Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 3.6.1.1 - inorganic diphosphatase and Organism(s) Escherichia coli and UniProt Accession P0A7A9

for references in articles please use BRENDA:EC3.6.1.1
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
     3 Hydrolases
         3.6 Acting on acid anhydrides
             3.6.1 In phosphorus-containing anhydrides
                3.6.1.1 inorganic diphosphatase
IUBMB Comments
Specificity varies with the source and with the activating metal ion. The enzyme from some sources may be identical with EC 3.1.3.1 (alkaline phosphatase) or EC 3.1.3.9 (glucose-6-phosphatase). cf. EC 7.1.3.1, H+-exporting diphosphatase.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Escherichia coli
UNIPROT: P0A7A9
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The taxonomic range for the selected organisms is: Escherichia coli
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
pyrophosphatase, inorganic pyrophosphatase, v-ppase, h+-ppase, vacuolar h(+)-pyrophosphatase, sppase, e-ppase, vacuolar h(+)-ppase, soluble inorganic pyrophosphatase, ippase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
inorganic pyrophosphatase
-
H+-PPase
-
-
-
-
inorganic diphosphatase
-
-
-
-
inorganic pyrophosphatase
PPase
pyrophosphatase
-
-
pyrophosphatase, inorganic
-
-
-
-
Pyrophosphate phospho-hydrolase
-
-
-
-
Pyrophosphate phosphohydrolase
-
-
-
-
Pyrophosphate-energized inorganic pyrophosphatase
-
-
-
-
soluble inorganic pyrophosphatase
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphorous acid anhydride hydrolysis
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -
SYSTEMATIC NAME
IUBMB Comments
diphosphate phosphohydrolase
Specificity varies with the source and with the activating metal ion. The enzyme from some sources may be identical with EC 3.1.3.1 (alkaline phosphatase) or EC 3.1.3.9 (glucose-6-phosphatase). cf. EC 7.1.3.1, H+-exporting diphosphatase.
CAS REGISTRY NUMBER
COMMENTARY hide
9024-82-2
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
diphosphate + H2O
2 phosphate
show the reaction diagram
ATP + H2O
?
show the reaction diagram
-
reaction only in the presence of Mn2+
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
tetrapolyphosphate + H2O
?
show the reaction diagram
-
-
-
-
?
triphosphate + H2O
?
show the reaction diagram
-
the enzyme is less efficient for the hydrolysis of triphosphate than for diphosphate but is the main enzyme responsible for triphosphate hydrolysis in vivo
-
-
?
tripolyphosphate + H2O
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
diphosphate + H2O
2 phosphate
show the reaction diagram
diphosphate + H2O
2 phosphate
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mn2+
binding depends highly on the pH, four ions bound per enzyme molecule, binds to the active site, binding structure, overview
lanthanum
-
results in a slow substrate binding to diphosphate
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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-benzyl-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
-
fluoride
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
Cyanate
-
-
Diazonium-1H-tetrazole
-
-
diphosphate
-
competes with ATP and methylenediphosphonate for binding at the allosteric regulatory site involving Lys112
Guanidine HCl
-
-
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
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ATP
-
ATP activates hydrolysis of MgPPi by E-PPase, molecular docking and kinetic analysis involving Lys112 and Lys115, activation mechanism, and regulatory function of ATP, modelling, overview
magnesium methylenediphosphonate
-
a non-hydrolyzable analogue, the enzyme contains an extra binding site for the substrate magnesium diphosphate or its non-hydrolyzable analogue magnesium methylenediphosphonate, binding of substrate at the effector site of pyrophosphatase increases the rate of its hydrolysis at the active site, overview
methylene diphosphate
-
noncompetitive activation of magnesium diphosphate hydrolysis
methylenebisphosphonate
-
activates the hexameric but not the dimeric form of the enzyme at pH 6
additional information
-
no activation by ADP and AMP
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.34 - 390
diphosphate
16.7
Triphosphate
-
at pH 9.1 and 25Ā°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.011
4-(azepan-1-yl)-N,N-dibutyl-6-[1-(2-phenylethyl)-1H-pyrrol-2-yl]-1,3,5-triazin-2-amine
recombinant enzyme, pH 7.5, 37Ā°C
0.0028 - 0.0358
fluoride
0.033
hydroxymethylbisphosphonate
-
pH 7.2
0.33
Methylenediphosphonate
-
pH 7.5, 25Ā°C, wild-type mutant
additional information
additional information
-
inhibition kinetics
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0002
-
with triphosphate as substrate, at pH 9.1 and 37Ā°C
13
-
crystallized enzyme
142
-
0.0025 mM substrate Mg-diphosphate, in presence of 0.0075 mM magnesium methylenediphosphonate
15
-
hexameric mutant E145Q
280
-
wild-type enzyme
360
-
0.015 mM substrate Mg-diphosphate, in presence or absence of 0.0075 mM magnesium methylenediphosphonate
82
-
0.0025 mM substrate Mg-diphosphate, in absence of magnesium methylenediphosphonate
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4
assay at, the pH heavily influences the metal binding of the enzyme, hydrolysis
8
assay at, synthesis
6.5 - 7.5
-
assay at
7.2 - 7.5
-
assay at
7.5
-
assay at
8.4
-
assay at
additional information
-
pH-dependence of wild-type and mutant activity, overview
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 9.7
-
-
7 - 11
-
20% relative activity at pH 7 and 11
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
structure comparisons of substrate-bound enzymes from Mycobacterum tuberculosis and Escherichia coli, quantum mechanics/molecular mechanics (QM/MM) analysis. Mycobacterum tuberculosis PPiase exhibits significant structural differences from the well characterized Escherichia coli PPiase in the vicinity of the bound diphosphate substrate. In Escherichia coli PPiase, Asp54 , rather than Asp89 as in Mycobacterum tuberculosis PPiase, can abstract a proton from a water molecule to activate it for a nucleophilic attack on the diphosphate substrate, catalytic reaction mechanism, and structure-function analysis, overview
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
120000
-
sedimentation equilibrium
20000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 20000, calculated from amino acid sequence
dimer
-
an active dimer can be obtained using 20% isopropanol from the native hexamer
hexamer
trimer
-
dissociated variant, SDS-PAGE
additional information
-
trimers, dimers and monomers can be obtained using isopropanol and weak acid, all forms are catalytically active with lowest activity for the monomer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
wild-type enzyme with bound fluoride trapped in an intermediate conformation, and mutant R43Q with one phosphate and four Mn2+ bound, 7-8 mg/ml protein, with 0.2 M sodium acetate, pH 5.5, using 1.5 M-1.7 M NaCl as precipitant, X-ray diffraction structure determination and analysis at 1.05-1.68 A resolution
different forms depending on the presence of NH4Cl or (NH4)2SO4 (alpha3'alpha3'')
-
purified enzyme, X-ray diffraction structure determination and analysis
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
E145Q
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
H136Q
H140Q
-
variant can be dissociated in trimers, hydrolytic activity 110% of wild-type enzyme
H60Q
-
catalytic activity unchanged compared to wild type enzyme
K112Q
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
K115A
K148Q
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
additional information
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
80
-
the enzyme activity is remarkably heat-stable (up to 80Ā°C)
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His10-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, gel filtration, tag cleavage, and again gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant expression of N-terminally His10-tagged enzyme in Escherichia coli strain BL21(DE3)
gene ppa, expression in rosette source leaf cytosol of Arabidopsis thaliana
-
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
-
an N-acetylhexosamine 1-kinase from Bifidobacterium infantis (NahK_15697), a guanosine 5'-diphosphate (GDP)-mannose pyrophosphorylase from Pyrococcus furiosus (PFManC), and an Escherichia coli inorganic pyrophosphatase (EcPpA) are used efficiently for a one-pot three enzyme synthesis of GDP-mannose, GDP-glucose, their derivatives, and GDP-talose from simple monosaccharides and derivatives in preparative scale
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
-
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
-
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team