosphate
Y117F
-
same activity compared to wild type, thermostability as wild type
Y141F
-
22% relative activity compared to wild type enzyme, decreased thermostability compared to wild type
Y16F
-
same activity compared to wild type, thermostability as wild type
Y30F
-
same activity compared to wild type, thermostability as wild type
Y51F
-
64% relative activity compared to wild type enzyme, thermostability as wild type
Y57F
-
same activity compared to wild type, thermostability as wild type
Y77F
-
same activity compared to wild type, thermostability as wild type
D26A
-
site-directed mutagenesis, the mutant does not obey Michaelis-Menten kinetics
D26A
-
site-directed mutagenesis, the mutant shows a decrease in affinity to the effector site and, as a consequence, kinetics of substrate hydrolysis that do not obey the Michaelis-Menten equation
D97E
-
decreased pH-independence rates of diphosphate hydrolysis and resynthesis, destabilized EMg2(Mgdiphosphate)2 complex, raised pKa, Mg2+ binding changed
D97E
-
increases affinity for diphosphate
E145Q
-
easy formation of dimers with 5% of activity of the corresponding hexamer, 5fold increase of Kd for Mg2+ at site 2, no inhibition with high concentrations of Mg2+
E145Q
-
site-directed mutagenesis, about 80% reduced activity and altered kinetic properties compared to the wild-type enzyme
E20D
-
lower specific activity
E20D
-
large decrease in metal binding affinity
E20D
-
strongly decreased affinity for diphosphate
E31D
-
increased metal binding affinity
E31D
-
strongly decreased affinity for diphosphate
H136Q
-
variant can be dissociated in trimers, hydrolytic activity 225% of wild-type enzyme
H136Q
-
increased metal binding affinity
K112Q
-
site-directed mutagenesis, the mutant shows a decrease in affinity to the effector site and, as a consequence, kinetics of substrate hydrolysis that do not obey the Michaelis-Menten equation
K112Q
-
site-directed mutagenesis, the mutant shows altered kinetics and reduced activity compared to the wild-type enzyme
K115A
-
site-directed mutagenesis, the mutant shows altered kinetics compared to the wild-type enzyme
K115A
-
site-directed mutagenesis, the mutant shows a decrease in affinity to the effector site and, as a consequence, kinetics of substrate hydrolysis that do not obey the Michaelis-Menten equation
K148Q
-
site-directed mutagenesis, the mutant shows altered kinetics compared to the wild-type enzyme
K148Q
-
site-directed mutagenesis, the mutant shows a decrease in affinity to the effector site and, as a consequence, kinetics of substrate hydrolysis that do not obey the Michaelis-Menten equation
R43Q
-
site-directed mutagenesis, the mutant shows altered kinetics compared to the wild-type enzyme
R43Q
-
site-directed mutagenesis, the mutant shows a decrease in affinity to the effector site and, as a consequence, kinetics of substrate hydrolysis that do not obey the Michaelis-Menten equation
Y55F
-
7% relative activity compared to wild type enzyme, conformational change, thermostability as wild type
Y55F
-
increased metal binding affinity
Y55F
-
strongly decreased affinity for diphosphate
additional information
-
several mutants described that have minor effects on the binding of metal ions or diphosphate
additional information
-
metabolic profiling, sugar content of transgenic Arabidopsis thaliana plants expressing the Escherichia coli enzyme, the level of free phosphate in the leaves of transgenic plants is increased 2-3fold, and the UDP-glucose level is increased 2-6fold, but neither sucrose nor glucose levels as well as triphosphate level are unaltered, the photosynthetic activity of the mutants is reduced by 20-40% due to phosphate accumulation, overview
additional information
-
construction of a modified variant of wild type PPase with a derivative of ATP chemically attached to the amino group of Lys146
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Josse, J.; Wong, S.C.K.
Inorganic Pyrophosphatase of Escherichia coli
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
4
499-527
1971
Escherichia coli
-
brenda
Wong, S.C.K.; Hall, D.C.; Josse, J.
Constitutive inorganic pyrophosphatase of Escherichia coli. 3. Molecular weight and physical properties of the enzyme and its subunits
J. Biol. Chem.
245
4335
1970
Escherichia coli
brenda
Baykov, A.A.; Hyytiä, T.; Turkina, M.V.; Efimova, I.S.; Kasho, V.N.; Goldman, A.; Cooperman, B.S.; Lahti, R.
Functional characterization of Escherichia coli inorganic pyrophosphatase in zwitterionic buffers
Eur. J. Biochem.
260
308-317
1999
Escherichia coli
brenda
Baykov, A.A.; Dudarenkov, V.Y.; Käpylä, J.; Salminen, T.; Hyytiä, T.; Kasho, V.N.; Husgafvel, S.; Cooperman, B.S.; Goldman, A.; Lahti, R.
Dissociation of hexameric Escherichia coli inorganic pyrophosphatase into trimers on His-136 -> Gln or His-140 -> substitution and its effect on enzyme catalytic activities
J. Biol. Chem.
270
30804-30812
1995
Escherichia coli
brenda
Avaeva, S.; Kurilova, S.; Nazarova, T.; Rodina, E.; Vorobyeva, N.; Sklyankina, V.; Grigorjeva, O.; Harutyunyan, E.; Oganessyan, V.; Wilson, K.; Dauter, Z.; Huber, R.; Mather, T.
Crystal structure of Escherichia coli inorganic pyrophosphatase complexed with SO42-
FEBS Lett.
410
502-508
1997
Escherichia coli
brenda
Volk, S.E.; Dudarenkov, V.Y.; Käpylä, J.; Kasho, V.N.; Voloshina, O. A.; Salminen, T.; Goldman, A.; Lahti, R.; Baykov, A.A.; Cooperman, B.S.
Effect of E20D substitution in the active site of Escherichia coli inorganic pyrophosphatase in its quaternary structure and catalytic properties
Biochemistry
35
4662-4669
1995
Escherichia coli
brenda
Käpylä, J; Hyytiä, T.; Lahti, R.; Goldman, A.; Baykov, A.A.; Cooperman, B.S.
Effect of D97E substitution on the kinetic and thermodynamic properties of Escherichia coli inorganic pyrophosphatase
Biochemistry
34
792-800
1995
Escherichia coli
brenda
Lahti, R.; Salminen, T.; Latonen, S.; Heikinheimo, P.; Pohjanoksa, K.; Heinonen, J.
Genetic engineering of Escherichia coli inorganic pyrophosphate Tyr55 and Tyr 141 are important for the structural integrity
Eur. J. Biochem.
198
293-297
1991
Escherichia coli
brenda
Zyryanov, A.B.; Shestakov, A.S.; Lahti, R.; Baykov, A.A.
Mechanism by which metal cofactors control substrate specificity in pyrophosphatase
Biochem. J.
367
901-906
2002
Saccharomyces cerevisiae, Escherichia coli, Rattus norvegicus, Streptococcus mutans, Escherichia coli MRE 600
brenda
Hyytiae, T.; Halonen, P.; Salminen, A.; Goldman, A.; Lahti, R.; Cooperman, B.S.
Ligand binding sites in Escherichia coli inorganic pyrophosphatase: Effects of active site mutations
Biochemistry
40
4645-4653
2001
Escherichia coli
brenda
Vainonen, Y.P.; Vorobyeva, N.N.; Kurilova, S.A.; Nazarova, T.I.; Rodina, E.V.; Avaeva, S.M.
Active dimeric form of inorganic pyrophosphatase from Escherichia coli
Biochemistry
68
1195-1199
2003
Escherichia coli
brenda
Vainonen, Y.P.; Kurilova, S.A.; Avaeva, S.M.
Hexameric, trimeric, dimeric, and monomeric forms of inorganic pyrophosphatase from Escherichia coli
Russ. J. Bioorg. Chem.
28
385-391
2002
Escherichia coli
-
brenda
Vainonen, J.P.; Vorobyeva, N.N.; Rodina, E.V.; Nazarova, T.I.; Kurilova, S.A.; Skoblov, J.S.; Avaeva, S.M.
Metal-free PPi activates hydrolysis of MgPPi by an Escherichia coli inorganic pyrophosphatase
Biochemistry (Moscow)
70
69-78
2005
Escherichia coli
brenda
Lee, J.W.; Lee, D.S.; Bhoo, S.H.; Jeon, J.S.; Lee, Y.H.; Hahn, T.R.
Transgenic Arabidopsis plants expressing Escherichia coli pyrophosphatase display both altered carbon partitioning in their source leaves and reduced photosynthetic activity
Plant Cell Rep.
24
374-382
2005
Escherichia coli
brenda
Rodina, E.V.; Vorobyeva, N.N.; Kurilova, S.A.; Sitnik, T.S.; Nazarova, T.I.
ATP as effector of inorganic pyrophosphatase of Escherichia coli. The role of residue Lys112 in binding effectors
Biochemistry (Moscow)
72
100-108
2007
Escherichia coli
brenda
Sitnik, T.S.; Avaeva, S.M.
Binding of substrate at the effector site of pyrophosphatase increases the rate of its hydrolysis at the active site
Biochemistry (Moscow)
72
68-76
2007
Escherichia coli
brenda
Rodina, E.V.; Vorobyeva, N.N.; Kurilova, S.A.; Belenikin, M.S.; Fedorova, N.V.; Nazarova, T.I.
ATP as effector of inorganic pyrophosphatase of Escherichia coli. Identification of the binding site for ATP
Biochemistry (Moscow)
72
93-99
2007
Escherichia coli
brenda
Samygina, V.R.; Moiseev, V.M.; Rodina, E.V.; Vorobyeva, N.N.; Popov, A.N.; Kurilova, S.A.; Nazarova, T.I.; Avaeva, S.M.; Bartunik, H.D.
Reversible inhibition of Escherichia coli inorganic pyrophosphatase by fluoride: trapped catalytic intermediates in cryo-crystallographic studies
J. Mol. Biol.
366
1305-1317
2007
Escherichia coli (P0A7A9), Escherichia coli
brenda
Yang, L.; Liao, R.Z.; Yu, J.G.; Liu, R.Z.
DFT study on the mechanism of Escherichia coli inorganic pyrophosphatase
J. Phys. Chem. B
113
6505-6510
2009
Escherichia coli (P0A7A9), Escherichia coli
brenda
Stockbridge, R.B.; Wolfenden, R.
Enhancement of the rate of pyrophosphate hydrolysis by nonenzymatic catalysts and by inorganic pyrophosphatase
J. Biol. Chem.
286
18538-18546
2011
Escherichia coli
brenda
Li, L.; Liu, Y.; Wan, Y.; Li, Y.; Chen, X.; Zhao, W.; Wang, P.G.
Efficient enzymatic synthesis of guanosine 5'-diphosphate-sugars and derivatives
Org. Lett.
15
5528-5530
2013
Escherichia coli
brenda
Kohn, G.; Delvaux, D.; Lakaye, B.; Servais, A.C.; Scholer, G.; Fillet, M.; Elias, B.; Derochette, J.M.; Crommen, J.; Wins, P.; Bettendorff, L.
High inorganic triphosphatase activities in bacteria and mammalian cells: identification of the enzymes involved
PLoS ONE
7
e43879
2012
Escherichia coli, Escherichia coli MG1655
brenda
Pang, A.H.; Garzan, A.; Larsen, M.J.; McQuade, T.J.; Garneau-Tsodikova, S.; Tsodikov, O.V.
Discovery of allosteric and selective inhibitors of inorganic pyrophosphatase from Mycobacterium tuberculosis
ACS Chem. Biol.
11
3084-3092
2016
Escherichia coli (P0A7A9), Mycobacterium tuberculosis (Q3LIE5), Mycobacterium tuberculosis
brenda
Pratt, A.C.; Dewage, S.W.; Pang, A.H.; Biswas, T.; Barnard-Britson, S.; Cisneros, G.A.; Tsodikov, O.V.
Structural and computational dissection of the catalytic mechanism of the inorganic pyrophosphatase from Mycobacterium tuberculosis
J. Struct. Biol.
192
76-87
2015
Escherichia coli, Mycobacterium tuberculosis (P9WI55), Mycobacterium tuberculosis
brenda