3.6.1.1: inorganic diphosphatase
This is an abbreviated version!
For detailed information about inorganic diphosphatase, go to the full flat file.
Word Map on EC 3.6.1.1
-
3.6.1.1
-
thiamine
-
ppases
-
vacuole
-
apparatus
-
nucleoside
-
tonoplast
-
triphosphate
-
cytochemical
-
cisternae
-
h+-atpase
-
lysosome
-
magnesium
-
polyphosphate
-
glucose-6-phosphatase
-
orthophosphate
-
mung
-
rubrum
-
cytochemistry
-
rhodospirillum
-
imidodiphosphate
-
saccule
-
nudix
-
h+-pumping
-
antiporter
-
5'-nucleotidase
-
proton-pumping
-
electrogenic
-
vigna
-
acpase
-
diadenosine
-
monophosphatase
-
tripolyphosphate
-
v-type
-
diphosphonate
-
ap4a
-
chromatophores
-
dihydrate
-
tetraphosphate
-
ectonucleotide
-
exopolyphosphatase
-
vacuolar-type
-
radiata
-
phosphomonoesterase
-
autotaxin
-
osmium
-
pyrophosphate-dependent
-
n,n'-dicyclohexylcarbodiimide
-
decapping
-
pyrophosphohydrolase
-
sulfurylase
-
molecular biology
-
synthesis
- 3.6.1.1
- thiamine
- ppases
- vacuole
- apparatus
- nucleoside
-
tonoplast
- triphosphate
-
cytochemical
-
cisternae
- h+-atpase
- lysosome
- magnesium
- polyphosphate
- glucose-6-phosphatase
- orthophosphate
-
mung
- rubrum
-
cytochemistry
- rhodospirillum
- imidodiphosphate
-
saccule
-
nudix
-
h+-pumping
-
antiporter
- 5'-nucleotidase
-
proton-pumping
-
electrogenic
- vigna
- acpase
-
diadenosine
-
monophosphatase
- tripolyphosphate
-
v-type
- diphosphonate
- ap4a
-
chromatophores
-
dihydrate
- tetraphosphate
-
ectonucleotide
- exopolyphosphatase
-
vacuolar-type
- radiata
- phosphomonoesterase
- autotaxin
-
osmium
-
pyrophosphate-dependent
- n,n'-dicyclohexylcarbodiimide
-
decapping
-
pyrophosphohydrolase
-
sulfurylase
- molecular biology
- synthesis
Reaction
Synonyms
acid PPase, AT727_13205, AtPPA1, AtPPsPase1, BT2127, CBS-PPase, CBS-PPase1, chloroplast inorganic pyrophosphatase 1, class A type PPA, cobalt-dependent inorganic pyrophosphatase, CPE2055, cytosolic PPase, D1C enzyme, dhPPase, E-PPase, EcPpA, EcPPiase, ehPPase, family I inorganic pyrophosphatase, family I PPase, family I pyrophosphatase, family II inorganic pyrophosphatase, family II PPase, H+-PPase, H+-pyrophosphatase, H+-translocating/vacuolar inorganic pyrophosphatase, Hpp1 protein, HVO_0729, HvPPA, hyperthermophilic inorganic pyrophosphatase, inorganic diphosphatase, inorganic PPase, inorganic pyrophosphatase, inorganic pyrophosphatase 1, inorganic pyrophosphatase-like protein, inorganic pyrophosphorylase, IPP, IPP1, Ipp1p, IPPase, LHPPase, M-PPase, manganese-dependent inorganic pyrophosphatase, MazG, MdPPa, membrane-integral inorganic pyrophosphatase, membrane-integral pyrophosphatase, miPPase, mitochondrial pyrophosphatase, Mn2+-bound canonical Family II PPase, More, Mtb PPiase, Mthe_0236, MtPPA1, MtPPiase, nucleotide-regulated pyrophosphatase, OVP1, p26.1a, p26.1b, PfPPase, PH1907, Pho-PPase, phospholysine phosphohistidine inorganic pyrophosphate phosphatase, phosphoprotein p26.1, PPA, PPA1, PpaC, PPase, PPase 1, PPase 2, ppase-1, PPase-2, PPase1, PPase2, PPase4, PPias, PPIase, proton-translocating inorganic pyrophosphatase, PYP-1, pyrophosphatase, pyrophosphatase, inorganic, Pyrophosphate phospho-hydrolase, pyrophosphate phospho-hydrolase 1, Pyrophosphate phosphohydrolase, Pyrophosphate-energized inorganic pyrophosphatase, RmPPase, Rv3628, siPPiase, soluble inorganic pyrophosphatase, soluble inorganic pyrophosphatase 2, soluble pyrophosphatase, soluble-type yeast PPase, sPPAse, ST2226, Tc-sPPase, TC004566, TcasGA2_TC004566, TgPPase, ThPP1, Tm-PPase, TM0913, V-PPase, vacuolar H(+)-PPase, vacuolar H(+)-pyrophosphatase, vacuolar H+-pyrophosphatase, vacuolar H+-translocating inorganic pyrophosphatase, vacuolar H+-translocating pyrophosphatase, vacuolar pyrophosphatase, VHP, VP1, VSP, VVPP1
ECTree
3.6.1.1 inorganic diphosphataseAdvanced search results
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results (Substrates Products
Substrates Products on EC 3.6.1.1 - inorganic diphosphatase
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-phosphorylethanolamine + H2O
ethanolamine + phosphate
low activity
-
-
?
3'-AMP + H2O
adenosine + phosphate
-
4% activity compared to diphosphate
-
-
?
ADP + H2O
? + phosphate
-
3-6% of the activity with diphosphate
-
-
?
ADP + H2O
AMP + phosphate
-
5% activity compared to diphosphate
-
-
?
AMP + H2O
?
-
3.6% relative activity compared to diphosphate
-
-
?
ATP + H2O
? + phosphate
-
3-6% of the activity with diphosphate
-
-
?
D-fructose-6-phosphate + H2O
D-fructose + phosphate
-
13% relative activity compared to diphosphate
-
-
?
D-glucose-6-phosphate + H2O
D-glucose + phosphate
low activity
-
-
?
dATP + H2O
dADP + phosphate
7% activity compared to diphosphate
-
-
?
diphosphates + H2O
?
-
hydrolysis of organic diphosphates in the presence of Zn2+
-
-
?
imidodiphosphate + 2 H2O
2 phosphate + NH3
-
hydrolysis even in the absence of divalent cations
-
-
ir
imidodiphosphate + H2O
phosphate + phosphoramidic acid
active site and substrate binding structure determination and analysis, overview
-
-
?
ITP + H2O
? + phosphate
-
10% of the activity with diphosphate
-
-
?
polyphosphate + H2O
?
-
less than 1% activity compared to diphosphate
-
-
?
triphosphate + H2O
? + phosphate
-
3-6% of the activity with diphosphate
-
-
?
TTP + H2O
? + phosphate
-
10% of the activity with diphosphate
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
low activity
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
low activity
-
-
?
ADP + H2O
?
-
2.6% relative activity compared to diphosphate
-
-
?
ADP + H2O
?
-
18% relative activity compared to diphosphate
-
-
?
ADP + H2O
?
-
18% relative activity compared to diphosphate
-
-
?
ADP + H2O
?
hydrolyzed at 36.2% of the rate compared to diphosphate
-
-
?
ADP + H2O
?
hydrolyzed at 36.2% of the rate compared to diphosphate
-
-
?
ATP + H2O
?
-
4.2% relative activity compared to diphosphate
-
-
?
ATP + H2O
?
-
7.8% relative activity compared to diphosphate
-
-
?
ATP + H2O
?
-
7.8% relative activity compared to diphosphate
-
-
?
ATP + H2O
?
-
7.8% relative activity compared to diphosphate
-
-
?
ATP + H2O
?
hydrolyzed at 19.4% of the rate compared to diphosphate
-
-
?
ATP + H2O
?
hydrolyzed at 19.4% of the rate compared to diphosphate
-
-
?
ATP + H2O
ADP + phosphate
1% activity compared to diphosphate
-
-
?
ATP + H2O
ADP + phosphate
-
4% activity compared to diphosphate
-
-
?
cyclic tripolyphosphate + H2O
?
hydrolyzed at 32.3% of the rate compared to diphosphate
-
-
?
cyclic tripolyphosphate + H2O
?
hydrolyzed at 32.3% of the rate compared to diphosphate
-
-
?
D-glucose-1-phosphate + H2O
D-glucose + phosphate
-
15% relative activity compared to diphosphate
-
-
?
D-glucose-1-phosphate + H2O
D-glucose + phosphate
-
very weak substrate compared to diphosphate
-
-
?
diphosphate + H2O
2 phosphate
an essential and ubiquitous metal-dependent enzyme
-
-
?
diphosphate + H2O
2 phosphate
important for energy metabolism, provides energy for biosynthetic reactions
-
-
?
diphosphate + H2O
2 phosphate
AtPPsPase1 catalyzes the specific cleavage
-
-
?
diphosphate + H2O
2 phosphate
AtPPsPase1 catalyzes the specific cleavage
-
-
?
diphosphate + H2O
2 phosphate
-
the enzyme plays an essential role in the worms molting and development, and in larval survival in the host, overview
-
-
?
diphosphate + H2O
2 phosphate
-
actual substrate is magnesium diphosphate or dimagnesium diphosphate
-
-
?
diphosphate + H2O
2 phosphate
the enzyme can also catalyze the reverse reaction of diphosphate synthesis from phosphate, but this activity does not seem physiologically important
-
-
r
diphosphate + H2O
2 phosphate
in vivo function as an inorganic diphosphatase. Substrate discrimination is based, in part, on active site space restrictions imposed by the cap domain, specifically by residues Tyr76 and Glu47
-
-
?
diphosphate + H2O
2 phosphate
structure-function analysis, overview. BT2127 conserves the His23-Lys79 diad, and in both the cap-open and -closed conformations, the Asp13 side chain is in the same conformation, engaged in a hydrogen bond with linker residue Ser15
-
-
?
diphosphate + H2O
2 phosphate
in vivo function as an inorganic diphosphatase. Substrate discrimination is based, in part, on active site space restrictions imposed by the cap domain, specifically by residues Tyr76 and Glu47
-
-
?
diphosphate + H2O
2 phosphate
structure-function analysis, overview. BT2127 conserves the His23-Lys79 diad, and in both the cap-open and -closed conformations, the Asp13 side chain is in the same conformation, engaged in a hydrogen bond with linker residue Ser15
-
-
?
diphosphate + H2O
2 phosphate
-
an essential and ubiquitous metal-dependent enzyme
-
-
?
diphosphate + H2O
2 phosphate
diphosphate hydrolysis provides a thermodynamic driving force for important biosynthetic reactions, PYP-1 is required for larval development and intestinal function, overview
-
-
?
diphosphate + H2O
2 phosphate
-
actual substrate is magnesium diphosphate or dimagnesium diphosphate
-
-
?
diphosphate + H2O
2 phosphate
the enzyme can also catalyze the reverse reaction of diphosphate synthesis from phosphate, but this activity does not seem physiologically important
-
-
r
diphosphate + H2O
2 phosphate
the enzyme can also catalyze the reverse reaction of diphosphate synthesis from phosphate, but this activity does not seem physiologically important
-
-
r
diphosphate + H2O
2 phosphate
the enzyme can also catalyze the reverse reaction of diphosphate synthesis from phosphate, but this activity does not seem physiologically important
-
-
r
diphosphate + H2O
2 phosphate
-
actual substrate is magnesium diphosphate or dimagnesium diphosphate
-
-
?
diphosphate + H2O
2 phosphate
the enzyme can also catalyze the reverse reaction of diphosphate synthesis from phosphate, but this activity does not seem physiologically important
-
-
r
diphosphate + H2O
2 phosphate
-
-
209796, 209817, 209821, 209830, 654506, 654598, 654779, 657344, 667761, 685299, 685304, 685305, 719929, 735065
-
-
?
diphosphate + H2O
2 phosphate
-
reaction may be reversed by coupling to glucose-6-phosphate to 6-phospho-gluconate
-
-
?, r
diphosphate + H2O
2 phosphate
-
actual substrate is magnesium diphosphate or dimagnesium diphosphate
-
-
?
diphosphate + H2O
2 phosphate
-
important for energy metabolism, provides energy for biosynthetic reactions
-
-
?
diphosphate + H2O
2 phosphate
-
high activity with magnesium diphosphate, low activity with lanthanum diphosphate
-
-
?
diphosphate + H2O
2 phosphate
-
Lys112 is supposed to play a key role in forming contacts with the phosphate groups of the three studied effectors, overview
-
-
?
diphosphate + H2O
2 phosphate
-
residues Arg43, Lys148, and Lys115 are involved in binding of diphosphate
-
-
?
diphosphate + H2O
2 phosphate
the rate-limiting step of Mn2+-supported hydrolysis of the phosphoanhydride bond is followed by a fast release of the leaving phosphate from the P1 site, overview
Mg- or Mn-bound substrate for the synthesis reaction
-
r
diphosphate + H2O
2 phosphate
-
diphosphate in form of Mg-diphosphate
-
-
?
diphosphate + H2O
2 phosphate
-
important for energy metabolism, provides energy for biosynthetic reactions
-
-
?
diphosphate + H2O
2 phosphate
-
the enzyme is very specific for diphosphate as substrate, substrate specificity, overview
-
-
?
diphosphate + H2O
2 phosphate
-
actual substrate is magnesium diphosphate or dimagnesium diphosphate
-
-
?
diphosphate + H2O
2 phosphate
PPase plays an essential role in energy conservation and provides the energy for many biosynthetic pathways controlling the intracellular diphosphate levels
-
-
?
diphosphate + H2O
2 phosphate
diphosphate binding does not cause a significant conformational change in the diphosphate-PPase complex, structure, overview
-
-
?
diphosphate + H2O
2 phosphate
-
diphosphate in form of Mg-diphosphate
-
-
?
diphosphate + H2O
2 phosphate
-
actual substrate is magnesium diphosphate or dimagnesium diphosphate
-
-
?
diphosphate + H2O
2 phosphate
-
diphosphate in form of Mg-diphosphate
-
-
?
diphosphate + H2O
2 phosphate
-
LHPPase is associated with hyperthyroidism
-
-
?
diphosphate + H2O
2 phosphate
important for energy metabolism, provides energy for biosynthetic reactions
-
-
?
diphosphate + H2O
2 phosphate
important for energy metabolism, provides energy for biosynthetic reactions
-
-
?
diphosphate + H2O
2 phosphate
-
high specificity
-
-
?
diphosphate + H2O
2 phosphate
-
high specificity
-
-
?
diphosphate + H2O
2 phosphate
the pyrophosphatase hydrolyzes the major part of diphosphate that is produced in the acetate activation reaction
-
-
?
diphosphate + H2O
2 phosphate
the pyrophosphatase hydrolyzes the major part of diphosphate that is produced in the acetate activation reaction
-
-
?
diphosphate + H2O
2 phosphate
-
the enzyme is regulated by reversible phosphorylation, another mechanism in regulation of several physiological processes, e.g. self-incompatibility-mediated pollen tube inhibition, overview
-
-
?
diphosphate + H2O
2 phosphate
the enzyme can also catalyze the reverse reaction of diphosphate synthesis from phosphate, but this activity does not seem physiologically important
-
-
r
diphosphate + H2O
2 phosphate
an essential and ubiquitous metal-dependent enzyme
-
-
?
diphosphate + H2O
2 phosphate
development and evaluation of a phosphate-based colorimetric assay to measure progress of PCR using the PPase-coupled enzyme assay, overview
-
-
?
diphosphate + H2O
2 phosphate
the enzyme shows high specificity for diphosphate but low reactivity to sodium tripolyphosphate and sodium tetrapolyphosphate. ADP and ATP can not serve as substrates
-
-
?
diphosphate + H2O
2 phosphate
development and evaluation of a phosphate-based colorimetric assay to measure progress of PCR using the PPase-coupled enzyme assay, overview
-
-
?
diphosphate + H2O
2 phosphate
the enzyme shows high specificity for diphosphate but low reactivity to sodium tripolyphosphate and sodium tetrapolyphosphate. ADP and ATP can not serve as substrates
-
-
?
diphosphate + H2O
2 phosphate
-
important for energy metabolism, provides energy for biosynthetic reactions
-
-
?
diphosphate + H2O
2 phosphate
-
intracellular diphosphate is a by-product of multiple biosynthetic reactions and its hydrolysis by cytosolic iPPase is an important homeostatic mechanism favoring biosynthesis, overview
-
-
?
diphosphate + H2O
2 phosphate
-
actual substrate is magnesium diphosphate or dimagnesium diphosphate
-
-
?
diphosphate + H2O
2 phosphate
-
diphosphate in form of Mg-diphosphate
-
-
?
diphosphate + H2O
2 phosphate
-
diphosphate in form of Ca-diphosphate
-
-
?
diphosphate + H2O
2 phosphate
-
diphosphate in form of Co-diphosphate
-
-
?
diphosphate + H2O
2 phosphate
-
diphosphate in form of Mn-diphosphate
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
-
?
diphosphate + H2O
2 phosphate
-
high specificity with Mg2+ as cofactor
-
-
r
diphosphate + H2O
2 phosphate
-
important for energy metabolism, provides energy for biosynthetic reactions
-
-
?
diphosphate + H2O
2 phosphate
-
important for energy metabolism, provides energy for biosynthetic reactions, central enzyme of phosphorus metabolism
-
-
?
diphosphate + H2O
2 phosphate
the rate-determining step for the forward reaction with Mg2+ is hydrolysis of PPi, the wild-type active site shows a closed comformation with one of the two product phosphates already dissociated, active site residues Tyr93 and Asp115 are important, six-state catalytic mechanism, overview
in the reverse, net synthesis direction, the rate-determining step is not the condensation of the two phosphate ions but the previous step, which involves isomerization of the enzyme
-
r
diphosphate + H2O
2 phosphate
-
actual substrate is magnesium diphosphate or dimagnesium diphosphate
-
-
?
diphosphate + H2O
2 phosphate
the enzyme can also catalyze the reverse reaction of diphosphate synthesis from phosphate, but this activity does not seem physiologically important
-
-
r
diphosphate + H2O
2 phosphate
the enzyme can also catalyze the reverse reaction of diphosphate synthesis from phosphate, but this activity does not seem physiologically important
-
-
r
diphosphate + H2O
2 phosphate
the enzyme can also catalyze the reverse reaction of diphosphate synthesis from phosphate, but this activity does not seem physiologically important
-
-
r
diphosphate + H2O
2 phosphate
the enzyme can also catalyze the reverse reaction of diphosphate synthesis from phosphate, but this activity does not seem physiologically important
-
-
r
diphosphate + H2O
2 phosphate
-
important for energy metabolism, provides energy for biosynthetic reactions
-
-
?
diphosphate + H2O
2 phosphate
-
diphosphate in form of Mg-diphosphate
-
-
?
diphosphate + H2O
2 phosphate
-
actual substrate is magnesium diphosphate or dimagnesium diphosphate
-
-
?
diphosphate + H2O
2 phosphate
as far as the release of phosphate, is concerned, diphosphate, is the best substrate
-
-
?
diphosphate + H2O
2 phosphate
-
actual substrate is magnesium diphosphate or dimagnesium diphosphate
-
-
?
diphosphate + H2O
2 phosphate
as far as the release of phosphate, is concerned, diphosphate, is the best substrate
-
-
?
diphosphate + H2O
2 phosphate
an essential and ubiquitous metal-dependent enzyme
-
-
?
diphosphate + H2O
2 phosphate
pronounced specificity for diphosphate
-
-
?
diphosphate + H2O
2 phosphate
no significant proton-translocation activity can be assayed in the total membrane fractions of pTVP-transformed yeast cells. This is probably due to the fact that the activity of the hyperthermophilic enzyme is negligible below 50-55°C. Above 50°C the high passive conductance of yeast membranes to protons makes it impossible to establish a reasonable pH gradient as demonstrated with V-PPases that hydrolyze PPi at these temperatures
-
-
?
diphosphate + H2O
2 phosphate
no significant proton-translocation activity can be assayed in the total membrane fractions of pTVP-transformed yeast cells. This is probably due to the fact that the activity of the hyperthermophilic enzyme is negligible below 50-55°C. Above 50°C the high passive conductance of yeast membranes to protons makes it impossible to establish a reasonable pH gradient as demonstrated with V-PPases that hydrolyze PPi at these temperatures
-
-
?
phosphoenolpyruvate + H2O
pyruvate + phosphate
-
12% relative activity compared to diphosphate
-
-
?
phosphoenolpyruvate + H2O
pyruvate + phosphate
-
12% relative activity compared to diphosphate
-
-
?
phosphoenolpyruvate + H2O
pyruvate + phosphate
-
12% relative activity compared to diphosphate
-
-
?
phosphoenolpyruvate + H2O
pyruvate + phosphate
-
1-2% of the activity with diphosphate
-
-
?
tetrapolyphosphate + H2O
?
25.2% activity compared to the activity with diphosphate
-
-
?
tetrapolyphosphate + H2O
?
25.2% activity compared to the activity with diphosphate
-
-
?
tetrapolyphosphate + H2O
?
-
very weak substrate compared to diphosphate
-
-
?
triphosphate + H2O
?
-
the enzyme is less efficient for the hydrolysis of triphosphate than for diphosphate but is the main enzyme responsible for triphosphate hydrolysis in vivo
-
-
?
triphosphate + H2O
?
-
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
?
40.3% activity compared to the activity with diphosphate
-
-
?
tripolyphosphate + H2O
?
40.3% activity compared to the activity with diphosphate
-
-
?
tripolyphosphate + H2O
?
-
hydrolysis only with Zn2+ or Mn2+ as cofactors
-
-
?
tripolyphosphate + H2O
?
-
reaction only in the presence of Mn2+ or Zn2+
-
-
?
tripolyphosphate + H2O
?
hydrolyzed at 44.3% of the rate compared to diphosphate
-
-
?
tripolyphosphate + H2O
?
hydrolyzed at 44.3% of the rate compared to diphosphate
-
-
?
UTP + H2O
?
-
32% relative activity compared to diphosphate
-
-
?
UTP + H2O
?
-
32% relative activity compared to diphosphate
-
-
?
additional information
?
-
substrate specificity, overview. The enzyme is highly specific, no or poor activity with ribose-5-phosphate, phospho-L-serine, o-phosphocholine, phosphoenolpyruvate, L-glycerol-3-phosphate, beta-glycerol-phosphate, and phospho-L-tyrosine
-
-
?
additional information
?
-
-
substrate specificity, overview. The enzyme is highly specific, no or poor activity with ribose-5-phosphate, phospho-L-serine, o-phosphocholine, phosphoenolpyruvate, L-glycerol-3-phosphate, beta-glycerol-phosphate, and phospho-L-tyrosine
-
-
?
additional information
?
-
substrate specificity, overview. The enzyme is highly specific, no or poor activity with ribose-5-phosphate, phospho-L-serine, o-phosphocholine, phosphoenolpyruvate, L-glycerol-3-phosphate, beta-glycerol-phosphate, and phospho-L-tyrosine
-
-
?
additional information
?
-
-
enzyme may be identical with EC 3.1.3.1 or EC 3.1.3.9
-
-
?
additional information
?
-
BT2127 substrate specificity profile, overview
-
-
?
additional information
?
-
-
BT2127 substrate specificity profile, overview
-
-
?
additional information
?
-
BT2127 substrate specificity profile, overview
-
-
?
additional information
?
-
-
the enzyme is a V-type vacuolar H+-pump and responsible for phosphate uptake across the vacuolar membrane, mechanism of activation of phosphate uptake into the vacuole under low phosphate status, overview
-
-
?
additional information
?
-
-
no hydrolysis of ATP in the presence of Mg2+
-
-
?
additional information
?
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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
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no hydrolysis of ATP in the presence of Mg2+
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enzyme HvPPA drives thermodynamically unfavorable reactions to completion under conditions of reduced water activity, development of a coupled assay. HvPPA hydrolyzes the PPi by-product generated in 2 M NaCl by UbaA (a salt-loving noncanonical E1 enzyme that adenylates ubiquitin-like proteins in the presence of ATP). Malachite green assay. Significant levels of phosphate are detected when UbaA and HvPPA are coupled with ATP and SAMP1 in the reaction, phosphate is not detected when ATP, UbaA, HvPPA, or SAMP1 are omitted from the adenylation assay, and no or poor amounts of phosphate are generated enzymatically when ATP is replaced by other nucleotides (AMP, ADP, AMP-PNP, CTP, GTP, TTP, and UTP)
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enzyme HvPPA drives thermodynamically unfavorable reactions to completion under conditions of reduced water activity, development of a coupled assay. HvPPA hydrolyzes the PPi by-product generated in 2 M NaCl by UbaA (a salt-loving noncanonical E1 enzyme that adenylates ubiquitin-like proteins in the presence of ATP). Malachite green assay. Significant levels of phosphate are detected when UbaA and HvPPA are coupled with ATP and SAMP1 in the reaction, phosphate is not detected when ATP, UbaA, HvPPA, or SAMP1 are omitted from the adenylation assay, and no or poor amounts of phosphate are generated enzymatically when ATP is replaced by other nucleotides (AMP, ADP, AMP-PNP, CTP, GTP, TTP, and UTP)
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a copper(II)-based two-dimensional metal-organic framework with nanosheet structure (CuBDC NS) that possesses peroxidase (POx) mimicking activity is prepared. In the presence of H2O2, the system catalyses the oxidation of terephthalic acid to a blue-fluorescent product (excitation at 315 nm, emission at 425 nm). Diphosphate has a very strong affinity for Cu2+ ion and blocks the POx-mimicking activity of the CuBDC NS. If inorganic diphosphatase is present, the POx mimicking activity is gradually restored because diphosphate is hydrolyzed. Design and evaluation of a method for determination of inorganic pyrophosphatase activity by fluorometry, method, overview
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no activity with sodium triphosphate, ADP, ATP, and glucose-6-phosphate
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polyphosphates and ATP are not hydrolyzed
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polyphosphates and ATP are not hydrolyzed
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polyphosphates and ATP are not hydrolyzed
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XM_008360526
apple soluble inorganic diphosphatase physically interacts with S-RNases, interaction analysis by pulldown assay with recombinant MBP-tagged S1, S2, S3, S9-RNase and His6-tagged A14 expressed from Escherichia coli, overview
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apple soluble inorganic diphosphatase physically interacts with S-RNases, interaction analysis by pulldown assay with recombinant MBP-tagged S1, S2, S3, S9-RNase and His6-tagged A14 expressed from Escherichia coli, overview
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usage of the malachite green assay. The location and the conformation of the PPi in all 12 active sites are nearly identical, whereas the location and the occupancy of a Ca2+ at position M1 (most commonly coordinating both Asp57 and Asp89) as well as the conformation of the side chain of Asp89 and, to a lesser extent of Asp57, are somewhat variable among the different active sites, substrate binding structures, detailed overview
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usage of the malachite green assay. The location and the conformation of the PPi in all 12 active sites are nearly identical, whereas the location and the occupancy of a Ca2+ at position M1 (most commonly coordinating both Asp57 and Asp89) as well as the conformation of the side chain of Asp89 and, to a lesser extent of Asp57, are somewhat variable among the different active sites, substrate binding structures, detailed overview
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cytosolic phosphoproteins p26.1 from incompatible pollen show rapid, self-incompatibility-induced Ca2+-dependent hyperphosphorylation in vivo, overview
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PfPPase is capable of utilizing PPi, polyP3, and ATP as substrates
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PfPPase is capable of utilizing PPi, polyP3, and ATP as substrates
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triphosphate, ATP, and ADP are poor substrates, AMP, phosphoenolpyruvate, and 4-nitrophenyl phosphate are no substrates
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triphosphate, ATP, and ADP are poor substrates, AMP, phosphoenolpyruvate, and 4-nitrophenyl phosphate are no substrates
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triphosphate, ATP, and ADP are poor substrates, AMP, phosphoenolpyruvate, and 4-nitrophenyl phosphate are no substrates
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no hydrolysis of ATP in the presence of Mg2+
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the soluble enzyme from cattle tick Rhipicephalus microplus is capable of hydrolysing polyphosphates, molecular docking assays of RmPPase with polyphosphates, and molecular modelling, overview
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the soluble enzyme from cattle tick Rhipicephalus microplus is capable of hydrolysing polyphosphates, molecular docking assays of RmPPase with polyphosphates, and molecular modelling, overview
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the recombinant enzyme rRmPPase has a greater affinity, higher catalytic efficiency and increased cooperativity for sodium phosphate glass type 15 (polyP15) than for sodium tripolyphosphate (polyP3). Molecular docking study. PolyP3 binds close to the Mg2+ atoms in the catalytic region of the protein, participating in their coordination network, whereas polyP15 interactions involve negatively charged phosphate groups and basic amino acid residues, such as Lys56, Arg58, and Lys193. PolyP15 has a more favourable theoretical binding affinity than polyP3, thus supporting the kinetic data
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the recombinant enzyme rRmPPase has a greater affinity, higher catalytic efficiency and increased cooperativity for sodium phosphate glass type 15 (polyP15) than for sodium tripolyphosphate (polyP3). Molecular docking study. PolyP3 binds close to the Mg2+ atoms in the catalytic region of the protein, participating in their coordination network, whereas polyP15 interactions involve negatively charged phosphate groups and basic amino acid residues, such as Lys56, Arg58, and Lys193. PolyP15 has a more favourable theoretical binding affinity than polyP3, thus supporting the kinetic data
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no hydrolysis of ATP and traces of activity with tripolyphosphate in the presence of Mg2+
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active site residues are His9, Arg13, Asp15, Asp77, His99, His100, Asp151, Lys207, Arg297 and Lys298
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active site residues are His9, Arg13, Asp15, Asp77, His99, His100, Asp151, Lys207, Arg297 and Lys298
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no hydrolysis of ATP in the presence of Mg2+
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enzyme is specific for diphosphate and does not cleave nucleotide-polyphosphates
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the enzyme is possibly involved in glycoprotein biosynthesis
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the enzyme is possibly involved in glycoprotein biosynthesis
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the enzyme is possibly involved in glycoprotein biosynthesis
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dCTP, ADP, dAMP, phosphoglycolate, phosphoserine, polyphosphate, and 4-nitrophenyl phosphate are no substrates for PPase
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no activity with PAP, PAPS, 3'-CMP, fructose 1,6-bisphosphate, and D-myo-inositol 1-monophosphate
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the product of the TM0913 gene, has both nucleoside triphosphate pyrophosphohydrolase and pyrophosphatase activities
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the product of the TM0913 gene, has both nucleoside triphosphate pyrophosphohydrolase and pyrophosphatase activities
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the product of the TM0913 gene, has both nucleoside triphosphate pyrophosphohydrolase and pyrophosphatase activities
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the enzyme acts as diphosphate-dependent H+-translocation pump
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