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2-phosphorylethanolamine + H2O
ethanolamine + phosphate
low activity
-
-
?
3'-AMP + H2O
adenosine + phosphate
-
4% activity compared to diphosphate
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
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
-
-
?
ATP + H2O
ADP + phosphate
c-Jun N-terminale kinase + H2O
?
-
-
-
-
?
cyclic tripolyphosphate + H2O
?
D-fructose-6-phosphate + H2O
D-fructose + phosphate
-
13% relative activity compared to diphosphate
-
-
?
D-glucose-1-phosphate + H2O
D-glucose + phosphate
D-glucose-6-phosphate + H2O
D-glucose + phosphate
low activity
-
-
?
dATP + H2O
dADP + phosphate
7% activity compared to diphosphate
-
-
?
diphosphate + H2O
2 phosphate
diphosphate + H2O
phosphate + phosphate
diphosphates + H2O
?
-
hydrolysis of organic diphosphates in the presence of Zn2+
-
-
?
GMP + H2O
?
-
18% relative activity compared to diphosphate
-
-
?
guanosine 5'-tetraphosphate + H2O
?
-
-
-
-
?
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
-
-
?
phosphoenolpyruvate + H2O
pyruvate + phosphate
polyphosphate + H2O
?
-
less than 1% activity compared to diphosphate
-
-
?
polyphosphate 75 + H2O
?
-
-
-
-
?
polyphosphate glass type 15 + H2O
?
-
-
-
?
tetrapolyphosphate + H2O
?
thiamine diphosphate + H2O
?
triphosphate + H2O
3 phosphate
triphosphate + H2O
? + phosphate
-
3-6% of the activity with diphosphate
-
-
?
TTP + H2O
? + phosphate
-
10% of the activity with diphosphate
-
-
?
UDP-glucose + H2O
?
-
-
-
?
additional information
?
-
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
?
-
18% relative activity compared to diphosphate
-
-
?
ADP + H2O
?
-
2.7% relative activity compared to diphosphate
-
-
?
ADP + H2O
?
-
2.7% 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
?
-
3% relative activity compared to diphosphate
-
-
?
ATP + H2O
?
-
reaction only in the presence of Mn2+
-
-
?
ATP + H2O
?
-
reaction only in the presence of Mn2+
-
-
?
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
?
-
reaction only in the presence of Mn2+
-
-
?
ATP + H2O
?
-
1.3% relative activity compared to diphosphate
-
-
?
ATP + H2O
?
-
1.3% relative activity compared to diphosphate
-
-
?
ATP + H2O
?
-
hydrolysis only with Zn2+ or Mn2+ as cofactors
-
-
?
ATP + H2O
?
-
reaction only in the presence of Mn2+ or Zn2+
-
-
?
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
-
-
?
CDP + H2O
?
-
-
-
?
CTP + H2O
?
-
-
-
?
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
-
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
?
diphosphate + H2O
2 phosphate
an essential and ubiquitous metal-dependent enzyme
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
?
diphosphate + H2O
2 phosphate
important for energy metabolism, provides energy for biosynthetic reactions
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
ir
diphosphate + H2O
2 phosphate
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
?
diphosphate + H2O
2 phosphate
AtPPsPase1 catalyzes the specific cleavage
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
?
diphosphate + H2O
2 phosphate
AtPPsPase1 catalyzes the specific cleavage
-
-
?
diphosphate + H2O
2 phosphate
Aranda Christine
-
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
-
?
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
-
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
r
diphosphate + H2O
2 phosphate
-
actual substrate is magnesium diphosphate or dimagnesium diphosphate
-
-
?
diphosphate + H2O
2 phosphate
-
high specificity
-
-
?
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
-
-
-
-
?
diphosphate + H2O
2 phosphate
-
an essential and ubiquitous metal-dependent enzyme
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
?
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
-
-
-
-
?
diphosphate + H2O
2 phosphate
-
actual substrate is magnesium diphosphate or dimagnesium diphosphate
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
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
-
-
-
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
-
-
-
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
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
r
diphosphate + H2O
2 phosphate
-
-
-
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
-
-
-
r
diphosphate + H2O
2 phosphate
-
-
-
r
diphosphate + H2O
2 phosphate
-
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
-
?
diphosphate + H2O
2 phosphate
-
high specificity
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
209796, 209817, 209821, 209830, 654506, 654598, 654779, 657344, 667761, 685299, 685304, 685305, 719929, 735065 -
-
?
diphosphate + H2O
2 phosphate
-
-
-
-
r
diphosphate + H2O
2 phosphate
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
r
diphosphate + H2O
2 phosphate
-
-
-
-
r
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
-
MgPPi
-
-
?
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
-
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
-
?
diphosphate + H2O
2 phosphate
-
important for energy metabolism, provides energy for biosynthetic reactions
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
r
diphosphate + H2O
2 phosphate
-
-
-
r
diphosphate + H2O
2 phosphate
-
-
-
-
?
diphosphate + H2O
2 phosphate
-
no other substrates
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
-
?
diphosphate + H2O
2 phosphate
-
the enzyme is very specific for diphosphate as substrate, substrate specificity, overview
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
?
diphosphate + H2O
2 phosphate
-
actual substrate is magnesium diphosphate or dimagnesium diphosphate
-
-
?
diphosphate + H2O
2 phosphate
-
high specificity
-
-
?
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
-
high specificity
-
-
?
diphosphate + H2O
2 phosphate
-
diphosphate in form of Mg-diphosphate
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
?
diphosphate + H2O
2 phosphate
-
LHPPase is associated with hyperthyroidism
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
?
diphosphate + H2O
2 phosphate
important for energy metabolism, provides energy for biosynthetic reactions
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
?
diphosphate + H2O
2 phosphate
important for energy metabolism, provides energy for biosynthetic reactions
-
-
?
diphosphate + H2O
2 phosphate
XM_008360526
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
-
?
diphosphate + H2O
2 phosphate
-
high specificity
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
-
?
diphosphate + H2O
2 phosphate
-
high specificity
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
-
?
diphosphate + H2O
2 phosphate
-
high specificity
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
?
diphosphate + H2O
2 phosphate
the pyrophosphatase hydrolyzes the major part of diphosphate that is produced in the acetate activation reaction
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
?
diphosphate + H2O
2 phosphate
the pyrophosphatase hydrolyzes the major part of diphosphate that is produced in the acetate activation reaction
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
r
diphosphate + H2O
2 phosphate
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
r
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
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
?
diphosphate + H2O
2 phosphate
an essential and ubiquitous metal-dependent enzyme
-
-
?
diphosphate + H2O
2 phosphate
most specific substrate
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
-
?
diphosphate + H2O
2 phosphate
specific for
-
-
?
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
-
-
-
?
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
-
-
-
?
diphosphate + H2O
2 phosphate
specific for
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
-
?
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
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
-
?
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
-
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
-
r
diphosphate + H2O
2 phosphate
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
r
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
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
-
?
diphosphate + H2O
2 phosphate
-
high specificity
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
-
?
diphosphate + H2O
2 phosphate
-
anabolism
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
-
?
diphosphate + H2O
2 phosphate
-
high specificity
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
-
?
diphosphate + H2O
2 phosphate
-
actual substrate is magnesium diphosphate or dimagnesium diphosphate
-
-
?
diphosphate + H2O
2 phosphate
-
high specificity
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
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
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
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
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
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
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
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
-
-
-
-
?
diphosphate + H2O
2 phosphate
-
important for energy metabolism, provides energy for biosynthetic reactions
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
-
?
diphosphate + H2O
2 phosphate
-
diphosphate in form of Mg-diphosphate
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
?
diphosphate + H2O
2 phosphate
-
actual substrate is magnesium diphosphate or dimagnesium diphosphate
-
-
?
diphosphate + H2O
2 phosphate
-
high specificity
-
-
?
diphosphate + H2O
2 phosphate
as far as the release of phosphate, is concerned, diphosphate, is the best substrate
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
-
?
diphosphate + H2O
2 phosphate
-
actual substrate is magnesium diphosphate or dimagnesium diphosphate
-
-
?
diphosphate + H2O
2 phosphate
-
high specificity
-
-
?
diphosphate + H2O
2 phosphate
as far as the release of phosphate, is concerned, diphosphate, is the best substrate
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
?
diphosphate + H2O
2 phosphate
an essential and ubiquitous metal-dependent enzyme
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
?
diphosphate + H2O
2 phosphate
pronounced specificity for diphosphate
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
?
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
-
-
-
?
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
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
-
?
diphosphate + H2O
phosphate + phosphate
-
-
-
?
diphosphate + H2O
phosphate + phosphate
-
-
-
-
?
diphosphate + H2O
phosphate + phosphate
-
100% activity
-
-
?
diphosphate + H2O
phosphate + phosphate
100% activity
-
-
?
diphosphate + H2O
phosphate + phosphate
-
-
-
?
diphosphate + H2O
phosphate + phosphate
-
-
-
?
diphosphate + H2O
phosphate + phosphate
-
-
-
?
diphosphate + H2O
phosphate + phosphate
-
-
-
?
diphosphate + H2O
phosphate + phosphate
-
-
-
-
?
GDP + H2O
?
-
20% relative activity compared to diphosphate
-
-
?
GTP + H2O
?
-
-
-
?
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
?
-
-
-
-
?
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
-
-
?
thiamine diphosphate + H2O
?
low activity
-
-
?
thiamine diphosphate + H2O
?
low activity
-
-
?
triphosphate + H2O
3 phosphate
-
-
-
?
triphosphate + H2O
3 phosphate
-
-
-
-
?
triphosphate + H2O
3 phosphate
-
-
-
?
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
-
-
?
triphosphate + H2O
?
-
-
-
?
triphosphate + H2O
?
-
-
-
-
?
tripolyphosphate + H2O
?
-
-
-
-
?
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
?
-
very weak substrate compared to diphosphate
-
-
?
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
-
-
?
UTP + H2O
?
-
32% relative activity compared to diphosphate
-
-
?
UTP + H2O
?
weakest substrate
-
-
?
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
?
-
-
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
-
-
?
additional information
?
-
-
no hydrolysis of ATP in the presence of Mg2+
-
-
?
additional information
?
-
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)
-
-
-
additional information
?
-
-
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)
-
-
-
additional information
?
-
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
-
-
-
additional information
?
-
-
no activity with sodium triphosphate, ADP, ATP, and glucose-6-phosphate
-
-
?
additional information
?
-
polyphosphates and ATP are not hydrolyzed
-
-
?
additional information
?
-
-
polyphosphates and ATP are not hydrolyzed
-
-
?
additional information
?
-
polyphosphates and ATP are not hydrolyzed
-
-
?
additional information
?
-
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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
cytosolic phosphoproteins p26.1 from incompatible pollen show rapid, self-incompatibility-induced Ca2+-dependent hyperphosphorylation in vivo, overview
-
-
?
additional information
?
-
PfPPase is capable of utilizing PPi, polyP3, and ATP as substrates
-
-
-
additional information
?
-
-
PfPPase is capable of utilizing PPi, polyP3, and ATP as substrates
-
-
-
additional information
?
-
triphosphate, ATP, and ADP are poor substrates, AMP, phosphoenolpyruvate, and 4-nitrophenyl phosphate are no substrates
-
-
?
additional information
?
-
-
triphosphate, ATP, and ADP are poor substrates, AMP, phosphoenolpyruvate, and 4-nitrophenyl phosphate are no substrates
-
-
?
additional information
?
-
triphosphate, ATP, and ADP are poor substrates, AMP, phosphoenolpyruvate, and 4-nitrophenyl phosphate are no substrates
-
-
?
additional information
?
-
-
no hydrolysis of ATP in the presence of Mg2+
-
-
?
additional information
?
-
the soluble enzyme from cattle tick Rhipicephalus microplus is capable of hydrolysing polyphosphates, molecular docking assays of RmPPase with polyphosphates, and molecular modelling, overview
-
-
-
additional information
?
-
-
the soluble enzyme from cattle tick Rhipicephalus microplus is capable of hydrolysing polyphosphates, molecular docking assays of RmPPase with polyphosphates, and molecular modelling, overview
-
-
-
additional information
?
-
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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
no hydrolysis of ATP and traces of activity with tripolyphosphate in the presence of Mg2+
-
-
?
additional information
?
-
active site residues are His9, Arg13, Asp15, Asp77, His99, His100, Asp151, Lys207, Arg297 and Lys298
-
-
?
additional information
?
-
-
active site residues are His9, Arg13, Asp15, Asp77, His99, His100, Asp151, Lys207, Arg297 and Lys298
-
-
?
additional information
?
-
-
no hydrolysis of ATP in the presence of Mg2+
-
-
?
additional information
?
-
-
enzyme is specific for diphosphate and does not cleave nucleotide-polyphosphates
-
-
?
additional information
?
-
the enzyme is possibly involved in glycoprotein biosynthesis
-
-
?
additional information
?
-
-
the enzyme is possibly involved in glycoprotein biosynthesis
-
-
?
additional information
?
-
the enzyme is possibly involved in glycoprotein biosynthesis
-
-
?
additional information
?
-
dCTP, ADP, dAMP, phosphoglycolate, phosphoserine, polyphosphate, and 4-nitrophenyl phosphate are no substrates for PPase
-
-
?
additional information
?
-
-
no activity with PAP, PAPS, 3'-CMP, fructose 1,6-bisphosphate, and D-myo-inositol 1-monophosphate
-
-
?
additional information
?
-
the product of the TM0913 gene, has both nucleoside triphosphate pyrophosphohydrolase and pyrophosphatase activities
-
-
?
additional information
?
-
-
the product of the TM0913 gene, has both nucleoside triphosphate pyrophosphohydrolase and pyrophosphatase activities
-
-
?
additional information
?
-
the product of the TM0913 gene, has both nucleoside triphosphate pyrophosphohydrolase and pyrophosphatase activities
-
-
?
additional information
?
-
-
the enzyme acts as diphosphate-dependent H+-translocation pump
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
c-Jun N-terminale kinase + H2O
?
-
-
-
-
?
diphosphate + H2O
2 phosphate
polyphosphate glass type 15 + H2O
?
-
-
-
?
triphosphate + H2O
3 phosphate
additional information
?
-
diphosphate + H2O
2 phosphate
-
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
-
?
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
-
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
ir
diphosphate + H2O
2 phosphate
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
?
diphosphate + H2O
2 phosphate
Aranda Christine
-
-
-
-
?
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
-
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
?
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
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
-
an essential and ubiquitous metal-dependent enzyme
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
?
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
-
-
-
-
?
diphosphate + H2O
2 phosphate
-
actual substrate is magnesium diphosphate or dimagnesium diphosphate
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
?
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
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
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
-
-
-
r
diphosphate + H2O
2 phosphate
-
-
-
r
diphosphate + H2O
2 phosphate
-
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
-
r
diphosphate + H2O
2 phosphate
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
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
-
-
-
-
?
diphosphate + H2O
2 phosphate
-
important for energy metabolism, provides energy for biosynthetic reactions
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
r
diphosphate + H2O
2 phosphate
-
-
-
r
diphosphate + H2O
2 phosphate
-
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
?
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
-
actual substrate is magnesium diphosphate or dimagnesium diphosphate
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
?
diphosphate + H2O
2 phosphate
-
LHPPase is associated with hyperthyroidism
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
-
?
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
XM_008360526
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
-
?
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
-
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
r
diphosphate + H2O
2 phosphate
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
-
?
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
-
-
-
?
diphosphate + H2O
2 phosphate
an essential and ubiquitous metal-dependent enzyme
-
-
?
diphosphate + H2O
2 phosphate
most specific substrate
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
-
?
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
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
-
?
diphosphate + H2O
2 phosphate
-
actual substrate is magnesium diphosphate or dimagnesium diphosphate
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
-
r
diphosphate + H2O
2 phosphate
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
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
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
-
?
diphosphate + H2O
2 phosphate
-
anabolism
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
-
?
diphosphate + H2O
2 phosphate
-
actual substrate is magnesium diphosphate or dimagnesium diphosphate
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
?
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
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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 + H2O
2 phosphate
-
actual substrate is magnesium diphosphate or dimagnesium diphosphate
-
-
?
diphosphate + H2O
2 phosphate
-
actual substrate is magnesium diphosphate or dimagnesium diphosphate
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
-
?
diphosphate + H2O
2 phosphate
an essential and ubiquitous metal-dependent enzyme
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
-
?
triphosphate + H2O
3 phosphate
-
-
-
?
triphosphate + H2O
3 phosphate
-
-
-
?
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
?
-
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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
cytosolic phosphoproteins p26.1 from incompatible pollen show rapid, self-incompatibility-induced Ca2+-dependent hyperphosphorylation in vivo, overview
-
-
?
additional information
?
-
the soluble enzyme from cattle tick Rhipicephalus microplus is capable of hydrolysing polyphosphates, molecular docking assays of RmPPase with polyphosphates, and molecular modelling, overview
-
-
-
additional information
?
-
-
the soluble enzyme from cattle tick Rhipicephalus microplus is capable of hydrolysing polyphosphates, molecular docking assays of RmPPase with polyphosphates, and molecular modelling, overview
-
-
-
additional information
?
-
the enzyme is possibly involved in glycoprotein biosynthesis
-
-
?
additional information
?
-
-
the enzyme is possibly involved in glycoprotein biosynthesis
-
-
?
additional information
?
-
the enzyme is possibly involved in glycoprotein biosynthesis
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Cd2+
-
4 Cd2+ sites per subunit, enzyme activity lower compared to Mg2+
CdCl2
20 mM, 155% stimulation
lanthanum
-
results in a slow substrate binding to diphosphate
Li+
Li+ can substitute for Na+ as activator. In the presence of K+, Li+ iss a less potent activator than Na+
MgCl2
20 mM, 163% stimulation
Na+
the enzyme absolutely requires Na+ for activity, whereas both Na+ and K+ are needed for maximal activity
NH4+
activity increases more than 6fold in the presence of KCl and NH4Cl in comparison with the activity measured in the absence of any monovalent cation
NiCl2
20 mM, 156% stimulation
Ca2+
Ca2+, a strong antagonist of Mg2+ and inhibitor of all other PPases, can replace Mg2+ as activator of Mn2+-bound canonical Family II PPases, conferring about 10% of their maximal activity
Ca2+
-
hydrolysis of nucleoside triphosphates stimulated
Ca2+
-
activates at up to 1 mM, inhibits at higher concentrations, complete inhibition at 2 mM, overview
Ca2+
-
alkaline enzyme activated
Ca2+
-
most potent activator
Ca2+
Ca2+, a strong antagonist of Mg2+ and inhibitor of all other PPases, can replace Mg2+ as activator of Mn2+-bound canonical Family II PPases, conferring about 10% of their maximal activity
Ca2+
-
2% of the activity with Mg2+
Co2+
-
25% relative activity compared to Mg2+
Co2+
activates to 50% of the activity with Mg2+ at 2 mM
Co2+
-
increases hydrolysis of imidophosphate
Co2+
required, cobalt-dependent enzyme
Co2+
required, cobalt-dependent enzyme
Co2+
-
24% relative activity compared to Mg2+
Co2+
-
activation of enzyme with acid pH
Co2+
-
activates at up to 1 mM, inhibits at higher concentrations, overview
Co2+
-
60.1% of the activity with Mg2+
Co2+
-
about 20% relative activity to Mg2+ when above 3 mM
Co2+
-
protects against fluoride inhibition
Co2+
-
can partially replace Mg2+, 15%
Co2+
-
CBS-PPase requires transition metal ions, Co2+ or Mn2+, for activity
Co2+
can substitute for Mg2+ at concentrations up to 0.5 mM, inhibitory above
Co2+
-
alkaline enzyme activated
Co2+
-
supports the hydrolysis of ATP and tripolyphosphate, very weak activation of diphosphate hydrolysis
Co2+
-
6.7% relative activity compared to Mg2+, no activity in the absence of divalent cations
Co2+
-
lower activation than Mg2+
Co2+
-
88% of the activity with Mg2+
Co2+
-
about 15% activity in the presence of 50 mM Co2+ compared to 50 mM Mg2+
Co2+
Mg2+ is 72% less effective when compared with Ni2+, maximum activity occurs at 0.5 mM Co2+
Co2+
absolute requirement for divalent cations, 2.5 mM Mn2+ activates 37% compared to 2.5 mM Mg2+
Co2+
-
preferred cofactor for hydrolysis of triphosphate
Cu2+
-
activates
Cu2+
can partially, upt to 30%, substitute for Mg2+
Fe2+
activates to 88% of the activity with Mg2+ at 2 mM
Fe2+
can partially, upt to 30%, substitute for Mg2+
Fe3+
bound in in sites M1 and M2, the Fe3+:Mn2+ ratio is about 6:1 in site M1 and about 2:1 in site M2
Fe3+
activates to a lesser extent than Mg2+
K+
determination of K+-binding sites
K+
activity increases more than 6fold in the presence of KCl and NH4Cl in comparison with the activity measured in the absence of any monovalent cation
K+
the enzyme absolutely requires Na+ for activity, whereas both Na+ and K+ are needed for maximal activity
K+
-
required, highly activating
Mg2+
-
maximum activity
Mg2+
-
required for activity
Mg2+
activates, Mg2+ is the highly preferred cofactor for family I sPPases
Mg2+
dependent on, can be partially substituted by Mn2+, both isozymes show similar catalytic constants and affinities for the Mg-pyrophosphate complex, while differed in their affinity for free Mg2+,
Mg2+
-
magnesium ions confer the highest activity
Mg2+
required, natural cofactor of AtPPA1, metal coordination and binding site
Mg2+
Aranda Christine
-
required for activity and stability
Mg2+
Aranda Christine
-
no other divalent cations can substitute for Mg2+
Mg2+
-
free Mg2+ ions are not required
Mg2+
required, functions in catalysis and binding structure, overview
Mg2+
-
activates, Mg2+ is the preferred cofactor for family I sPPases
Mg2+
-
increases hydrolysis of imidophosphate
Mg2+
-
or other divalent cation required for hydrolysis of diphosphate
Mg2+
-
required for activity
Mg2+
-
no other divalent cations can substitute for Mg2+
Mg2+
required, best divalent cation
Mg2+
-
required for activity
Mg2+
-
required for activity
Mg2+
-
no other divalent cations can substitute for Mg2+
Mg2+
-
maximum activation compared to other divalent ion activators
Mg2+
-
activation of enzyme with alkaline pH
Mg2+
-
required for activity and stability
Mg2+
-
wild type: two Mg2+ ions per active site required for catalysis
Mg2+
-
stabilization of the hexameric E20D enzyme
Mg2+
-
four Mg2+ ions per active site required for catalysis
Mg2+
-
required, inhibitory for the native hexamer above 5 mM, no inhibition of the dimeric form
Mg2+
-
required, three binding sites in the absence of substrate
Mg2+
-
required, substrate is magnesium diphoshate
Mg2+
binding depends highly on the pH, binds to the active site, binding structure, overview
Mg2+
-
dependent on, activates, bound to the substrate as magnesium diphosphate
Mg2+
-
dependent on, bound to the enzyme
Mg2+
dependent on, the active site contains four Mg2+ ions
Mg2+
-
required, one of the three active site Mg2+ ions is bound along with phosphate
Mg2+
dependent on, Mg2+ concentration-dependence of kinetic cooperativity in wild-type ehPPase and mutant S213N-ehPPase, overview
Mg2+
metal-binding protein
Mg2+
-
7-8fold activation
Mg2+
-
activates by decreasing the value of the Michaelis-Menten constant, dependent on, highest activity at pH 7.4 and 5.0 mM, Mg2+ shifts the pH optimum, Mg2+ associates rather weakly with the pyrophosphatase active center and can be readily displaced by Ca2+ , overview
Mg2+
requires Mg2+ or Mn2+, Km at 25°C and pH 8.5 is 13.4 mM. Sigmoidal kinetic profiles indicative of positive cooperative binding are detected for Mg2+
Mg2+
-
required, best divalent cation, binding site structure
Mg2+
dependent on, other divalent cations substituted poorly for Mg2+
Mg2+
required, binds to diphosphate, effects on enzyme activity and kinetics, pH-dependence, overview
Mg2+
-
required for activity
Mg2+
required, optimal at 5 mM
Mg2+
-
most effetive divalent cation, can partially be replaced by other divalent cations
Mg2+
-
maximum activity at 3 mM
Mg2+
much less effective than Ca2+, 20% of the activity with Ca2+
Mg2+
required, metal coordination and binding site
Mg2+
-
required for activity
Mg2+
required for catalysis
Mg2+
the activity of the enzyme is strongly dependent on Mg2+. High enzyme activity is found between 1 and 100 mM Mg2+ with a maximum activity at 10 mM. At pH 7.5, the maximum PPase activity is at 50 mM Mg2+
Mg2+
-
required for activity and stability
Mg2+
-
no other divalent cations can substitute for Mg2+
Mg2+
-
activity enhanced of the mitochondrial enzyme
Mg2+
-
dependent on, cannot be substituted by Mn2+ or Ca2+
Mg2+
activates, Mg2+ is the highly preferred cofactor for family I sPPases
Mg2+
required, best divalent cation, 5 mM, Km is 0.303 mM
Mg2+
maximum activity in the presence of Mg2+, influence of other metal cations is negligible
Mg2+
-
activation of enzyme with alkaline pH
Mg2+
-
alkaline enzyme activated
Mg2+
-
maximum activation at 4 mM
Mg2+
-
no other divalent cations can substitute for Mg2+
Mg2+
required, family I diphosphatases are Mg2+-dependent, activates
Mg2+
-
required for activity
Mg2+
-
required for activity
Mg2+
-
maximum activation compared to other divalent ion activators
Mg2+
-
required, serves as physiological cofactor
Mg2+
the pyrophosphatase requires four divalent metal cations for catalysis, magnesium provides the highest activity
Mg2+
-
required for activity
Mg2+
-
no other divalent cations can substitute for Mg2+
Mg2+
-
the enzyme utilizes Mn2+ over Mg2+ for activity
Mg2+
-
required for activity
Mg2+
-
no other divalent cations can substitute for Mg2+
Mg2+
-
required for activity
Mg2+
-
no other divalent cations can substitute for Mg2+
Mg2+
binding structure, overview
Mg2+
the enzyme requires divalent cations, 5 mM
Mg2+
-
required for activity
Mg2+
-
required for activity
Mg2+
one Mg2+ per active site
Mg2+
-
preferred divalent cation, Km value 0.9 mM
Mg2+
-
no other divalent cations can substitute for Mg2+
Mg2+
activates, Mg2+ is the highly preferred cofactor for family I sPPases
Mg2+
-
maximal activity in the presence of 0.2 mM Mg2+
Mg2+
Mg2+ is 9% less effective when compared with Ni2+, maximum activity occurs at 2 mM Mg2+
Mg2+
absolute requirement for divalent cations for catalytic action, Mg2 + (2.5 mM) conferring the highest activity. KM for Mg2+ is approximately 1.7 mM
Mg2+
the enzyme shows maximal activity with magnesium pyrophosphate, the physiological substrate of the protein. The enzyme strongly binds magnesium ions to acquire the right conformation and that it is isolated in a stable magnesium-containing form, unless cations are removed by a harsh treatment with a potent chelator
Mg2+
-
required, the active site of TgPPase contains two bound Mg2+ ions. One Mg2+ is bound at M1 site coordinated by Asp190, Asp195, and Asp227. The Mg2+ is bound to protein in M2 site predominantly through water molecules and Asp195. The observed conformation in the active site represents a state where both phosphates have already dissociated
Mg2+
-
preferred cofactor for the hydrolysis of diphosphate, highest stimulation of activity at about 0.5 mM
Mg2+
-
required for activity
Mg2+
-
preferred by family I PPase, 20 mM
Mg2+
-
required for activity
Mn2+
-
10.6% relative activity compared to Mg2+
Mn2+
can partially substitute for Mg2+
Mn2+
activates to 39% of the activity with Mg2+ at 2 mM
Mn2+
-
conversion of the enzyme from inactive dimer to active trimer
Mn2+
bound in in sites M1 and M2, the Fe3+:Mn2+ ratio is about 6:1 in site M1 and about 2:1 in site M2
Mn2+
required, a Mn2+-bound canonical Family II PPase
Mn2+
-
increases hydrolysis of imidophosphate
Mn2+
can partially, upt to 30%, substitute for Mg2+
Mn2+
-
can partially replace Mg2+
Mn2+
-
supports the hydrolysis of ATP and tripolyphosphate, very weak activation of diphosphate hydrolysis
Mn2+
binding depends highly on the pH, four ions bound per enzyme molecule, binds to the active site, binding structure, overview
Mn2+
-
activates at up to 1 mM, inhibits at higher concentrations, overview
Mn2+
requires Mg2+ or Mn2+
Mn2+
-
32.8% of the activity with Mg2+
Mn2+
-
protects against fluoride inhibition
Mn2+
-
CBS-PPase requires transition metal ions, Co2+ or Mn2+, for activity
Mn2+
substitution of Mg2+ cations with Mn2+ results in significantly lower activity of 25.34% of the Mg2+-induced activity
Mn2+
activates to a lesser extent than Mg2+
Mn2+
can substitute for Mg2+ at concentrations up to 0.5 mM, inhibitory above
Mn2+
-
supports the hydrolysis of ATP and tripolyphosphate, very weak activation of diphosphate hydrolysis
Mn2+
-
can partially replace for Mg2+
Mn2+
-
supports the hydrolysis of ATP and tripolyphosphate, very weak activation of diphosphate hydrolysis
Mn2+
-
7.3% relative activity compared to Mg2+, no activity in the absence of divalent cations
Mn2+
-
Mn2+ ions influence the activity, temperature dependence, and thermostability of the enzyme and are required to function in cold environments
Mn2+
-
the enzyme utilizes Mn2+ over Mg2+ for activity, Mn2+ activation increases the enzyme's activity at low temperatures
Mn2+
dependent on, the active site contains two catalytic Mn2+ binding sites
Mn2+
required, a Mn2+-bound canonical Family II PPase
Mn2+
required, a Mn2+-bound canonical Family II PPase
Mn2+
the enzyme requires divalent cations
Mn2+
required, activates at 2 mM
Mn2+
required, a Mn2+-bound canonical Family II PPase
Mn2+
-
lower activation than Mg2+
Mn2+
-
32% of the activity with Mg2+
Mn2+
absolute requirement for divalent cations, 2.5 mM Mn2+ activates 17% compared to 2.5 mM Mg2+
Mn2+
-
required for activity
Mn2+
-
preferred by family II PPase, 50 mM
NaCl
the enzyme is fully active up to 3 M
NaCl
NaCl produces a slight increase in activity
Ni2+
activates to 83% of the activity with Mg2+ at 2 mM
Ni2+
activates to a lesser extent than Mg2+
Ni2+
-
3% of the activity with Mg2+
Ni2+
dependent on, divalent metal cation with highest efficiency on enzymatic activity, maximum activity occurs at 0.5 mM Ni2+
Zn2+
about the same activation as with Mg2+
Zn2+
can partially, upt to 30%, substitute for Mg2+
Zn2+
-
highly activates at up to 1 mM, inhibits at higher concentrations, overview
Zn2+
substitution of Mg2+ cations with Zn2+ results in significantly lower activity of 14.3% of the Mg2+-induced activity
Zn2+
stimulates, Zn2+ is the preferred co-factor for hydrolysis of polyP3 and ATP
Zn2+
can substitute for Mg2+ at concentrations up to 0.5 mM, inhibitory above
Zn2+
-
alkaline enzyme activated
Zn2+
-
required for activity
Zn2+
-
required for activity
Zn2+
-
required for activity
Zn2+
-
higher activation than Co2+, Mn2+
Zn2+
-
supports the hydrolysis of ATP and tripolyphosphate, very weak activation of diphosphate hydrolysis
Zn2+
-
95% of the activity with Mg2+
Zn2+
13% of the activity with Mg2+
Zn2+
absolute requirement for divalent cations, 2.5 mM Mn2+ activates 21% compared to 2.5 mM Mg2+
Zn2+
-
preferred cofactor for hydrolysis of polyphosphate 75
additional information
the enzyme is absolutely dependent on divalent cations, poor activity with Mn2+, Cu2+, Fe2+, Zn2+, and Co2+
additional information
the enzyme contains a unique trinuclear metal center, detailed structure analysis, overview. Mn2+ and Fe3+ do not exchange for Mg2+ even in the presence of a large excess of Mg2+
additional information
soluble Family II PPase enzymes require both magnesium and a transition metal ion (manganese or cobalt) for maximal activity and are the most active among all PPase types. Catalysis by the enzyme requires four metal ions per substrate molecule, three of which form a unique trimetal center that coordinates the nucleophilic water and converts it to a reactive hydroxide ion. One or two additional sites that bind Mn2+ and Mg2+ with millimolar affinities have been detected in canonical Family II PPases of Bacillus subtilis. An additional Mg2+ ion is brought to the enzyme as part of a Mg-phosphate complex, the true substrate. In the cell, Mg2+ ions appear to occupy all sites except that containing a transition metal ion
additional information
the metal binding residues are Asp171, Asn172, and Glu47
additional information
-
the metal binding residues are Asp171, Asn172, and Glu47
additional information
-
the enzyme is absolutely dependent on divalent cations
additional information
soluble Family II PPase enzymes require both magnesium and a transition metal ion (manganese or cobalt) for maximal activity and are the most active among all PPase types. Catalysis by the enzyme requires four metal ions per substrate molecule, three of which form a unique trimetal center that coordinates the nucleophilic water and converts it to a reactive hydroxide ion
additional information
soluble Family II PPase enzymes require both magnesium and a transition metal ion (manganese or cobalt) for maximal activity and are the most active among all PPase types. Catalysis by the enzyme requires four metal ions per substrate molecule, three of which form a unique trimetal center that coordinates the nucleophilic water and converts it to a reactive hydroxide ion
additional information
-
no divalent cations required for activity
additional information
no effect by Ca2+, Cd2+, and Ni2+
additional information
-
no effect by Ca2+, Cd2+, and Ni2+
additional information
-
no divalent cations required for activity
additional information
-
no effect by Ca2+, Cu2+, and Fe2+
additional information
other metal ions can partially replace Ca+, activation decreases in the order Ca2+> Cu2+> Mn2+> Fe2+> Mg2+> Zn2+> Co2+
additional information
-
other metal ions can partially replace Ca+, activation decreases in the order Ca2+> Cu2+> Mn2+> Fe2+> Mg2+> Zn2+> Co2+
additional information
the enzyme activity depends on Mg2+. Other divalent cations such as Co2+, Zn2+ and Mn2+ stimulate diphosphate hydrolysis but with lower efficiency. The relative PfPPase diphosphate activity confers by divalent metal ions fell in the descending order Mg2+, Co2+ and Zn2+, Mn2+. But Zn2+ is the preferred cofactor for hydrolysis of polyP3 and ATP
additional information
-
the enzyme activity depends on Mg2+. Other divalent cations such as Co2+, Zn2+ and Mn2+ stimulate diphosphate hydrolysis but with lower efficiency. The relative PfPPase diphosphate activity confers by divalent metal ions fell in the descending order Mg2+, Co2+ and Zn2+, Mn2+. But Zn2+ is the preferred cofactor for hydrolysis of polyP3 and ATP
additional information
the enzyme is absolutely dependent on divalent cations, poor activity with Mn2+, Cu2+, Fe2+, Zn2+, and Co2+
additional information
not activated by Zn2+
additional information
no activation by Ni2+
additional information
-
no activation by Ni2+
additional information
no effect on activity by Mn2+ and Zn2+
additional information
-
no effect on activity by Mn2+ and Zn2+
additional information
-
no activity in the absence of divalent cations
additional information
soluble Family II PPase enzymes require both magnesium and a transition metal ion (manganese or cobalt) for maximal activity and are the most active among all PPase types. Catalysis by the enzyme requires four metal ions per substrate molecule, three of which form a unique trimetal center that coordinates the nucleophilic water and converts it to a reactive hydroxide ion
additional information
soluble Family II PPase enzymes require both magnesium and a transition metal ion (manganese or cobalt) for maximal activity and are the most active among all PPase types. Catalysis by the enzyme requires four metal ions per substrate molecule, three of which form a unique trimetal center that coordinates the nucleophilic water and converts it to a reactive hydroxide ion
additional information
soluble Family II PPase enzymes require both magnesium and a transition metal ion (manganese or cobalt) for maximal activity and are the most active among all PPase types. Catalysis by s requires four metal ions per substrate molecule, three of which form a unique trimetal center that coordinates the nucleophilic water and converts it to a reactive hydroxide ion. One or two additional sites that bind Mn2+ and Mg2+ with millimolar affinities have been detected in canonical Family II PPases of Streptococcus gordonii. An additional Mg2+ ion is brought to the enzyme as part of a Mg-phosphate complex, the true substrate. In the cell, Mg2+ ions appear to occupy all sites except that containing a transition metal ion
additional information
-
no divalent cation required
additional information
-
divalent cation required. Activity in decreasing order: Mg2+, Zn2+, Co2+, Mn2+, Ni2+, Ca2+
additional information
divalent cations are not essential for the acid PPase activity
additional information
the enzyme is absolutely dependent on divalent cations, poor activity with Mn2+, Cu2+, Fe2+, and Co2+
additional information
little or no activity is observed in the presence of Cu2+, Zn2+, Ca2+, or Mn2+
additional information
-
not affected by 50 mM Mn2+, Ni2+, Ca2+, Zn2+, and Cu2+
additional information
PPase has an absolute dependence on divalent metal cations because no measurable activity is observed in their absence
additional information
-
the enzyme retains measurable activity up to 0.7-0.8 M NaCl, KCl, or NH4Cl
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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)
1,1,1,1-azodimethyl diamide
-
-
1-(2-phenylethyl)-1H-pyrrole
1-(3,5-dimethylphenyl)-1H-pyrrole
1-(3-phenylpropyl)-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
2,4,6-Trinitrobenzenesulfonic acid
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
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-(3-(3-(3-chlorophenyl)pyrrolidin-1-yl)-1,2,4-triazin-5-yl)aniline
-
3-(3-(3-(benzyloxy)phenyl)pyrrolidin-1-yl)-5-(5-methylfuran-2-yl)-1,2,4-triazine
-
3-(3-(3-chlorophenyl)pyrrolidin-1-yl)-5-(3,4-dimethoxyphenyl)-1,2,4-triazine
-
3-(3-(3-chlorophenyl)pyrrolidin-1-yl)-5-(3-nitrophenyl)-1,2,4-triazine
-
3-(3-(3-chlorophenyl)pyrrolidin-1-yl)-5-(5-(2-(trifluoromethyl)phenyl)furan-2-yl)-1,2,4-triazine
-
3-(3-(3-chlorophenyl)pyrrolidin-1-yl)-5-phenyl-1,2,4-triazine
-
3-(butylsulfanyl)-6-(5-methylfuran-2-yl)-6,7-dihydro[1,2,4]triazino[5,6-d][3,1]benzoxazepine
3-[3-(3-chlorophenyl)pyrrolidin-1-yl]-5-(5-methylfuran-2-yl)-1,2,4-triazine
-
4-(1-benzyl-1H-pyrrol-2-yl)-N,N-dibutyl-6-chloro-1,3,5-triazin-2-amine
4-(3-(3-(3-chlorophenyl)pyrrolidin-1-yl)-1,2,4-triazin-5-yl)aniline
-
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
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-(4-bromophenyl)-3-(3-(3-chlorophenyl)pyrrolidin-1-yl)-1,2,4-triazine
-
5-(5-methylfuran-2-yl)-3-(3-(3-(trifluoromethyl)phenyl)pyrrolidin-1-yl)-1,2,4-triazine
-
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
7-Chloro-4-nitrobenzo-2-oxa-1,3-diazole
-
-
alpha,beta-methyleneadenosine triphosphate
cannot be hydrolyzed and blocks both NTPase and pyrophosphatase activities
aminomethylenediphosphonate
Ca2+-diphosphate
-
nonhydrolyzable substrate analogue
cAMP
-
58% inhibition at 0.1 mM
CDP
-
50% inhibition at 0.1 mM
D-glucose
-
non-competitive
D-Glucose-6-phosphate
-
competitive
Diazonium-1H-tetrazole
-
-
dipropan-2-yl [(E)-(2-benzoylhydrazinylidene)(hydroxyamino)methyl]phosphonate
free divalent cations
-
-
-
fructose-1,6-bisphosphate
-
-
GDP
-
19% inhibition at 0.1 mM
GMP
-
18% inhibition at 0.1 mM
GSH
activates up to 4 mM, and inhibits at higher concentrations
Guanidine nucleotides
-
-
-
hydroxymethylbisphosphonate
-
competitive with diphosphate
imidodiphosphoric acid
a nonhydrolyzable PPi analogue, inhibits by 50% at 2 mM
L-malate
-
allosteric mechanism
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
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
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
p-chloromercuribenzenesulfonic acid
-
-
p-chloromercuriphenyl sulfonate
-
50% inhibition of hydrolysis of diphosphate at 25 µM
phenylmercuric acetate
-
-
phenylmethanesulfonyl fluoride
-
-
Sodium fluoride
inhibition kinetics
UDP
-
35% inhibition at 0.1 mM
[1,1'-biphenyl]-2,2'-dicarbonitrile
1,1'-[6-(1-phenyl-1H-pyrrol-2-yl)-1,3,5-triazine-2,4-diyl]bis(azepane)
-
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)
-
1,1'-[6-[1-(3,5-dimethylphenyl)-1H-pyrrol-2-yl]-1,3,5-triazine-2,4-diyl]bis(azepane)
-
1-(2-phenylethyl)-1H-pyrrole
-
1-(2-phenylethyl)-1H-pyrrole
-
1-(3,5-dimethylphenyl)-1H-pyrrole
-
1-(3,5-dimethylphenyl)-1H-pyrrole
-
1-(3-phenylpropyl)-1H-pyrrole
-
1-(3-phenylpropyl)-1H-pyrrole
-
1-benzyl-1H-pyrrole
-
1-cyclohexyl-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-(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
-
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
-
10-bromo-3-(butylsulfanyl)-6-(thiophen-2-yl)-6,7-dihydro[1,2,4]triazino[5,6-d][3,1]benzoxazepine
-
2,4,6-Trinitrobenzenesulfonic acid
-
-
2,4,6-Trinitrobenzenesulfonic acid
-
-
2,4,6-Trinitrobenzenesulfonic acid
-
-
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-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(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(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-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-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-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-(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-(3,5-dimethylphenyl)-1H-pyrrol-2-yl]-1,3,5-triazine
-
2,4-dichloro-6-[1-(3-phenylpropyl)-1H-pyrrol-2-yl]-1,3,5-triazine
-
2,4-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-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(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-(1-phenyl-1H-pyrrol-2-yl)-4,6-di(pyrrolidin-1-yl)-1,3,5-triazine
-
2-chloro-4-(methanesulfonyl)benzoic acid
-
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-methyl-4-(3-phenyl[1,2,4]triazolo[3,4-b][1,3,4]thiadiazol-6-yl)quinoline
-
2-phosphoglyceric acid
-
in the absence of free Mg2+
2-phosphoglyceric acid
-
in the absence of free Mg2+
2-phosphoglyceric acid
-
in the absence of free Mg2+
2-[(5-cyanopyridin-2-yl)(methyl)amino]ethyl 4-methyl-1,2,3-thiadiazole-5-carboxylate
-
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
-
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
-
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-(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)-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-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-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-(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-(3,5-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-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-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-(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
-
4-chloro-N,N-dihexyl-6-(1-phenyl-1H-pyrrol-2-yl)-1,3,5-triazin-2-amine
-
4-hydroxymercuribenzoate
-
-
4-hydroxymercuribenzoate
-
-
4-hydroxymercuribenzoate
-
-
5-bromo-1,3-dimethylpyrimidine-2,4(1H,3H)-dione
-
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-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
-
6-(1-phenyl-1H-pyrrol-2-yl)-1,3,5-triazine-2,4-diamine
-
adenine nucleotide
a quarter of Family II PPases contain an autoinhibitory regulatory insert formed by two cystathionine beta-synthase (CBS) domains and one DRTGG domain. Adenine nucleotide binding either activates or inhibits the CBS domain-containing PPases, thereby tuning their activity and, hence, diphosphate levels, in response to changes in cell energy status (ATP/ADP ratio)
adenine nucleotide
a quarter of Family II PPases contain an autoinhibitory regulatory insert formed by two cystathionine beta-synthase (CBS) domains and one DRTGG domain. Adenine nucleotide binding either activates or inhibits the CBS domain-containing PPases, thereby tuning their activity and, hence, diphosphate levels, in response to changes in cell energy status (ATP/ADP ratio)
adenine nucleotide
a quarter of Family II PPases contain an autoinhibitory regulatory insert formed by two cystathionine beta-synthase (CBS) domains and one DRTGG domain. Adenine nucleotide binding either activates or inhibits the CBS domain-containing PPases, thereby tuning their activity and, hence, diphosphate levels, in response to changes in cell energy status (ATP/ADP ratio)
adenine nucleotide
a quarter of Family II PPases contain an autoinhibitory regulatory insert formed by two cystathionine beta-synthase (CBS) domains and one DRTGG domain. Adenine nucleotide binding either activates or inhibits the CBS domain-containing PPases, thereby tuning their activity and, hence, diphosphate levels, in response to changes in cell energy status (ATP/ADP ratio)
adenine nucleotide
a quarter of Family II PPases contain an autoinhibitory regulatory insert formed by two cystathionine beta-synthase (CBS) domains and one DRTGG domain. Adenine nucleotide binding either activates or inhibits the CBS domain-containing PPases, thereby tuning their activity and, hence, diphosphate levels, in response to changes in cell energy status (ATP/ADP ratio)
adenine nucleotide
a quarter of Family II PPases contain an autoinhibitory regulatory insert formed by two cystathionine beta-synthase (CBS) domains and one DRTGG domain. Adenine nucleotide binding either activates or inhibits the CBS domain-containing PPases, thereby tuning their activity and, hence, diphosphate levels, in response to changes in cell energy status (ATP/ADP ratio)
ADP
-
ADP
allosteric inhibition
ADP
-
partially inhibited
ADP
-
complete inhibition at 0.1 mM
aminomethylenediphosphonate
-
-
aminomethylenediphosphonate
-
-
AMP
the structures of the CBSPPase regulatory part contain AMP or diadenosine tetraphosphate (Ap4A) bound to the CBS domains in different modes. AMP is bound in each monomeric unit at the interface between its CBS domains, whereas one Ap4A molecule occupies both AMP-binding sites. The conformational states of the AMP- and Ap4A-bound CBS modules are significantly different, explaining the different effects of the nucleotides on enzyme activity
AMP
allosteric inhibition
AMP
the structures of the CBSPPase regulatory part contain AMP or diadenosine tetraphosphate (Ap4A) bound to the CBS domains in different modes. AMP is bound in each monomeric unit at the interface between its CBS domains, whereas one Ap4A molecule occupies both AMP-binding sites. The conformational states of the AMP- and Ap4A-bound CBS modules are significantly different, explaining the different effects of the nucleotides on enzyme activity
AMP
-
partially inhibited
AMP
-
96% inhibition at 0.1 mM
ATP
-
competes with methylenediphosphonate and diphosphate for binding at the allosteric regulatory site involving Lys112
ATP
50% inhibition at 2 mM, 90% at 3 mM ATP
ATP
-
partially inhibited
Ca2+
-
Ca2+
Aranda Christine
-
most effective inhibitor among the cations tested
Ca2+
-
activates at up to 1 mM, inhibits at higher concentrations, complete inhibition at 2 mM, overview
Ca2+
over 90% inhibition at 0.12 mM; over 90% inhibition at 0.12 mM
Ca2+
complete inhibition at 42 mM
Ca2+
enzymatic activity is inhibited more than 95% in the presence of 5 mM Ca2+
Ca2+
-
inhibits sPPase activity of the enzyme, 62% inhibition of p26.1a, 49% of p26.1b
Ca2+
-
less effective than Cd2+
Ca2+
-
50% at 0.012 mM: Mg2+ 0.4 mM
Ca2+
-
50% inhibition at 0.1 mM, no effect at physiological concentrations
Ca2+
inhibits the cleavage of diphosphate in the presence of 2.5 mM Mg2+. 0.01 mM CaCl2 inhibits the enzyme by about 50%
Cd2+
Aranda Christine
-
-
Co2+
Aranda Christine
-
-
Co2+
-
activates at up to 1 mM, inhibits at higher concentrations, overview
Co2+
can substitute for Mg2+ at concentrations up to 0.5 mM, inhibitory above
Co2+
-
less effective than Ca2+
Cu2+
-
Cu2+
-
less effective then Mn2+
diphosphate
high substrate inhibition at low levels of Mg2+
diphosphate
-
hydrolysis of imidophosphate competitively inhibited in the absence of divalent cations
diphosphate
-
competes with ATP and methylenediphosphonate for binding at the allosteric regulatory site involving Lys112
dipropan-2-yl [(E)-(2-benzoylhydrazinylidene)(hydroxyamino)methyl]phosphonate
-
dipropan-2-yl [(E)-(2-benzoylhydrazinylidene)(hydroxyamino)methyl]phosphonate
-
EDTA
-
EDTA
Aranda Christine
-
-
EDTA
-
Na2SO4, Li2SO4 enhance deactivation, Mn2+ is protective
EDTA
-
89% activation at 0.9 mM, complete inhibition at 5 mM
EDTA
enzymatic activity is inhibited more than 70% in the presence of 5 mM EDTA
F-
Aranda Christine
-
-
F-
-
Co2+ and Mn2+ protect against fluoride inhibition
fluoride
inhibition of wild-type and mutant enzyme
fluoride
inhibits Family I PPases at micromolar concentrations by replacing the nucleophilic water molecule. The effect of fluoride on Family II enzymes strongly depends on the metal cofactor in the tight binding site. Mn/Co enzymes are inhibited weakly by fluoride, but if the transition metal is replaced by Mg2+, fluoride binds 1000times tighter, achieving an affinity characteristic of Family I enzymes
fluoride
reversible inhibition, binds to the active site, binding structure, overview
fluoride
-
50% inhibition at 0.5 mM, 70-80% at 1.0 mM
fluoride
potent inhibition, IC50: 0.1 mM
fluoride
inhibits Family I PPases at micromolar concentrations by replacing the nucleophilic water molecule. The effect of fluoride on Family II enzymes strongly depends on the metal cofactor in the tight binding site. Mn/Co enzymes are inhibited weakly by fluoride, but if the transition metal is replaced by Mg2+, fluoride binds 1000times tighter, achieving an affinity characteristic of Family I enzymes
Guanidine HCl
-
-
Hg2+
-
Imidodiphosphate
-
-
iodoacetamide
-
-
iodoacetate
-
-
KF
-
90% at 0.5 mM
methyl 2-(4-methoxyphenyl)-3-methyl-4-oxo-3,4-dihydro[1]benzopyrano[3,4-b]pyrrole-1-carboxylate
-
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-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
-
methyl 3-benzyl-2-(4-methoxyphenyl)-4-oxo-3,4-dihydro[1]benzopyrano[3,4-b]pyrrole-1-carboxylate
-
Mn2+
Aranda Christine
-
-
Mn2+
-
activates at up to 1 mM, inhibits at higher concentrations, overview
Mn2+
-
60% inhibition at 1 mM Mn2+: 24 mM Mg2+
Mn2+
can substitute for Mg2+ at concentrations up to 0.5 mM, inhibitory above
Mn2+
-
less effective than Zn2+
N'-(2,4,5-trichlorobenzene-1-sulfonyl)pyridine-3-carbohydrazide
-
N'-(2,4,5-trichlorobenzene-1-sulfonyl)pyridine-3-carbohydrazide
-
N'-(2,6-dichlorophenyl)-5-nitrofuran-2-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-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-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-(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-(3,5-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,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-(2-[[(4-chlorophenyl)methyl]sulfanyl]ethyl)-3-methylbut-2-enamide
-
N-(3-chlorophenyl)-N'-(5-[[(4-chlorophenyl)sulfanyl]methyl]furan-2-yl)urea
-
N-(3-chlorophenyl)-N'-(5-[[(4-chlorophenyl)sulfanyl]methyl]furan-2-yl)urea
-
N-ethylmaleimide
-
-
N-ethylmaleimide
inhibits 38% of PPase activity at 37.5 mM
N-[4-[(3,5-dichlorophenyl)sulfamoyl]phenyl]acetamide
-
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,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
-
N2,N4-dimethyl-6-(1-phenyl-1H-pyrrol-2-yl)-1,3,5-triazine-2,4-diamine
-
NaF
-
-
NaF
inhibits 46% and 91.4% of the activity at 0.04 mM and 0.5 mM, respectively
p-chloromercuribenzoate
-
-
p-chloromercuribenzoate
-
-
p-chloromercuribenzoate
-
-
P2O74-
-
-
Phenylglyoxal
-
-
Phenylglyoxal
the inhibitory effect of phenylglyoxal is higher at 56°C than at room temperature. With 5 mM phenylglyoxal almost complete inhibition can be observed after 15 min incubation at 56°C
Phosphonates
-
-
SDS
-
-
SDS
SDS acts as a mixed-type reversible inhibitor of PPase, PPase can be fully inactivated at SDS concentration of 2 mM
Zn2+
-
-
Zn2+
-
activates at up to 1 mM, inhibits at higher concentrations, overview
Zn2+
-
inhibition caused at a separate site rather than as Zn-diphosphate substrate
Zn2+
can substitute for Mg2+ at concentrations up to 0.5 mM, inhibitory above
Zn2+
-
less effective then Co2+
[1,1'-biphenyl]-2,2'-dicarbonitrile
-
[1,1'-biphenyl]-2,2'-dicarbonitrile
-
additional information
C-substituted derivatives of methylene bisphosphonate, which are nonhydrolyzable diphosphate analogues, bind to Family II PPases 2-3 orders of magnitude more weakly than to Family I enzymes, whereas PNP binds with similar affinity, regardless of the metal cofactor bound. Structure-function analysis of canonical Family II PPases, catalytic reaction mechanism, detailed, overview
-
additional information
inorganic diphosphatase containing a pair of regulatory CBS domains (CBS-PPase1) is allosterically inhibited by AMP and ADP and activated by ATP and diadenosine polyphosphates
-
additional information
-
inorganic diphosphatase containing a pair of regulatory CBS domains (CBS-PPase1) is allosterically inhibited by AMP and ADP and activated by ATP and diadenosine polyphosphates
-
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
-
additional information
XM_008360526
apple S-RNase binds to two variable regions of MdPPa, resulting in a noncompetitive inhibition of its activity
-
additional information
-
apple S-RNase binds to two variable regions of MdPPa, resulting in a noncompetitive inhibition of its activity
-
additional information
not inhibited by nucleotides or its end product phosphate: neither addition of 0.75 mM AMP or 0.005 mM ADP nor addition of up to 1.5 mM phosphate led to a reduced reaction rate
-
additional information
-
not inhibited by nucleotides or its end product phosphate: neither addition of 0.75 mM AMP or 0.005 mM ADP nor addition of up to 1.5 mM phosphate led to a reduced reaction rate
-
additional information
-
poor inhibition by adenosine and UTP, no inhibition by cytidine, guanosine, uridine, CMP, CTP, GTP, cGMP, and UMP
-
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
-
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
-
additional information
-
the enzyme is inhibited by phosphorylation
-
additional information
C-substituted derivatives of methylene bisphosphonate, which are nonhydrolyzable diphosphate analogues, bind to Family II PPases 2-3 orders of magnitude more weakly than to Family I enzymes, whereas PNP binds with similar affinity, regardless of the metal cofactor bound
-
additional information
addition of EDTA up to 0.5 mM to the assay mixture does not result in any change in the PPase activity
-
additional information
-
the enzyme is not inhibited by Na+
-
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4.43
ADP
at pH 9.5 and 95°C
3.12
CDP
at pH 9.5 and 95°C
3.61
CTP
at pH 9.5 and 95°C
3.56
GDP
at pH 9.5 and 95°C
3.63
GTP
at pH 9.5 and 95°C
0.1554
guanosine 5'-tetraphosphate
-
with 3 mM Zn2+, at pH 6.5 and 30°C
3.47
IDP
at pH 9.5 and 95°C
0.12
Imidodiphosphate
-
-
0.012
imidodiphosphoric acid
pH 7.2, 25°C, wild-type enzyme
5.01
ITP
at pH 9.5 and 95°C
0.00045 - 4.2
Mg-diphosphate
0.0174
polyphosphate 75
-
with 3 mM Zn2+, at pH 6.5 and 30°C
-
0.3315
polyphosphate glass type 15
recombinant enzyme, pH 7.5, 30°C
-
0.0167 - 1.37
Triphosphate
3.32
UDP
at pH 9.5 and 95°C
6.09
UDP-glucose
at pH 9.5 and 95°C
11.8
UTP
at pH 9.5 and 95°C
additional information
additional information
-
0.064
ATP
pH 7.2, 37°C, recombinant enzyme
4.13
ATP
at pH 9.5 and 95°C
0.00001
diphosphate
-
at pH 9.1 and 25°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
0.0024
diphosphate
-
pH 7.5, 25°C, recombinant PPase1, in presence of Mg2+
0.0026
diphosphate
-
in the presence of 5 mM Mg2+, in 50 mM Tris-HCl, at pH 9.0 and 25°C
0.0027
diphosphate
-
pH 7.5, 25°C, mutant K112Q/K148Q
0.0028
diphosphate
native enzyme
0.0028
diphosphate
-
in the presence of 0.005 mM Mn2+, in 50 mM HEPES-NaOH, at pH 7.5 and 25°C
0.003
diphosphate
recombinant enzyme
0.0032
diphosphate
-
pH 7.5, 25°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
0.004
diphosphate
-
in the presence of 2 mM Mg2+, in 50 mM HEPES-NaOH,at pH 7.5 and 25°C
0.0045
diphosphate
-
pH 7.5, 25°C, mutant K112Q
0.0053
diphosphate
-
pH 7.5, 25°C, trimeric mutant K112Q
0.0054
diphosphate
-
pH 7.0, 75°C
0.0065
diphosphate
-
in the presence of Mg2+, at 25°C, pH not specified in the publication
0.007
diphosphate
-
in the presence of 10 mM Mg2+, in 50 mM Mes-NaOH, at pH 6.5 and 25°C
0.007
diphosphate
pH 6.2, 56°C
0.008
diphosphate
-
pH 8.0, 37°C, mutant Y230A
0.008
diphosphate
-
with 3 mM Mg2+, at pH 8.5 and 30°C
0.01
diphosphate
pH 7.2, 37°C, recombinant wild-type enzyme
0.0106
diphosphate
pH 7.5, 22°C, recombinant wild-type enzyme
0.0143
diphosphate
pH 8.0, 90°C
0.016
diphosphate
-
pH 8.0, 37°C, mutant G231A
0.0188
diphosphate
-
pH and temperature not specified in the publication
0.022
diphosphate
-
pH 8.0, 37°C, mutant R242A
0.034
diphosphate
-
pH 7.5, 25°C, recombinant PPase2, in presence of Mn2+
0.035
diphosphate
-
pH 8.0, 37°C, mutant L232A
0.0358
diphosphate
pH 7.5, 22°C, recombinant wild-type enzyme
0.0388
diphosphate
pH 8.0, 37°C
0.039
diphosphate
pH 7.5, in the presence of Ca2+
0.041
diphosphate
recombinant mutant I260D, pH 9.0, 25°C
0.0426
diphosphate
pH 7.2, 37°C, recombinant mutant D198N
0.0432
diphosphate
pH 7.5, 22°C, recombinant truncated mutant AtPPA1-DELTA(1-29)
0.0457
diphosphate
pH 7.2, 37°C, recombinant mutant D235N
0.047
diphosphate
-
presence of MgSO4
0.049 - 0.097
diphosphate
pH 7.2, 25°C, mutant enzyme N312S
0.0538
diphosphate
pH 7.2, 37°C, recombinant mutant D203N
0.054
diphosphate
-
pH 8.0, 37°C, mutant E225A
0.054
diphosphate
recombinant mutants I260V and I260E, pH 9.0, 25°C
0.055
diphosphate
recombinant mutant I259V, pH 9.0, 25°C
0.057
diphosphate
-
isoform 1
0.059
diphosphate
pH 7.5, 25°C, isozyme PPa4 in a complex with Mg2+
0.06
diphosphate
-
Mg2+ at 5 mM, enzyme from astroblasts
0.06
diphosphate
pH 7.2, 25°C, wild-type enzyme
0.062
diphosphate
pH 9.0, 25°C, 5 mM Mg2+, wild-type enzyme
0.062
diphosphate
recombinant wild-type enzyme, pH 9.0, 25°C
0.0642
diphosphate
pH 7.2, 37°C, recombinant mutant R158K
0.068
diphosphate
-
pH 8.0, 37°C, mutant G229A
0.069
diphosphate
pH 7.5, 25°C, isozyme PPa1 in a complex with Mg2+
0.07
diphosphate
-
Mg2+ at 5 mM, enzyme from neuroblasts
0.07
diphosphate
-
pH 8.0, 37°C, mutant G234A
0.07
diphosphate
pH 9.0, 25°C, 5 mM Mg2+, mutant G190W
0.072
diphosphate
-
isoform 2
0.074
diphosphate
-
pH 8.0, 37°C, mutant G233A
0.081
diphosphate
pH 9.0, 25°C, 5 mM Mg2+, mutant T191G
0.083
diphosphate
pH 8.0, 37°C, recombinant wild-type enzyme
0.098
diphosphate
pH 8.0, 37°C, recombinant mutant C16S
0.099
diphosphate
-
pH 8.0, 37°C, mutant F240A
0.105
diphosphate
-
pH 8.0, 37°C, mutant S236A
0.112
diphosphate
-
pH 8.0, 37°C, mutant M237A
0.113
diphosphate
pH 7.5, 60°C, recombinat enzyme
0.1224
diphosphate
recombinant enzyme, pH 7.5, 30°C
0.123
diphosphate
pH 9.0, 25°C, 5 mM Mg2+, mutant G190A
0.13
diphosphate
-
wild type hexamer, pH 7.5
0.14
diphosphate
-
pH 8.0, 37°C, mutant I227A
0.146
diphosphate
-
pH 8.0, 37°C, mutant T228A
0.148
diphosphate
-
pH 8.0, 37°C, mutant G221A
0.154
diphosphate
-
pH 8.0, 37°C, wild-type enzyme
0.161
diphosphate
pH 3.0, 55°C
0.163
diphosphate
recombinant mutant I259D, pH 9.0, 25°C
0.173
diphosphate
pH 8.0, 37°C, recombinant mutant Y140F
0.173
diphosphate
at pH 9.5 and 95°C
0.185
diphosphate
-
pH 8.0, 37°C, mutant A226S
0.196
diphosphate
-
pH 8.0, 37°C, mutant A238S
0.199
diphosphate
-
pH 8.0, 37°C, mutant S235A
0.214
diphosphate
recombinant enzyme
0.221
diphosphate
-
pH 8.0, 37°C, mutant L239A
0.248
diphosphate
recombinant mutant I259E, pH 9.0, 25°C
0.25 - 1.67
diphosphate
-
varying Mg2+ and EDTA concentrations
0.26
diphosphate
recombinant enzyme, pH 8.5, 25°C
0.27
diphosphate
pH 8.0, 37°C, with Mn2+ as metal cofactor
0.305
diphosphate
-
pH 8.0, 37°C, mutant F224A
0.318
diphosphate
-
pH 8.0, 37°C, mutant G222A
0.32
diphosphate
pH 7.5, 25°C, recombinant wild-type BT2127
0.332
diphosphate
-
pH 8.0, 37°C, mutant G241A
0.35
diphosphate
wild type enzyme, in 50 mM MOPS (pH 6.5), in the presence of Mg2+, at 80°C
0.37
diphosphate
pH 7.5, in the presence of Mg2+
0.4028
diphosphate
pH 7.2, 37°C, recombinant mutant K136R
0.438
diphosphate
-
pH 8.0, 37°C, mutant L223A
0.48
diphosphate
wild type enzyme, in 50 mM MOPS (pH 6.5), in the presence of Ni2+, at 80°C
0.49
diphosphate
wild type enzyme, in 50 mM MOPS (pH 6.5), in the presence of Co2+, at 80°C
0.55
diphosphate
recombinant enzyme, pH 8.5, 42°C
0.6
diphosphate
pH 7.2, 25°C, wild-type enzyme
0.8
diphosphate
-
wild type dimer, pH 7.5
1.3
diphosphate
-
E145Q hexamer, pH 7.5
1.32
diphosphate
-
pH 6.9
1.8
diphosphate
-
E145Q dimer, pH 7.5
1.98
diphosphate
-
pH 7.0, 50°C, in presence of 5 mM Mg2+
35
diphosphate
pH 7.2, 25°C, mutant enzyme S213N
46
diphosphate
pH 7.2, 25°C, wild-type enzyme
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
1.65
Mg2+
-
-
2.27
Mg2+
-
diphosphate at 1 mM, enzyme from astroblasts
3.15
Mg2+
-
diphosphate at 1 mM, enzyme from neuroblasts
0.0167
Triphosphate
-
with 3 mM Co2+, at pH 6.5 and 30°C
0.7244
Triphosphate
recombinant enzyme, pH 7.5, 30°C
0.91
Triphosphate
-
at pH 9.1 and 25°C
1.37
Triphosphate
at pH 9.5 and 95°C
additional information
additional information
kinetics
-
additional information
additional information
-
kinetics
-
additional information
additional information
-
kinetics of wild-type and mutant enzymes
-
additional information
additional information
kinetics of wild-type and mutant enzymes
-
additional information
additional information
-
kinetics of wild-type and mutant enzymes
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
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
Michaelis-Menten kinetics, overview
-
additional information
additional information
-
Michaelis-Menten kinetics, overview
-
additional information
additional information
effects of cysteine, homocysteine, and NaBH4 on kinetics of wild-type and mutant C16S enzymes, overview
-
additional information
additional information
-
effects of cysteine, homocysteine, and NaBH4 on kinetics of wild-type and mutant C16S enzymes, overview
-
additional information
additional information
-
kinetic analysis of wild-type and mutant enzymes in presence of different nucleotides, 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
metal binding affinities and kinetics of wild-type and mutant enzymes, overview
-
additional information
additional information
-
metal binding affinities and kinetics of wild-type and mutant enzymes, overview
-
additional information
additional information
ordered binding of free Mg2+ and of the Mg-diphosphate complex. Both isozymes show similar catalytic constants and affinities for the Mg-diphosphate complex, while differed in their affinity for free Mg2+, kinetics, overview
-
additional information
additional information
-
kinetics and thermodynamics, detailed overview
-
additional information
additional information
wild-type and mutant BT2127 steady-state kinetics, overview
-
additional information
additional information
-
wild-type and mutant BT2127 steady-state kinetics, overview
-
additional information
additional information
CBS-PPase activity shows positive cooperativity
-
additional information
additional information
CBS-PPase activity shows positive cooperativity
-
additional information
additional information
ehPPase lacks kinetic cooperativity, kinetic analysis, Michaelis-Menten kinetics, overview. The S213N substitution conferred significant negative cooperativity on the enzyme, decreasing the Hill coefficient to 0.7, and the Km2/Km1 ratio increases to approximately 13 over the entire range of Mg2+ concentrations
-
additional information
additional information
HvPPA displays non-Michaelis-Menten kinetics with a Vmax of 465 U/mg for diphosphate hydrolysis at optimal conditions of 42°C and pH 8.5, and Hill coefficients that indicate cooperative binding to diphosphate and Mg2+
-
additional information
additional information
-
HvPPA displays non-Michaelis-Menten kinetics with a Vmax of 465 U/mg for diphosphate hydrolysis at optimal conditions of 42°C and pH 8.5, and Hill coefficients that indicate cooperative binding to diphosphate and Mg2+
-
additional information
additional information
kinetic analysis, Michaelis-Menten kinetics, overview. With the wild-type enzyme, hydrolysis kinetics remains positively cooperative in the presence of ATP
-
additional information
additional information
Michaelis-Menten steady-state kinetic analysis
-
additional information
additional information
-
Michaelis-Menten steady-state kinetic analysis
-
additional information
additional information
mononucleotide binding to CBS domains and substrate binding to catalytic domains are characterized by positive co-operativity, kinetic analysis, overview
-
additional information
additional information
-
mononucleotide binding to CBS domains and substrate binding to catalytic domains are characterized by positive co-operativity, kinetic analysis, overview
-
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19.7
ADP
at pH 9.5 and 95°C
51.3
CDP
at pH 9.5 and 95°C
94.2
CTP
at pH 9.5 and 95°C
39.9
GDP
at pH 9.5 and 95°C
91.7
GTP
at pH 9.5 and 95°C
0.0022
guanosine 5'-tetraphosphate
-
with 3 mM Zn2+, at pH 6.5 and 30°C
57.3
IDP
at pH 9.5 and 95°C
0.014
imidodiphosphoric acid
pH 7.2, 25°C, wild-type enzyme
116
ITP
at pH 9.5 and 95°C
0.000165
polyphosphate 75
-
with 3 mM Zn2+, at pH 6.5 and 30°C
-
0.05
tripolyphosphate
-
pH 7.2, 25°C, in the presence of Mg2+
27.5
UDP
at pH 9.5 and 95°C
29.7
UDP-glucose
at pH 9.5 and 95°C
99.1
UTP
at pH 9.5 and 95°C
0.005
ATP
-
less than 0.005/sec, pH 7.2, 25°C, in the presence of Mg2+
91.7
ATP
at pH 9.5 and 95°C
0.16
diphosphate
wild type enzyme, in 50 mM MOPS (pH 6.5), in the presence of Mg2+, at 80°C
0.21
diphosphate
wild type enzyme, in 50 mM MOPS (pH 6.5), in the presence of Ni2+, at 80°C
0.22
diphosphate
wild type enzyme, in 50 mM MOPS (pH 6.5), in the presence of Co2+, at 80°C
0.22
diphosphate
-
with 3 mM Mg2+, at pH 8.5 and 30°C
0.34
diphosphate
-
pH 7.2, D97E, resynthesis of diphosphate
0.53
diphosphate
pH 7.2, 37°C, recombinant mutant D203N
0.67
diphosphate
-
pH 8, D97E, resynthesis of diphosphate
1.31
diphosphate
pH 7.2, 37°C, wild-type enzyme, in presence of 0.5 mM AMP
1.64
diphosphate
-
pH 7.2, 25°C
2.1
diphosphate
-
pH and temperature not specified in the publication
3.6
diphosphate
pH 7.5, 25°C, recombinant wild-type BT2127
5.3
diphosphate
pH 7.5, 22°C, recombinant wild-type enzyme
7.2
diphosphate
pH 7.2, 37°C, wild-type enzyme, in presence of 0.5 mM ADP
7.7
diphosphate
-
E145Q mutant dimer, pH 7.5
10
diphosphate
pH 7.2, 25°C, mutant enzyme S213N
10.8
diphosphate
pH 7.5, 22°C, recombinant wild-type enzyme
11
diphosphate
recombinant mutant I259D, pH 9.0, 25°C
11.9
diphosphate
pH 7.5, 25°C, isozyme PPa4
12
diphosphate
-
pH 7.2, D97E, hydrolysis of diphosphate
12.1
diphosphate
pH 7.5, 25°C, isozyme PPa1
18
diphosphate
pH 7.2, 37°C, mutant R276E, in presence of 0.5 mM AMP
21.4
diphosphate
pH 7.5, 22°C, recombinant truncated mutant AtPPA1-DELTA(1-29)
21.8
diphosphate
pH 7.2, 37°C, recombinant mutant K136R
25.8
diphosphate
pH 7.2, 37°C, recombinant mutant D198N
38
diphosphate
-
in the presence of 10 mM Mg2+, in 50 mM Mes-NaOH, at pH 6.5 and 25°C
42
diphosphate
-
at pH 9.1 and 25°C
48
diphosphate
recombinant mutant I259E, pH 9.0, 25°C
51
diphosphate
-
in the presence of 0.005 mM Mn2+, in 50 mM HEPES-NaOH, at pH 7.5 and 25°C
52.5
diphosphate
pH 7.2, 37°C, recombinant mutant D235N
54
diphosphate
pH 7.2, 37°C, mutant R276E, in presence of 0.5 mM ADP
55
diphosphate
-
pH 8, D97E, hydrolysis of diphosphate
58
diphosphate
pH 7.2, 37°C, mutant R276A, in presence of 0.5 mM AMP
60.4
diphosphate
pH 7.2, 37°C, recombinant mutant R158K
76
diphosphate
-
wild type dimer, pH 7.5
78.4
diphosphate
pH 8.0, 37°C, recombinant mutant Y140F
83
diphosphate
-
E145Q mutant hexamer, pH 7.5
83
diphosphate
-
pH 7.5, 25°C, hexameric mutant E145Q, 5 mM Mg2+
86
diphosphate
-
pH 6.5, wild type, hydrolysis of diphosphate
88
diphosphate
pH 7.2, 37°C, mutant R276A, in presence of 0.5 mM ADP
93
diphosphate
-
in the presence of 2 mM Mg2+, in 50 mM HEPES-NaOH, at pH 7.5 and 25°C
104
diphosphate
-
pH 6.5, wild type, resynthesis of diphosphate
109
diphosphate
-
pH 7.5, 25°C, recombinant PPase1, in presence of Mg2+
112
diphosphate
pH 7.2, 37°C, mutant R276A, in presence of 0.5 mM Ap4A
114
diphosphate
-
pH 8, wild type, resynthesis of diphosphate
115
diphosphate
pH 7.2, 37°C, mutant R276A, in presence of 0.5 mM ATP
116
diphosphate
-
pH 7.2, wild type, resynthesis of diphosphate
120
diphosphate
pH 7.2, 37°C, mutant R276E, in presence of 0.5 mM ATP
155
diphosphate
-
pH 7.2, wild type, hydrolysis of diphosphate
173
diphosphate
pH 7.2, 37°C, mutant R276K, in presence of 0.5 mM ATP
173.1
diphosphate
pH 8.0, 37°C, recombinant mutant C16S
177
diphosphate
-
in the presence of 5 mM Mg2+, in 50 mM Tris-HCl, at pH 9.0 and 25°C
187
diphosphate
-
pH 8, wild type, hydrolysis of diphosphate
215
diphosphate
pH 7.2, 37°C, mutant R276K, in presence of 0.5 mM Ap4A
225
diphosphate
pH 7.2, 37°C, wild-type enzyme, in presence of 0.5 mM ATP
240
diphosphate
pH 7.2, 37°C, mutant R276E, in presence of 0.5 mM Ap4A
260
diphosphate
-
pH 7.2, 25°C, in the presence of Mg2+
266
diphosphate
pH 7.2, 37°C, recombinant wild-type enzyme
308
diphosphate
pH 7.2, 37°C, wild-type enzyme, in presence of 0.5 mM Ap4A
320
diphosphate
pH 7.2, 25°C, wild-type enzyme
343.9
diphosphate
pH 8.0, 37°C, recombinant wild-type enzyme
369
diphosphate
pH 7.5, in the presence of Mg2+
390
diphosphate
-
wild type hexamer, pH 7.5
390
diphosphate
-
pH 7.5, 25°C, wild-type enzyme, 5 mM Mg2+
410
diphosphate
pH 7.2, 25°C, mutant enzyme S213N
560
diphosphate
recombinant mutant I260D, pH 9.0, 25°C
570
diphosphate
recombinant mutant I260E, pH 9.0, 25°C
744
diphosphate
pH 7.5, 60°C, recombinat enzyme
800
diphosphate
recombinant enzyme
916
diphosphate
native enzyme
1050
diphosphate
recombinant enzyme, pH 8.5, 42°C
1230
diphosphate
at pH 9.5 and 95°C
1600
diphosphate
-
pH 7.5, 25°C, recombinant PPase2, in presence of Mn2+
1700
diphosphate
-
pH 7.0, 75°C
1850
diphosphate
pH 7.2, 25°C, wild-type enzyme
2130
diphosphate
pH 9.0, 25°C, 5 mM Mg2+, mutant T191G
2200
diphosphate
pH 6.2, 56°C
3270
diphosphate
pH 9.0, 25°C, 5 mM Mg2+, mutant G190A
3436
diphosphate
pH 8.0, 90°C
3460
diphosphate
pH 9.0, 25°C, 5 mM Mg2+, mutant G190W
3693
diphosphate
pH 7.5, in the presence of Ca2+
4420
diphosphate
recombinant mutant I259V, pH 9.0, 25°C
6290
diphosphate
pH 9.0, 25°C, 5 mM Mg2+, wild-type enzyme
6290
diphosphate
recombinant wild-type enzyme, pH 9.0, 25°C
6480
diphosphate
recombinant mutant I260V, pH 9.0, 25°C
0.13
Triphosphate
-
with 3 mM Co2+, at pH 6.5 and 30°C
16.7
Triphosphate
-
at pH 9.1 and 25°C
226
Triphosphate
at pH 9.5 and 95°C
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evolution
AtPPsPase1 belongs to the haloacid dehalogenase, HAD, superfamily
evolution
enzyme BT2127 is a member of the haloalkanoate dehalogenase superfamily, HADSF
evolution
family II soluble inorganic pyrophosphatase
evolution
Mycobacterium tuberculosis and Mycobacterium leprae genomes include genes for the only two family I inorganic pyrophosphatases known to contain two histidines in the active site, structure comparison of family I enzymes, overview
evolution
hierarchical clustering and three-dimensional (3D) homology modeling reveals that HvPPA is distinct in structure from characterized inorganic diphosphatases, PPAs. HvPPA beongs to the class A type inorganic diphosphatases, PPAs. Evolutionary relationships of archaeal PPAs, overview
evolution
-
PPases include membrane associated V-H+-PPases (vacuolar H+-translocating PPases) and soluble form PPases, where latter comprise two families that differ in their sequence and structure. Family I PPases are Mg2+ dependent enzymes known to exist as homo-hexamers in prokaryotes and dimers in eukaryotes6. Family II PPases are Mn2+-dependent enzymes with bi-domain structures, and active in dimeric or trimeric forms. Structure comparisons of the enzyme from Plasmodium falciparum (PfPPase) and Toxoplasma gondii (TgPPase), overview. Comparison of eukaryotic family I PPases reveal diversity in dimerization modes
evolution
PPases include membrane associated V-H+-PPases (vacuolar H+-translocating PPases) and soluble form PPases, where latter comprise two families that differ in their sequence and structure6. Family I PPases are Mg2+ dependent enzymes known to exist as homo-hexamers in prokaryotes and dimers in eukaryotes. Family II PPases are Mn2+ dependent enzymes with bi-domain structures, and active in dimeric or trimeric forms. Structure comparisons of the enzyme from Plasmodium falciparum (PfPPase) and Toxoplasma gondii (TgPPase), overview. Comparison of eukaryotic family I PPases reveals diversity in dimerization modes
evolution
soluble PPases belong to three nonhomologous families, of which family II is found in approximately a quarter of prokaryotic organisms, often pathogenic ones. Each subunit of dimeric canonical Family II PPases is formed by two domains connected by a flexible linker, with the active site located between the domains. The enzymes require both magnesium and a transition metal ion (manganese or cobalt) for maximal activity and are the most active among all PPase types. Soluble PPases convert diphosphate energy into heat, as opposed to membrane-bound PPases, which employ diphosphate energy to transport H+ or Na+ across membranes in plants and some bacteria, archaea, and protists. Soluble PPases belong to three nonhomologous families, I, II, and III. Family I PPases are found in all kingdoms of life, whereas Family II and Family III PPases are found in prokaryotes. Distribution of Family II PPases, overview
evolution
soluble PPases belong to three nonhomologous families, of which family II is found in approximately a quarter of prokaryotic organisms, often pathogenic ones. Each subunit of dimeric canonical Family II PPases is formed by two domains connected by a flexible linker, with the active site located between the domains. The enzymes require both magnesium and a transition metal ion (manganese or cobalt) for maximal activity and are the most active among all PPase types. Soluble PPases convert diphosphate energy into heat, as opposed to membrane-bound PPases, which employ diphosphate energy to transport H+ or Na+ across membranes in plants and some bacteria, archaea, and protists. Soluble PPases belong to three nonhomologous families, I, II, and III. Family I PPases are found in all kingdoms of life, whereas Family II and Family III PPases are found in prokaryotes. Distribution of Family II PPases, overview
evolution
soluble PPases belong to three nonhomologous families, of which family II is found in approximately a quarter of prokaryotic organisms, often pathogenic ones. Each subunit of dimeric canonical Family II PPases is formed by two domains connected by a flexible linker, with the active site located between the domains. The enzymes require both magnesium and a transition metal ion (manganese or cobalt) for maximal activity and are the most active among all PPase types. Soluble PPases convert diphosphate energy into heat, as opposed to membrane-bound PPases, which employ diphosphate energy to transport H+ or Na+ across membranes in plants and some bacteria, archaea, and protists. Soluble PPases belong to three nonhomologous families, I, II, and III. Family I PPases are found in all kingdoms of life, whereas Family II and Family III PPases are found in prokaryotes. Distribution of Family II PPases, overview
evolution
soluble PPases belong to three nonhomologous families, of which family II is found in approximately a quarter of prokaryotic organisms, often pathogenic ones. Each subunit of dimeric canonical Family II PPases is formed by two domains connected by a flexible linker, with the active site located between the domains. The enzymes require both magnesium and a transition metal ion (manganese or cobalt) for maximal activity and are the most active among all PPase types. Soluble PPases convert diphosphate energy into heat, as opposed to membrane-bound PPases, which employ diphosphate energy to transport H+ or Na+ across membranes in plants and some bacteria, archaea, and protists. Soluble PPases belong to three nonhomologous families, I, II, and III. Family I PPases are found in all kingdoms of life, whereas Family II and Family III PPases are found in prokaryotes. Distribution of Family II PPases, overview
evolution
soluble PPases belong to three nonhomologous families, of which family II is found in approximately a quarter of prokaryotic organisms, often pathogenic ones. Each subunit of dimeric canonical Family II PPases is formed by two domains connected by a flexible linker, with the active site located between the domains. The enzymes require both magnesium and a transition metal ion (manganese or cobalt) for maximal activity and are the most active among all PPase types. Soluble PPases convert diphosphate energy into heat, as opposed to membrane-bound PPases, which employ diphosphate energy to transport H+ or Na+ across membranes in plants and some bacteria, archaea, and protists. Soluble PPases belong to three nonhomologous families, I, II, and III. Family I PPases are found in all kingdoms of life, whereas Family II and Family III PPases are found in prokaryotes. Distribution of Family II PPases, overview
evolution
soluble PPases belong to three nonhomologous families, of which family II is found in approximately a quarter of prokaryotic organisms, often pathogenic ones. Each subunit of dimeric canonical Family II PPases is formed by two domains connected by a flexible linker, with the active site located between the domains. The enzymes require both magnesium and a transition metal ion (manganese or cobalt) for maximal activity and are the most active among all PPase types. Soluble PPases convert diphosphate energy into heat, as opposed to membrane-bound PPases, which employ diphosphate energy to transport H+ or Na+ across membranes in plants and some bacteria, archaea, and protists. Soluble PPases belong to three nonhomologous families, I, II, and III. Family I PPases are found in all kingdoms of life, whereas Family II and Family III PPases are found in prokaryotes. Distribution of Family II PPases, overview
evolution
soluble PPases belong to three nonhomologous families, of which family II is found in approximately a quarter of prokaryotic organisms, often pathogenic ones. The enzymes require both magnesium and a transition metal ion (manganese or cobalt) for maximal activity and are the most active among all PPase types. Soluble PPases convert diphosphate energy into heat, as opposed to membrane-bound PPases, which employ diphosphate energy to transport H+ or Na+ across membranes in plants and some bacteria, archaea, and protists. Soluble PPases belong to three nonhomologous families, I, II, and III. Family I PPases are found in all kingdoms of life, whereas Family II and Family III PPases are found in prokaryotes. Distribution of Family II PPases, overview
evolution
the enzyme belongs to the CBS-PPases
evolution
the enzyme belongs to the CBS-PPases
evolution
the ThPP1 gene was a PPase family I member. ThPP1 gene exhibits a typical structural characteristic of PPase family
evolution
-
family II soluble inorganic pyrophosphatase
-
evolution
-
the enzyme belongs to the CBS-PPases
-
evolution
-
enzyme BT2127 is a member of the haloalkanoate dehalogenase superfamily, HADSF
-
evolution
-
AtPPsPase1 belongs to the haloacid dehalogenase, HAD, superfamily
-
evolution
-
soluble PPases belong to three nonhomologous families, of which family II is found in approximately a quarter of prokaryotic organisms, often pathogenic ones. Each subunit of dimeric canonical Family II PPases is formed by two domains connected by a flexible linker, with the active site located between the domains. The enzymes require both magnesium and a transition metal ion (manganese or cobalt) for maximal activity and are the most active among all PPase types. Soluble PPases convert diphosphate energy into heat, as opposed to membrane-bound PPases, which employ diphosphate energy to transport H+ or Na+ across membranes in plants and some bacteria, archaea, and protists. Soluble PPases belong to three nonhomologous families, I, II, and III. Family I PPases are found in all kingdoms of life, whereas Family II and Family III PPases are found in prokaryotes. Distribution of Family II PPases, overview
-
evolution
-
soluble PPases belong to three nonhomologous families, of which family II is found in approximately a quarter of prokaryotic organisms, often pathogenic ones. Each subunit of dimeric canonical Family II PPases is formed by two domains connected by a flexible linker, with the active site located between the domains. The enzymes require both magnesium and a transition metal ion (manganese or cobalt) for maximal activity and are the most active among all PPase types. Soluble PPases convert diphosphate energy into heat, as opposed to membrane-bound PPases, which employ diphosphate energy to transport H+ or Na+ across membranes in plants and some bacteria, archaea, and protists. Soluble PPases belong to three nonhomologous families, I, II, and III. Family I PPases are found in all kingdoms of life, whereas Family II and Family III PPases are found in prokaryotes. Distribution of Family II PPases, overview
-
evolution
-
the enzyme belongs to the CBS-PPases
-
evolution
-
soluble PPases belong to three nonhomologous families, of which family II is found in approximately a quarter of prokaryotic organisms, often pathogenic ones. Each subunit of dimeric canonical Family II PPases is formed by two domains connected by a flexible linker, with the active site located between the domains. The enzymes require both magnesium and a transition metal ion (manganese or cobalt) for maximal activity and are the most active among all PPase types. Soluble PPases convert diphosphate energy into heat, as opposed to membrane-bound PPases, which employ diphosphate energy to transport H+ or Na+ across membranes in plants and some bacteria, archaea, and protists. Soluble PPases belong to three nonhomologous families, I, II, and III. Family I PPases are found in all kingdoms of life, whereas Family II and Family III PPases are found in prokaryotes. Distribution of Family II PPases, overview
-
evolution
-
Mycobacterium tuberculosis and Mycobacterium leprae genomes include genes for the only two family I inorganic pyrophosphatases known to contain two histidines in the active site, structure comparison of family I enzymes, overview
-
evolution
-
the enzyme belongs to the CBS-PPases
-
malfunction
knockdown of pyrophosphatase 1 decreases colony formation and viability of MCF-7 cells
malfunction
deletion of the low complexity asparagine-rich N-terminal region has an unexpected and substantial effect on the stability of PfPPase domain, resulting in aggregation and significant loss of enzyme activity
malfunction
naturally occuring ehPPase mutant containing an inherent mutation in an otherwise conserved asparagine residue in a loop near the active site exhibits noncooperative hydrolysis kinetics
malfunction
naturally occuring ehPPase mutant containing an inherent mutation in an otherwise conserved asparagine residue in a loop near the active site exhibits noncooperative hydrolysis kinetics
malfunction
replacement of the regulatory Asn residue with Ser abolishes the kinetic cooperativity in Desulfitobacterium hafniense CBS-PPase and modifies the effect of Ap4A on it
malfunction
replacement of the regulatory Asn residue with Ser abolishes the kinetic cooperativity in Desulfitobacterium hafniense CBS-PPase and modifies the effect of Ap4A on it
malfunction
the vacuolar H+-translocating pyrophosphatase (H+-PPase) loss-of-function fugu5 mutant is susceptible to drought and displays pleotropic postgerminative growth defects due to excess diphosphate. Stomatal closure after abscisic acid (ABA) treatment is delayed in vhp1-1, a fugu5 allele. In contrast, specific removal of diphosphate rescues all of the above fugu5 developmental and growth defects. Hydrolysis of PPi within guard cells alleviates delayed growth in fugu5-1. The GC1 promoter is properly expressed in guard cells in the fugu5-1 background. Stomatal development is mildly affected in fugu5-1. Dysfunction of H+-PPase in the fugu5 mutant leads to elevated cytosolic PPi levels and results in a pleiotropic phenotype. Mutant fugu5 plants exhibit seasonal fluctuations, growing better during the humid summer but exhibiting susceptibility to the dry winter. Recombinant expression of IPP1 in the guard cells of the pGC1::IPP1/fugu5-1 lines does not affect the palisade cell phenotype. Effect of pGC1::IPP1 expression on palisade tissue development and hypocotyl elongation, overview
malfunction
tripolyphosphate is able to increase the F-ATPase activity in wild-type and Tc-sPPase RNAi beetles. sPPase gene knock-down influences polyP metabolism in mitochondria, mainly tripolyphosphate metabolism
malfunction
XM_008360526
when treated with self S-RNases, apple pollen tubes show a marked growth inhibition, as well as a decrease in endogenous soluble diphosphatase activity and elevated levels of inorganic diphosphate. In addition, S-RNase is found to bind to two variable regions of MdPPa, resulting in a noncompetitive inhibition of its activity. Silencing of MdPPa expression leads to a reduction in pollen tube growth. tRNA aminoacylation is inhibited in self S-RNase-treated or MdPPa-silenced pollen tubes, resulting in the accumulation of uncharged tRNA, but this disturbance of tRNA aminoacylation is independent of RNase activity. Excess diphosphate causes uncharged tRNA accumulation in pollen tubes
malfunction
-
naturally occuring ehPPase mutant containing an inherent mutation in an otherwise conserved asparagine residue in a loop near the active site exhibits noncooperative hydrolysis kinetics
-
malfunction
-
naturally occuring ehPPase mutant containing an inherent mutation in an otherwise conserved asparagine residue in a loop near the active site exhibits noncooperative hydrolysis kinetics
-
malfunction
-
naturally occuring ehPPase mutant containing an inherent mutation in an otherwise conserved asparagine residue in a loop near the active site exhibits noncooperative hydrolysis kinetics
-
metabolism
PPase is an essential constitutive enzyme for energy metabolism and clearance of excess diphosphate
metabolism
the soluble pyrophosphatasem RNA exists in great copy numbers in cells of Methanosaeta thermophila
metabolism
inorganic pyrophosphatase modulates polyphosphate metabolism in mitochondria and affects the link between mitochondrial activity and polyphosphate metabolism in Tibolium castaneum. Mitochondrial respiration modulates exopolyphosphatase activity (EC 3.6.1.11) only in wild-type beetles. The soluble form has a greater affinity for polyP3, and the membrane form has a greater affinity for polyP15, with only the soluble PPX activity being affected by Tc-sPPase RNAi
metabolism
the inorganic diphosphatase from Rhipicephalus microplus seems to be involved in polyphosphate metabolism
metabolism
-
PPase is an essential constitutive enzyme for energy metabolism and clearance of excess diphosphate
-
metabolism
-
the soluble pyrophosphatasem RNA exists in great copy numbers in cells of Methanosaeta thermophila
-
physiological function
-
the soluble inorganic diphosphatases recycle the pyrophosphate produced by many biosynthetic reactions, and may play a role in the plant adaptation to phosphorus deficiency
physiological function
the vacuolar H+-translocating inorganic pyrophosphatase is an electrogenic proton pump, which is related to growth as well as abiotic stress tolerance in plants. MdVHP1 is an important regulator for plant tolerance to abiotic stresses by modulating internal stores of ions and solutes
physiological function
tight control of AtPPsPase1 gene expression underlines its important role in the phosphate starvation response, cleavage of diphosphate is an immediate metabolic adaptation reaction
physiological function
V-PPase is an important element in the survival strategies of plants under cold stress. OVP1-enhanced cold tolerance is related to cell membrane integrity and proline accumulation
physiological function
-
enzyme-overexpressing parasites show a significant growth defect in fibroblasts, less responsiveness to hyperosmotic stress, and reduced persistence in tissues of mice
physiological function
-
the enzyme can pump protons through membranes
physiological function
-
the membrane-integral enzyme uses binding of diphosphate to drive pumping H+
physiological function
-
the membrane-integral enzyme uses binding of diphosphate to drive pumping Na+
physiological function
-
the upregulation of the enzyme during neuronal development in the hypothyroid chick cerebellum may lead to impaired social behaviors as well as to impaired learning and memory via JNK dephosphorylation and inactivation in the chick cerebellum
physiological function
diphosphate, a byproduct and regulator of numerous biosynthetic reactions, is converted to metabolizable phosphate via the action of specific constitutive enzymes-inorganic pyrophosphatases (PPases). Soluble PPases convert diphosphate energy into heat, as opposed to membrane-bound PPases, which employ diphosphate energy to transport H+ or Na+ across membranes in plants and some bacteria, archaea, and protists. Both PPase types can also catalyze the reverse reaction of diphosphate synthesis from phosphate, but this activity does not seem physiologically important
physiological function
diphosphate, a byproduct and regulator of numerous biosynthetic reactions, is converted to metabolizable phosphate via the action of specific constitutive enzymes-inorganic pyrophosphatases (PPases). Soluble PPases convert diphosphate energy into heat, as opposed to membrane-bound PPases, which employ diphosphate energy to transport H+ or Na+ across membranes in plants and some bacteria, archaea, and protists. Both PPase types can also catalyze the reverse reaction of diphosphate synthesis from phosphate, but this activity does not seem physiologically important
physiological function
diphosphate, a byproduct and regulator of numerous biosynthetic reactions, is converted to metabolizable phosphate via the action of specific constitutive enzymes-inorganic pyrophosphatases (PPases). Soluble PPases convert diphosphate energy into heat, as opposed to membrane-bound PPases, which employ diphosphate energy to transport H+ or Na+ across membranes in plants and some bacteria, archaea, and protists. Both PPase types can also catalyze the reverse reaction of diphosphate synthesis from phosphate, but this activity does not seem physiologically important
physiological function
diphosphate, a byproduct and regulator of numerous biosynthetic reactions, is converted to metabolizable phosphate via the action of specific constitutive enzymes-inorganic pyrophosphatases (PPases). Soluble PPases convert diphosphate energy into heat, as opposed to membrane-bound PPases, which employ diphosphate energy to transport H+ or Na+ across membranes in plants and some bacteria, archaea, and protists. Both PPase types can also catalyze the reverse reaction of diphosphate synthesis from phosphate, but this activity does not seem physiologically important
physiological function
diphosphate, a byproduct and regulator of numerous biosynthetic reactions, is converted to metabolizable phosphate via the action of specific constitutive enzymes-inorganic pyrophosphatases (PPases). Soluble PPases convert diphosphate energy into heat, as opposed to membrane-bound PPases, which employ diphosphate energy to transport H+ or Na+ across membranes in plants and some bacteria, archaea, and protists. Both PPase types can also catalyze the reverse reaction of diphosphate synthesis from phosphate, but this activity does not seem physiologically important. Family II PPase containing CBS domains are the only PPases that are regulated by a well-established universal mechanism based on adenine nucleotide binding to the auxiliary CBS domains
physiological function
diphosphate, a byproduct and regulator of numerous biosynthetic reactions, is converted to metabolizable phosphate via the action of specific constitutive enzymes-inorganic pyrophosphatases (PPases). Soluble PPases convert diphosphate energy into heat, as opposed to membrane-bound PPases, which employ diphosphate energy to transport H+ or Na+ across membranes in plants and some bacteria, archaea, and protists. Both PPase types can also catalyze the reverse reaction of diphosphate synthesis from phosphate, but this activity does not seem physiologically important. Family II PPase containing CBS domains are the only PPases that are regulated by a well-established universal mechanism based on adenine nucleotide binding to the auxiliary CBS domains
physiological function
diphosphate, a byproduct and regulator of numerous biosynthetic reactions, is converted to metabolizable phosphate via the action of specific constitutive enzymes-inorganic pyrophosphatases (PPases). Soluble PPases convert diphosphate energy into heat, as opposed to membrane-bound PPases, which employ diphosphate energy to transport H+ or Na+ across membranes in plants and some bacteria, archaea, and protists. Both PPase types can also catalyze the reverse reaction of diphosphate synthesis from phosphate, but this activity does not seem physiologically important. Phosphorylation of the Family I PPase from the flowering plant, Papaver rhoeas, suppresses PPase activity and is a key event in preventing self-fertilization
physiological function
ehPPase lacks kinetic cooperativity and is not regulated by adenine nucleotides. ehPPase shows insensitivity (below 10% activity change) to adenine nucleotides (AMP, ADP, ATP and diadenosine polyphosphates, ApnA, with n=3-6) over a wide range of substrate concentrations (0.001-0.30 mM), metal cofactor concentrations (0.05-20 mM), and nucleotide concentrations (10 nM-1.0 mM) for mononucleotides and 0.01 nM-0.1 mM for dinucleotides
physiological function
hydrolysis of diphosphate byenzyme PPA releases a considerable amount of energy that can drive unfavorable biochemical transformations to completion
physiological function
inorganic diphosphatases (PPases), which hydrolyze inorganic diphosphate to phosphate in the presence of divalent metal cations, play a key role in maintaining phosphorus homeostasis in cells
physiological function
inorganic diphosphatases (PPases), which hydrolyze inorganic diphosphate to phosphate in the presence of divalent metal cations, play a key role in maintaining phosphorus homeostasis in cells
physiological function
inorganic pyrophosphatases (PPases) are ubiquitous, essential metal-dependent enzymes capable of supplying thermodynamic energy to many important biosynthetic reactions by hydrolysis of diphosphate to phosphate
physiological function
inorganic pyrophosphorylase gene, ThPP1, modulates the accumulations of phosphate and osmolytes by upregulating the differentially expression genes, thus enhancing the tolerance of the transgenic rice to alkali stress
physiological function
presence of two exopolyphosphatase isoforms in mitochondria. Tribolium castaneum mitochondrial polyP levels decrease after injection with soluble diphosphatase (Tc-sPPase) dsRNA, while the membrane exopolyphosphate activity (EC 3.6.1.11) increases
physiological function
XM_008360526
SRNase is necessary and sufficient for the pistil to reject self-pollen. S-RNase causes a decrease in sPPase activity and diphosphate accumulation in self-pollen tubes
physiological function
-
the enzyme inorganic pyrophosphatase (PPase) catalyzes the hydrolysis of pyrophosphate (PPi) to inorganic phosphate (Pi). This is an exergonic reaction and can be coupled to several unfavorable and energy demanding biochemical transformations such as DNA replication, protein synthesis and lipid metabolism
physiological function
the enzyme inorganic pyrophosphatase (PPase) catalyzes the hydrolysis of pyrophosphate (PPi) to inorganic phosphate (Pi). This is an exergonic reaction and can be coupled to several unfavorable and energy demanding biochemical transformations such as DNA replication, protein synthesis and lipid metabolism. Cambialistic PfPPase actively hydrolyzes linear short chain polyphosphates like diphosphate, polyP3, and ATP in the presence of Zn2+
physiological function
the H+-PPase contributes to stomatal functioning not only as a proton pump that acidifies the vacuoles, but also as an enzyme that maintains adequate PPi levels within guard cells. Regulation of PPi levels by H+-PPase is critical for proper resumption of postgerminative plant development. Diphosphate homeostasis is important for stomatal closure. Stomatal opening is independent of H+-PPase, but a balance between PPi level and vacuolar membrane potential is required for proper regulation of stomata, excess PPi selectively affects stomatal closure movement
physiological function
-
tight control of AtPPsPase1 gene expression underlines its important role in the phosphate starvation response, cleavage of diphosphate is an immediate metabolic adaptation reaction
-
physiological function
-
diphosphate, a byproduct and regulator of numerous biosynthetic reactions, is converted to metabolizable phosphate via the action of specific constitutive enzymes-inorganic pyrophosphatases (PPases). Soluble PPases convert diphosphate energy into heat, as opposed to membrane-bound PPases, which employ diphosphate energy to transport H+ or Na+ across membranes in plants and some bacteria, archaea, and protists. Both PPase types can also catalyze the reverse reaction of diphosphate synthesis from phosphate, but this activity does not seem physiologically important. Family II PPase containing CBS domains are the only PPases that are regulated by a well-established universal mechanism based on adenine nucleotide binding to the auxiliary CBS domains
-
physiological function
-
diphosphate, a byproduct and regulator of numerous biosynthetic reactions, is converted to metabolizable phosphate via the action of specific constitutive enzymes-inorganic pyrophosphatases (PPases). Soluble PPases convert diphosphate energy into heat, as opposed to membrane-bound PPases, which employ diphosphate energy to transport H+ or Na+ across membranes in plants and some bacteria, archaea, and protists. Both PPase types can also catalyze the reverse reaction of diphosphate synthesis from phosphate, but this activity does not seem physiologically important
-
physiological function
-
diphosphate, a byproduct and regulator of numerous biosynthetic reactions, is converted to metabolizable phosphate via the action of specific constitutive enzymes-inorganic pyrophosphatases (PPases). Soluble PPases convert diphosphate energy into heat, as opposed to membrane-bound PPases, which employ diphosphate energy to transport H+ or Na+ across membranes in plants and some bacteria, archaea, and protists. Both PPase types can also catalyze the reverse reaction of diphosphate synthesis from phosphate, but this activity does not seem physiologically important. Family II PPase containing CBS domains are the only PPases that are regulated by a well-established universal mechanism based on adenine nucleotide binding to the auxiliary CBS domains
-
physiological function
-
ehPPase lacks kinetic cooperativity and is not regulated by adenine nucleotides. ehPPase shows insensitivity (below 10% activity change) to adenine nucleotides (AMP, ADP, ATP and diadenosine polyphosphates, ApnA, with n=3-6) over a wide range of substrate concentrations (0.001-0.30 mM), metal cofactor concentrations (0.05-20 mM), and nucleotide concentrations (10 nM-1.0 mM) for mononucleotides and 0.01 nM-0.1 mM for dinucleotides
-
additional information
His21 and His86 are not essential for diphosphate hydrolysis, but are responsible for a shift in the optimal pH for the reaction compared with the Escherichia coli enzyme
additional information
-
His21 and His86 are not essential for diphosphate hydrolysis, but are responsible for a shift in the optimal pH for the reaction compared with the Escherichia coli enzyme
additional information
MdVHP1 overexpression enhances tolerance to salt, PEG-mimic drought, cold and heat in transgenic apple calluses, which is related to an increased accumulation of proline and decreased MDA content compared with control calli. In addition, MdVHP1 overexpression confers improves tolerance to salt and drought in transgenic tomato, along with an increased ion accumulation, high RWC and low solute potential compared with wild-type, phenotypes, overview
additional information
-
MdVHP1 overexpression enhances tolerance to salt, PEG-mimic drought, cold and heat in transgenic apple calluses, which is related to an increased accumulation of proline and decreased MDA content compared with control calli. In addition, MdVHP1 overexpression confers improves tolerance to salt and drought in transgenic tomato, along with an increased ion accumulation, high RWC and low solute potential compared with wild-type, phenotypes, overview
additional information
modelling of the active site
additional information
-
modelling of the active site
additional information
OVP1 overexpression results in enhanced cold tolerance in transgenic rice, which is related to an increased integrity of cell membrane, decreased MDA content and accumulation of proline to higher level as compared with wild-type rice seedlings
additional information
-
OVP1 overexpression results in enhanced cold tolerance in transgenic rice, which is related to an increased integrity of cell membrane, decreased MDA content and accumulation of proline to higher level as compared with wild-type rice seedlings
additional information
the catalytic residues are Asp11, Asp13, Thr113, and Lys147, structure-guided site-directed mutagenesis coupled with kinetic analysis of the mutant enzymes identifies the residues required for catalysis, substrate binding, and domain-domain association
additional information
-
the catalytic residues are Asp11, Asp13, Thr113, and Lys147, structure-guided site-directed mutagenesis coupled with kinetic analysis of the mutant enzymes identifies the residues required for catalysis, substrate binding, and domain-domain association
additional information
the hinge region plays an important role in opening and closing of the active site between the N- and C-terminal domains of PPase
additional information
-
the hinge region plays an important role in opening and closing of the active site between the N- and C-terminal domains of PPase
additional information
-
active site structure analysis
additional information
active site structure analysis
additional information
-
active site structure analysis
additional information
AtPPA1 three-dimensional structure analysis and modelling, overview
additional information
-
AtPPA1 three-dimensional structure analysis and modelling, overview
additional information
comparison of the primary structure of ehPPase with those of five other CBS-PPases. Molecular dynamic simulations, overview
additional information
HvPPA is highly negative in surface charge, which explains its extreme resistance to organic solvents. Active site structure comparisons, overview. Three-dimensional homology modeling suggests HvPPA to have an OB fold consisting of a central beta-barrel structure and alpha-helices associated in a beta1-8-alpha1-beta9-alpha2 topology and to homo-oligomerize into a trimer and/or dimer of trimers. Active-site residues of diphosphate hydrolysis are found conserved in HvPPA, including Asp69, which is predicted to provide the carboxylate functional group that performs the nucleophilic attack on the diphosphate substrate when Mg2+ ions are present. The two cysteine residues, Cys24 and Cys85, of HvPPA are found in a Cys-X63-Cys configuration that is highly conserved among haloarchaeal PPAs and distinct from other class A type PPAs
additional information
-
HvPPA is highly negative in surface charge, which explains its extreme resistance to organic solvents. Active site structure comparisons, overview. Three-dimensional homology modeling suggests HvPPA to have an OB fold consisting of a central beta-barrel structure and alpha-helices associated in a beta1-8-alpha1-beta9-alpha2 topology and to homo-oligomerize into a trimer and/or dimer of trimers. Active-site residues of diphosphate hydrolysis are found conserved in HvPPA, including Asp69, which is predicted to provide the carboxylate functional group that performs the nucleophilic attack on the diphosphate substrate when Mg2+ ions are present. The two cysteine residues, Cys24 and Cys85, of HvPPA are found in a Cys-X63-Cys configuration that is highly conserved among haloarchaeal PPAs and distinct from other class A type PPAs
additional information
inorganic diphosphatase containing a pair of regulatory CBS domains (CBS-PPase1) is allosterically inhibited by AMP and ADP and activated by ATP and diadenosine polyphosphatesegulated involving residue Arg276 at the interface of the regulatory and catalytic domains of CBS-PPase1, overview. The H-bond formed by the Arg276 sidechain is essential for signal transduction between the regulatory and catalytic domains within one subunit and between the catalytic but not regulatory domains of different subunits
additional information
-
inorganic diphosphatase containing a pair of regulatory CBS domains (CBS-PPase1) is allosterically inhibited by AMP and ADP and activated by ATP and diadenosine polyphosphatesegulated involving residue Arg276 at the interface of the regulatory and catalytic domains of CBS-PPase1, overview. The H-bond formed by the Arg276 sidechain is essential for signal transduction between the regulatory and catalytic domains within one subunit and between the catalytic but not regulatory domains of different subunits
additional information
metal-binding sites are found in the DHH domain, whereas the substrate recruits ligands from both domains
additional information
metal-binding sites are found in the DHH domain, whereas the substrate recruits ligands from both domains. Structure-function analysis of canonical Family II PPases, catalytic reaction mechanism, detailed, overview
additional information
MtPPA1 three-dimensional structure analysis and modelling, overview
additional information
-
MtPPA1 three-dimensional structure analysis and modelling, overview
additional information
structure comparisons of CBS-PPases and molecular dynamic simulations, overview
additional information
structure comparisons of substrate-bound enzymes from Mycobacterum tuberculosis and Escherichia coli, quantum mechanics/molecular mechanics (QM/MM) analysis. Mtb PPiase exhibits significant structural differences from the well characterized Escherichia coli PPiase in the vicinity of the bound diphosphate substrate. In Mtb PPiase, Asp89, rather than Asp54 as in Escherichia coli PPiase, can abstract a proton from a water molecule to activate it for a nucleophilic attack on the diphosphate substrate, catalytic reaction mechanism, detailed overview. Structure-function analysis. Asp54 does not play a major catalytic role, and another residue (e.g. Asp89) acts as a catalytic base
additional information
-
structure comparisons of substrate-bound enzymes from Mycobacterum tuberculosis and Escherichia coli, quantum mechanics/molecular mechanics (QM/MM) analysis. Mtb PPiase exhibits significant structural differences from the well characterized Escherichia coli PPiase in the vicinity of the bound diphosphate substrate. In Mtb PPiase, Asp89, rather than Asp54 as in Escherichia coli PPiase, can abstract a proton from a water molecule to activate it for a nucleophilic attack on the diphosphate substrate, catalytic reaction mechanism, detailed overview. Structure-function analysis. Asp54 does not play a major catalytic role, and another residue (e.g. Asp89) acts as a catalytic base
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
additional information
structure-function analysis of canonical Family II PPases, catalytic reaction mechanism, detailed, overview
additional information
structure-function analysis of canonical Family II PPases, catalytic reaction mechanism, detailed, overview. An Asn residue located in the DHH domain between the active site and subunit interface as lying at the crossroads of information paths connecting all sites within the enzyme dimer
additional information
structure-function analysis of canonical Family II PPases, catalytic reaction mechanism, detailed, overview. An Asn residue located in the DHH domain between the active site and subunit interface as lying at the crossroads of information paths connecting all sites within the enzyme dimer
additional information
the Family II PPase from Staphylococcus aureus adopts the closed conformation in the absence of substrate, which causes a further induced-fit conformational change in the loop containing a conserved Arg-Lys-Lys motif. Metal-binding sites are found in the DHH domain, whereas the substrate recruits ligands from both domains. Structure-function analysis of canonical Family II PPases, catalytic reaction mechanism, detailed, overview
additional information
ThPP1 protein is a hydrolase with the sites of metal binding protein, but having a tight single domain without the transmembrane structure
additional information
-
ThPP1 protein is a hydrolase with the sites of metal binding protein, but having a tight single domain without the transmembrane structure
additional information
-
the hinge region plays an important role in opening and closing of the active site between the N- and C-terminal domains of PPase
-
additional information
-
structure comparisons of CBS-PPases and molecular dynamic simulations, overview
-
additional information
-
the catalytic residues are Asp11, Asp13, Thr113, and Lys147, structure-guided site-directed mutagenesis coupled with kinetic analysis of the mutant enzymes identifies the residues required for catalysis, substrate binding, and domain-domain association
-
additional information
-
modelling of the active site
-
additional information
-
structure-function analysis of canonical Family II PPases, catalytic reaction mechanism, detailed, overview
-
additional information
-
metal-binding sites are found in the DHH domain, whereas the substrate recruits ligands from both domains. Structure-function analysis of canonical Family II PPases, catalytic reaction mechanism, detailed, overview
-
additional information
-
structure comparisons of CBS-PPases and molecular dynamic simulations, overview
-
additional information
-
structure-function analysis of canonical Family II PPases, catalytic reaction mechanism, detailed, overview
-
additional information
-
His21 and His86 are not essential for diphosphate hydrolysis, but are responsible for a shift in the optimal pH for the reaction compared with the Escherichia coli enzyme
-
additional information
-
comparison of the primary structure of ehPPase with those of five other CBS-PPases. Molecular dynamic simulations, overview
-
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121000
recombinant His-tagged enzyme, gel filtration
122000
-
ultracentrifuge method
17000
-
4 * 17000, SDS-PAGE, 4 * 19365, calculated
18600
4 * 18600, calculated from amino acid sequence
19100
-
6 * 19100, SDS-PAGE
19272
-
6 * 19272, amino acid sequence calculation, structure-based phylogenetic tree of diphosphatases, overview
19435
-
x * 19435, calculated
20675
6 * 20675, recombinant His-tagged enzyme, mass spectrometry
20833
x * 24500, recombinant enzyme, SDS-PAGE, x * 20833, amino acid sequence calculation
20850
x * 20850, calculated from amino acid sequence
21740
2 * 21740, calculated from amino acid sequence
24350
1 * 24000, isozyme sPPase-II, SDS-PAGE, 1 * 24350, isozyme sPPase-II, mass spectrometry
24400
-
x * 24400, p26.1a, SDS-PAGE, x * 26500, p26.1b, SDS-PAGE
24484
x * 24484, isozyme PPa1, DNA sequence calculation, x * 24576, isozyme PPa4, DNA sequence calculation
24500
x * 24500, recombinant enzyme, SDS-PAGE, x * 20833, amino acid sequence calculation
24576
x * 24484, isozyme PPa1, DNA sequence calculation, x * 24576, isozyme PPa4, DNA sequence calculation
26000
1 * 26000, SDS-PAGE
26500
-
x * 24400, p26.1a, SDS-PAGE, x * 26500, p26.1b, SDS-PAGE
27000
1 x * 27000 + 1 * 57000, recombinant mutant I259V, native PAGE in absence of Mn2+, 1 * 32000 + 1 x 62000, recombinant wild-type enzyme, native PAGE in absence of Mn2+
28000
Aranda Christine
-
gel filtration
28000 - 32000
gel filtration and native PAGE
28900
calculated from predicted amino acid sequence
29850
1 * 30000, isozyme sPPase-I, SDS-PAGE, 1 * 29850, isozyme sPPase-I, mass spectrometry
32042
-
2 * 32042, amino acid sequence
32500
-
4 * 32500, SDS-PAGE
33000 - 37000
gel filtration and native PAGE
33407
2 * 33407, mass spectrometry
33494
4 * 33500, SDS-PAGE, 4 * 33494, sequence calculation
33500
4 * 33500, SDS-PAGE, 4 * 33494, sequence calculation
37000
-
x * 37000, SDS-PAGE
41000
-
amino acid sequence
43000
-
ultracentrifuge method
45000
-
x * 45000, His-tagged enzyme, SDS-PAGE
47900
-
x * 47900, calculated from amino acid sequence
55000
-
gel filtration, SDS-PAGE, amino acid sequence
56000
-
ultracentrifuge method
57000
1 x * 27000 + 1 * 57000, recombinant mutant I259V, native PAGE in absence of Mn2+, 1 * 32000 + 1 x 62000, recombinant wild-type enzyme, native PAGE in absence of Mn2+
63000 - 70000
-
gel filtration
63000 - 71000
-
sedimentation equilibrium
64000
recombinant mutant I260V, native PAGE, in presence of Mn2+
65000 - 70000
-
gel filtration
78000
recombinant wild-type enzyme, native PAGE, in presence of Mn2+
100000
-
gel filtration
110000
gel filtration
120000
native PAGE
120000
-
sedimentation equilibrium
120000
recombinant wild-type enzyme, gel filtration
19365
-
4 * 17000, SDS-PAGE, 4 * 19365, calculated
19365
-
x * 19365, calculated
19365
4 * 19365, calculated from sequence
20000
x * 20000, SDS-PAGE
20000
-
2 * 20000, SDS-PAGE
20000
-
4 * 20000, SDS-PAGE
20000
4 * 20000, SDS-PAGE
20000
-
6 * 20000, sedimentation equilibrium
20000
-
6 * 20000, (alpha3)2
20000
-
6 * 20000, homohexameric, 175 amino acid residues per subunit, wild type enzyme
20000
6 * 20000, SDS-PAGE
20000
-
x * 20000, calculated from amino acid sequence
21000
x * 21000, SDS-PAGE
21000
-
4 * 21000, SDS-PAGE
22000
2 * 22000, SDS-PAGE
22000
6 * 22000, SDS-PAGE
24000
-
amino acid sequence
24000
1 * 24000, isozyme sPPase-II, SDS-PAGE, 1 * 24350, isozyme sPPase-II, mass spectrometry
25000
-
4 * 25000, gel filtration, dimeric form also active
25000
-
2 * 25000, SDS-PAGE
30000
SDS-PAGE
30000
1 * 30000, isozyme sPPase-I, SDS-PAGE, 1 * 29850, isozyme sPPase-I, mass spectrometry
32000
-
2 * 32000, SDS-PAGE
32000
1 x * 27000 + 1 * 57000, recombinant mutant I259V, native PAGE in absence of Mn2+, 1 * 32000 + 1 x 62000, recombinant wild-type enzyme, native PAGE in absence of Mn2+
32000
-
x * 32000, calculated from amino acid sequence
32000
x * 32000, calculated from amino acid sequence
32000
x * 32000, calculated from amino acid sequence
32000
x * 32000, calculated from amino acid sequence
33000
-
2 * 33000, SDS-PAGE
33000
-
2 * 33000, SDS-PAGE
33000
DQ978330
x * 33000, recombinant enzyme, SDS-PAGE
34000
-
mass spectrometry
34000
2 * 34000, SDS-PAGE
34000
-
x * 34000, SDS-PAGE
35000
gel filtration
35000
-
2 * 35000, SDS-PAGE
35000
2 * 35000, SDS-PAGE
36000
-
SDS-PAGE
36000
-
x * 36000, SDS-PAGE
42000
-
gel filtration
42000
-
gel filtration, SDS-PAGE
50000
-
gel filtration
50000
recombinant mutant I259D, native PAGE, in absence of Mn2+
60000
-
gel filtration
60000
recombinant mutant I260D, native PAGE, in presence or absence of Mn2+
60000
recombinant mutants I260E and I259E, native PAGE, in absence of Mn2+
61000
-
gel filtration
61000
recombinant mutant I260V, native PAGE, in absence of Mn2+
62000
-
gel filtration
62000
recombinant mutant I260E, native PAGE, in presence of Mn2+
64080
-
-
64080
-
amino acid sequence
67000
-
gel filtration
67000
native PAGE and analytical ultracentrifugation
70000
-
PAGE
70000
-
2 * 70000, SDS-PAGE
80000
-
gel filtration
additional information
the enzyme is ellipsoidal with an axial ratio of 3.37, which increases in absence of divalent cation to 3.94, analytical ultracentrifugation
additional information
-
the enzyme is ellipsoidal with an axial ratio of 3.37, which increases in absence of divalent cation to 3.94, analytical ultracentrifugation
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
oligomer
x * 20000, SDS-PAGE
?
x * 24484, isozyme PPa1, DNA sequence calculation, x * 24576, isozyme PPa4, DNA sequence calculation
?
x * 32000, calculated from amino acid sequence
?
-
x * 20000, calculated from amino acid sequence
?
-
x * 20000, calculated from amino acid sequence
-
?
x * 33500, about, sequence calculation
?
x * 32000, calculated from amino acid sequence
?
x * 32000, calculated from amino acid sequence
?
-
x * 24400, p26.1a, SDS-PAGE, x * 26500, p26.1b, SDS-PAGE
?
x * 24500, recombinant enzyme, SDS-PAGE, x * 20833, amino acid sequence calculation
?
-
x * 24500, recombinant enzyme, SDS-PAGE, x * 20833, amino acid sequence calculation
-
?
DQ978330
x * 33000, recombinant enzyme, SDS-PAGE
?
-
x * 34000, SDS-PAGE
-
?
-
x * 19365, calculated
?
-
x * 19435, calculated
?
-
x * 19435, calculated
-
?
-
x * 32000, calculated from amino acid sequence
?
x * 20850, calculated from amino acid sequence
?
-
x * 45000, His-tagged enzyme, SDS-PAGE
?
-
x * 47900, calculated from amino acid sequence
dimer
-
2 * 34000, dimer when inactive
dimer
each subunit of dimeric canonical Family II PPases is formed by two domains connected by a flexible linker, with the active site located between the domains. Canonical Family II PPases structures, domain structures, overview
dimer
-
2 * 33000, SDS-PAGE
dimer
each subunit of dimeric canonical Family II PPases is formed by two domains connected by a flexible linker, with the active site located between the domains. Canonical Family II PPases structures, domain structures, overview. The isolated regulatory part (residues 66-306) of Clostridium perfringens CBS-PPase, comprised of two CBS domains and one DRTGG domain, dimerizes by forming CBS1-CBS1', CBS2-CBS2', and DRTGG-DRTGG' contacts. Two interacting pairs of CBS domains (Bateman modules) form a disk-like structure (CBS module), characteristic of CBS domain-containing proteins
dimer
-
each subunit of dimeric canonical Family II PPases is formed by two domains connected by a flexible linker, with the active site located between the domains. Canonical Family II PPases structures, domain structures, overview. The isolated regulatory part (residues 66-306) of Clostridium perfringens CBS-PPase, comprised of two CBS domains and one DRTGG domain, dimerizes by forming CBS1-CBS1', CBS2-CBS2', and DRTGG-DRTGG' contacts. Two interacting pairs of CBS domains (Bateman modules) form a disk-like structure (CBS module), characteristic of CBS domain-containing proteins
-
dimer
-
each subunit of dimeric canonical Family II PPases is formed by two domains connected by a flexible linker, with the active site located between the domains. Canonical Family II PPases structures, domain structures, overview. The isolated regulatory part (residues 66-306) of Clostridium perfringens CBS-PPase, comprised of two CBS domains and one DRTGG domain, dimerizes by forming CBS1-CBS1', CBS2-CBS2', and DRTGG-DRTGG' contacts. Two interacting pairs of CBS domains (Bateman modules) form a disk-like structure (CBS module), characteristic of CBS domain-containing proteins
-
dimer
each subunit of dimeric canonical Family II PPases is formed by two domains connected by a flexible linker, with the active site located between the domains. Canonical Family II PPases structures, domain structures, overview
dimer
-
an active dimer can be obtained using 20% isopropanol from the native hexamer
dimer
-
2 * 70000, SDS-PAGE
dimer
-
2 * 20000, SDS-PAGE
dimer
-
2 * 25000, SDS-PAGE
dimer
-
the enzyme CBS-PPase contains cystathionine beta-synthase domains
dimer
-
2 * 35000, SDS-PAGE
dimer
2 * 45000, recombinant enzyme, SDS-PAGE
dimer
-
2 * 32000, SDS-PAGE
dimer
-
2 * 32042, amino acid sequence
dimer
each subunit of dimeric canonical Family II PPases is formed by two domains connected by a flexible linker, with the active site located between the domains. Canonical Family II PPases structures, domain structures, overview
dimer
the enzyme structure consists of two domains, comprising residues 1-191 and 198-311, respectively, with the active site located between them, overview
dimer
each subunit of dimeric canonical Family II PPases is formed by two domains connected by a flexible linker, with the active site located between the domains. Canonical Family II PPases structures, domain structures, overview
dimer
2 * 33407, mass spectrometry
dimer
1 x * 27000 + 1 * 57000, recombinant mutant I259V, native PAGE in absence of Mn2+, 1 * 32000 + 1 x 62000, recombinant wild-type enzyme, native PAGE in absence of Mn2+
dimer
each subunit of dimeric canonical Family II PPases is formed by two domains connected by a flexible linker, with the active site located between the domains. Canonical Family II PPases structures, domain structures, overview
dimer
-
1 x * 27000 + 1 * 57000, recombinant mutant I259V, native PAGE in absence of Mn2+, 1 * 32000 + 1 x 62000, recombinant wild-type enzyme, native PAGE in absence of Mn2+
-
dimer
-
2 * 33407, mass spectrometry
-
dimer
-
each subunit of dimeric canonical Family II PPases is formed by two domains connected by a flexible linker, with the active site located between the domains. Canonical Family II PPases structures, domain structures, overview
-
dimer
-
2 * 33000, SDS-PAGE
dimer
-
TgPPase forms dimers in solution and in the crystal. Structure comparisons of the enzyme from Plasmodium falciparum (PfPPase) and Toxoplasma gondii (TgPPase), overview
dimer
-
the homodimer contains several transmembrane segments, the conserved transmembrane segment 5 at the N-terminal side near the putative substrate binding loop contains the GYG motif which is important in maintaining structure and function of the enzyme, overview
hexamer
6 * 20000, SDS-PAGE
hexamer
-
6 * 20000, sedimentation equilibrium
hexamer
-
6 * 20000, (alpha3)2
hexamer
-
6 * 20000, homohexameric, 175 amino acid residues per subunit, wild type enzyme
hexamer
-
composed of two trimers
hexamer
-
native form, composed of two trimers
hexamer
-
dimer of active trimers
hexamer
-
two trimers, preparation of wild-type trimers by incubation of enzyme in 0.1 M MES-NaOH, pH 5.3, for 20 h at 25°C, and of the mutant K112Q in 0.1 M Na-citrate buffer, pH 4.5, for 20 h at 25°C
hexamer
-
6 * 19100, SDS-PAGE
hexamer
-
6 * 19272, amino acid sequence calculation, structure-based phylogenetic tree of diphosphatases, overview
hexamer
6 * 20675, recombinant His-tagged enzyme, mass spectrometry
hexamer
-
6 * 19100, SDS-PAGE
-
hexamer
-
dimeric trimer, crystal structure
hexamer
6 * 19 187, mass spectrometry
hexamer
6 * 22000, SDS-PAGE
homodimer
-
-
homodimer
2 * 35000, SDS-PAGE
homodimer
-
2 * 35000, SDS-PAGE
-
homodimer
2 * 22000, SDS-PAGE
homodimer
2 * 21740, calculated from amino acid sequence
homodimer
-
2 * 22000, SDS-PAGE
-
homodimer
-
2 * 21740, calculated from amino acid sequence
-
homodimer
2 * 34000, SDS-PAGE
homodimer
-
2 * 34000, SDS-PAGE
-
homohexamer
6 * 25000, crecombinant detagged enzyme, SDS-PAGE
homohexamer
6 * 27000, SDS-PAGE
homohexamer
6 * 24500, dimer of trimers, recombinant detagged enzyme, SDS-PAGE
homotetramer
4 * 20000, SDS-PAGE
homotetramer
4 * 18600, calculated from amino acid sequence
monomer
1 * 24000, isozyme sPPase-II, SDS-PAGE, 1 * 24350, isozyme sPPase-II, mass spectrometry
monomer
1 * 30000, isozyme sPPase-I, SDS-PAGE, 1 * 29850, isozyme sPPase-I, mass spectrometry
monomer
-
1 * 60000, SDS-PAGE
monomer
-
1 * 55000, SDS-PAGE
monomer
1 * 26000, SDS-PAGE
monomer
-
1 * 26000, SDS-PAGE
-
tetramer
-
4 * 20000, SDS-PAGE
tetramer
4 * 33500, SDS-PAGE, 4 * 33494, sequence calculation
tetramer
-
4 * 33500, SDS-PAGE, 4 * 33494, sequence calculation
-
tetramer
-
4 * 32500, SDS-PAGE
tetramer
-
4 * 25000, gel filtration, dimeric form also active
tetramer
-
4 * 25000, gel filtration, dimeric form also active
-
tetramer
-
4 * 21000, SDS-PAGE
tetramer
-
4 * 17000-18000, SDS-PAGE
tetramer
-
4 * 17000, SDS-PAGE, 4 * 19365, calculated
tetramer
4 * 19365, calculated from sequence
tetramer
-
4 * 21000, SDS-PAGE
-
tetramer
-
4 * 19365, calculated from sequence
-
trimer
-
3 * 34000, trimer when active
trimer
-
dissociated variant, SDS-PAGE
additional information
circular dichroism spectrum, secondary structure of isozymes, overview
additional information
topology and conformation of the PPA1 subunits, comparison to the enzyme from Medicago truncatula. The N-terminal peptide of immature AtPPA1 is mostly disordered
additional information
-
topology and conformation of the PPA1 subunits, comparison to the enzyme from Medicago truncatula. The N-terminal peptide of immature AtPPA1 is mostly disordered
additional information
-
B-cell epitope mapping of the recombinant enzyme, epitopes are spread across the whole enzyme molecule
additional information
structure modeling and 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
additional information
-
structure modeling and 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
additional information
-
structure modeling and 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
-
additional information
peptide mass fingerprint analysis of isozyme sPPase-I
additional information
peptide mass fingerprint analysis of isozyme sPPase-I
additional information
-
peptide mass fingerprint analysis of isozyme sPPase-I
additional information
peptide mass fingerprint analysis of isozyme sPPase-II
additional information
peptide mass fingerprint analysis of isozyme sPPase-II
additional information
-
peptide mass fingerprint analysis of isozyme sPPase-II
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
additional information
ThPP1 gene exhibits a typical structural characteristic of PPase family. ThPP1 protein is a hydrolase with the sites of metal binding protein, but having a tight single domain without the transmembrane structure
additional information
-
ThPP1 gene exhibits a typical structural characteristic of PPase family. ThPP1 protein is a hydrolase with the sites of metal binding protein, but having a tight single domain without the transmembrane structure
additional information
three-dimensional homology modeling suggests HvPPA to have an OB fold consisting of a central beta-barrel structure and alpha-helices associated in a beta1-8-alpha1-beta9-alpha2 topology and to homo-oligomerize into a trimer and/or dimer of trimers
additional information
-
three-dimensional homology modeling suggests HvPPA to have an OB fold consisting of a central beta-barrel structure and alpha-helices associated in a beta1-8-alpha1-beta9-alpha2 topology and to homo-oligomerize into a trimer and/or dimer of trimers
additional information
structure analysis, PPase comprises three alpha-helices and nine beta-strands and folds as a barrel structure, it forms a hexamer in both the solution and crystal states, and each monomer has its own PPi-binding site
additional information
-
structure analysis, PPase comprises three alpha-helices and nine beta-strands and folds as a barrel structure, it forms a hexamer in both the solution and crystal states, and each monomer has its own PPi-binding site
additional information
topology and conformation of the PPA1 subunits, comparison to the enzyme from Arabidospis thaliana
additional information
-
topology and conformation of the PPA1 subunits, comparison to the enzyme from Arabidospis thaliana
additional information
structure comparison of family I enzymes, overview
additional information
-
structure comparison of family I enzymes, overview
additional information
-
structure comparison of family I enzymes, overview
-
additional information
enzyme PfPPase exists predominantly as a dimer in solution with a minor tetrameric peak. PfPPase low complexity asparagine-rich N-terminal region mediates its dimerization. Structure comparisons of the enzyme from Plasmodium falciparum (PfPPase) and Toxoplasma gondii (TgPPase), overview
additional information
-
enzyme PfPPase exists predominantly as a dimer in solution with a minor tetrameric peak. PfPPase low complexity asparagine-rich N-terminal region mediates its dimerization. Structure comparisons of the enzyme from Plasmodium falciparum (PfPPase) and Toxoplasma gondii (TgPPase), overview
additional information
-
structural basis for the high thermostability
additional information
the free N- and C-terminal domains do not interact productively, when mixed together, the interdomain region has the function of a mechanical hinge, structure modelling
additional information
-
the free N- and C-terminal domains do not interact productively, when mixed together, the interdomain region has the function of a mechanical hinge, structure modelling
additional information
the hinge region plays an important role in opening and closing of the active site between the N- and C-terminal domains of PPase. Family II PPases are dimer under physiological conditions with Mn2+ present, and may dissociate into monomers at low enzyme concentration in the absence of Mn2+
additional information
-
the hinge region plays an important role in opening and closing of the active site between the N- and C-terminal domains of PPase. Family II PPases are dimer under physiological conditions with Mn2+ present, and may dissociate into monomers at low enzyme concentration in the absence of Mn2+
additional information
-
the hinge region plays an important role in opening and closing of the active site between the N- and C-terminal domains of PPase. Family II PPases are dimer under physiological conditions with Mn2+ present, and may dissociate into monomers at low enzyme concentration in the absence of Mn2+
-
additional information
-
the free N- and C-terminal domains do not interact productively, when mixed together, the interdomain region has the function of a mechanical hinge, structure modelling
-
additional information
-
analysis of amino acid composition and comparison with Escherichia coli, saccharomyces cerevisiae and Bacillus sp. enzymes
additional information
-
analysis of amino acid composition and comparison with Escherichia coli, saccharomyces cerevisiae and Bacillus sp. enzymes
-
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purified recombinant enzyme, hanging drop vapor diffusion method, mixing of 7.5-10 mg/ml protein with precipitant solution containing 100 mM succinic acid, pH 7.0, and 15% PEG3350, or 100 mM bicine, pH 9.0, 7% PEG 6000, and 3 mM MgCl2 for the Mg2+-bound enzyme, 2 weeks, 19°C, 20% glycerol or PEG400 as cryoprotectants, X-ray diffraction structure determination and analysis at 1.93 A and 1.83 A resolution, respectively, structure modelling. Growth of AtPPA1 crystal is strongly correlated with the progression of proteolysis
purified recombinant wild-type and mutant enzymes in complex with substrate analogue imidodiphosphate, PNP, and/or inhibitor fluoride, 35-40 mg/ml protein in 83mM TES/K+, pH 7.2, 17 mM KCl and 0.05 mM EGTA is mixed with 5 mM MgCl2 and 10 mM NaF, 1 mM PNP, sitting drop vapour diffusion method, 4°C, 3:2 ratio of protein to well solution, the latter containing 100 mM HEPES/K+, pH 7.5, 2.3-2.5 M ammonium sulfate, 3-4% PEG 400, 2-3 days, X-ray diffraction structure determination and anaylsis at 1.75-2.15 A resolution, the mutant H98Q crystals do not contain fluoride ions
purified recombinant His-tagged wild-type and mutant BT2127 variants, sitting-drop vapor diffusion method, X-ray diffraction structure determination and analysis at
regulatory part of Clostridium perfringens CBS-PPase complexed with AMP, PDB ID 3L31
different forms depending on the presence of NH4Cl or (NH4)2SO4 (alpha3'alpha3'')
-
purified enzyme, X-ray diffraction structure determination and analysis
-
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
purified recombinant enzyme, free and in complex with diphosphate, hanging drop vapor diffusion method, for the free enzyme: 20 mg/ml protein in 20 mM Tris-HCl, pH 7.5, and 200 mM NaCl, precipitation with 1.44 M sodium citrate, and 100 mM Na HEPES, pH 7.4, 6 days at 25°C, for the diphosphate-bound enzyme: the diphosphate-PPase complex from the same buffer condition as the free enzyme with a 1:7.5 molar excess of K4diphosphate in the absence of divalent metal ion, the complex crystals are grown in the same buffer as free PPase using 3.6 M sodium formate as a precipitant, 3 days at 25°C, X-ray diffraction structure determination and analysis at 1.9 A and 2.3 A resolution, respectively, molecular replacement
purified recombinant His-tagged selenomethionine-enzyme, hanging drop vapour diffusion method, 14 mg/ml protein in 50 mM Tris-HCl, pH 7.0, 0.1 M NaCl, 1 mM 2-mercaptoethanol, and 10 mM MgCl2, against a reservoir solution containing 36% v/v methylpentanediol, 0.2 M MgCl2, and 0.1 M imidazole, pH 8.0, X-ray diffraction structure determination and analysis at 2.6 A resolution
-
purified recombinant enzyme, hanging drop vapor diffusion method, mixing of 7.7 mg/ml bromelain-treated protein with precipitant solution containing 1.6% Tacsimate, pH 5.0, 80 mM tribasic sodium citrate, pH 5.6, 12.8% PEG 3350, and 20% glycerol, 2 days, 19°C, X-ray diffraction structure determination and analysis at 1.84-2.89A resolution, structure modelling
purified enzyme bound to catalytic metals, to substrate diphosphate, and to one or two inorganic phosphate ions, hanging drop vapour diffusion method, mixing of 0.001 ml of 14 mg/ml protein in 40 mM Tris-HCl, pH 8.0, and 100 mM NaCl, with 0.001 ml of reservoir solution containing 1.65 M NaKHPO4, 100 mM HEPES, pH 7.75, and 2 mM CaCl2, xthe crystals of Mtb PPiase in complex with two phosphate ions are obtained with the reservoir solution composed of 1.6 M KH2PO4, 100 mM HEPES, pH 7.75, and 2 mM CaCl2, and the crystals of Mtb PPiase in complex with one phosphate are obtained with the reservoir solution containing 1.57 M NaKHPO4, 100 mM HEPES pH 7.75 and 2 mM MnCl2, 22°C, X-ray diffraction structure determination and analysis at 1.85-3.30 A resolution, molecular replacement with the structure of the Mtb PPiase-Mg2+ complex as a search model
purified recombinant detagged enzyme in complex with inhibitor 2,4-bis(aziridin-1-yl)-6-(1-phenylpyrrol-2-yl)-S-triazine or N2,N4-dimethyl-6-(1-phenyl-1H-pyrrol-2-yl)-1,3,5-triazine-2,4-diamine, hanging drop vapour diffusion method, mixing of 7 mg/ml protein in 40 mM Tris-HCl pH 8.0, 100 mM NaCl, and 2 mM 2-mercaptoethanol, with reservoir solution containing 0.1 M HEPES pH 7.5, 1.6 M NaH2PO4, and 0.2 M KH2PO4, or 0.1 M HEPES pH 7.75, 1.4 M KH2PO4, and 2 mM CaCl2, respectively, 22°C, overnight, X-ray diffraction structure determination and analysis at 2.65 A and 2.45 A resolution, respectively. 2,4-Bis(aziridin-1-yl)-6-(1-phenylpyrrol-2-yl)-S-triazine is co-crystallized, while N2,N4-dimethyl-6-(1-phenyl-1H-pyrrol-2-yl)-1,3,5-triazine-2,4-diamine is bound by soaking
purified recombinant Rv3628, hanging drop vapour diffusion method, mixing of 0.001 ml protein in150 mM Na HEPES, pH 7.0, and 0.001 ml reservoir solution, containing 1.6 M NaKHPO4, pH 7.0, and equilibration against 1 ml reservoir solution, X-ray diffraction structure determination and analysis at 1.5 A resolution, modeling
purified recombinant detagged wild-type enzyme complexed with Mg2+, vapor diffusion method, 10 mg/ml seleno-methionine substituted PfPPase in buffer are mixed with condition 8% Tacsimate, pH 8.0, and 20% PEG 3350, 20°C, 4 days, X-ray diffraction structure determination and analysis at 2.35 A resolution
purified recombinant enzyme, 20 mg/ml protien hanging drop vapour diffusion method, 3,8% PEG 4000, 0.1 M Na-acetate, pH 5.0-5.2, and 0.02 M MgCl2, asymmetric trimeric crystals, dimerization to hexamers, X-ray diffraction structure determination and analysis at 2.66 A resolution
-
purified recombinant enzyme, hanging drop vapour diffusion method, 20 mg/ml protein in 5 mM Tris-HCl, pH 8.0, and 50 mM NaCl, 18°C, 0.001 ml versus 0.001 ml reservoir solution containing 8% PEG 4000, 0.1 M sodium acetate, pH 4.5, for needle-shaped crystals, and 3.8% PEG 4000, 0.1 M sodium acetate, pH 5.0-5.2, for large crystals, X-ray diffraction structure determination and analysis at 2.7 A resolution
-
purified recombinant wild-type enzyme or mutants E48D, Y93F, D115E, D117E, D120E, D120N, and D152E in 60 mM MES, pH 6.0, and 10 mM Mg2+, 4°C, 0.008 ml sitting drops in the presence of 5 mM Mg2+, 1 mM PO43-, and a MPD concentration gradient from 16 to 19%, 2-4 weeks, cryoprotection by soaking of crystals at 4°C in 32% MPD, 30 mM MES, 10 mM Mg2+, and 1 mM PO43- for a few min, X-ray diffraction structure determination and analysis at 1.5-1.9 A resolution
isoform PpaC in complex with Mn2+, hanging drop vapor diffusion method, using 1.32 M ammonium citrate tribasic
complexed enzyme with each enzyme monomer containing the diphosphate analogue imidodiphosphate and three metal ions per active site: two Mn2+ ions in sites M1 and M2 and an Mg2+ ion in site M3, X-ray diffraction structure determination and analysis at 2.8 A resolution, molecular replacement
purified recombinant enzyme, 5-20 mg/ml protein in 20 mM Tris-HCl, pH 7.0, hanging drop vapour diffusion method, 0.001 ml of protein and well solution are mixed, 2 weeks at room temperature, X-ray diffraction structure determination and analysis at 2.8 A resolution
at 2.7 A resolution. Comparison with Thermus thermophilus and Escherichia coli enzymes
CD and FTIR spectra demonstrate a similar overall fold for enzyme and PPases from Escherichia coli and Thermus thermophilus
-
strucutural model based on structure of Thermus thermophilus enzyme
-
sitting drop vapor diffusion method, using 25% (w/v) 2-methyl-2,4-pentanediol, 100 mM sodium acetate pH 4.6, 10 mM calcium chloride, 2 mM ammonium sulfate
purified enzyme, vapour diffusion method, mixing of 10 mg/ml protein solution with 10% PEG 4000, 20% glycerol, 0.03 M glycols, and 0.1 M HEPES/MOPS, pH 7.5, 20°C, 6-8 days, X-ray diffraction structure determination and analysis at 2.35 A resolution, molecular replacement method using ScPPase (PDB ID 1WGJ) as a template
-
vapor diffusion method, using 15-20% (w7v) 2,4-methylpentanediol, and 3% (w/v) PEG4000
-
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D103N
site-directed mutagenesis
D135N
site-directed mutagenesis
D19A
site-directed mutagenesis
D98N
site-directed mutagenesis
D19A
-
site-directed mutagenesis
-
H98Q
the mutant shows highly reduced activity compared to the wild-type enzyme, crystal structure determination and comparison of substrate/inhibitor binding to the wild-type enzyme
D11N
site-directed mutagenesis, inactive mutant
D13A
site-directed mutagenesis, inactive mutant
D13N
site-directed mutagenesis, inactive mutant
E47A
site-directed mutagenesis, inactive mutant
E47D
site-directed mutagenesis, inactive mutant
E47N
site-directed mutagenesis, inactive mutant
E47Q
site-directed mutagenesis, altered kinetics compared to the wild-type enzyme
H23A
site-directed mutagenesis, altered kinetics compared to the wild-type enzyme
K147A
site-directed mutagenesis, inactive mutant
K79A
site-directed mutagenesis, inactive mutant
M20A
site-directed mutagenesis, altered kinetics compared to the wild-type enzyme
M20K
site-directed mutagenesis, altered kinetics compared to the wild-type enzyme
M20L
site-directed mutagenesis, altered kinetics compared to the wild-type enzyme
N172A
site-directed mutagenesis, altered kinetics compared to the wild-type enzyme
Q117A
site-directed mutagenesis, inactive mutant
R49A
site-directed mutagenesis, inactive mutant
S115A
site-directed mutagenesis, altered kinetics compared to the wild-type enzyme
S19A
site-directed mutagenesis, inactive mutant
S80A
site-directed mutagenesis, altered kinetics compared to the wild-type enzyme
T113A
site-directed mutagenesis, altered kinetics compared to the wild-type enzyme
T50A
site-directed mutagenesis, altered kinetics compared to the wild-type enzyme
Y76F
site-directed mutagenesis, inactive mutant
D13A
-
site-directed mutagenesis, inactive mutant
-
E47A
-
site-directed mutagenesis, inactive mutant
-
K79A
-
site-directed mutagenesis, inactive mutant
-
M20L
-
site-directed mutagenesis, altered kinetics compared to the wild-type enzyme
-
S19A
-
site-directed mutagenesis, inactive mutant
-
N312S
site-directed mutagenesis, the mutant shows altered Mg2+ dependence and kinetics compared to wild-type. The N312S substitution in dhPPase abolishes kinetic cooperativity and reverses the effect of Ap4A on it. In the presence of 0.05 mMATP and 5 mM Mg2+, the hydrolysis kinetics of N312S-dhPPase remains non-cooperative, the catalytic constant increases 1.5fold, and the average Km value increases about 5.5fold
R276A
site-directed mutagenesis, the mutant retains about 50% catalytic efficiency compared to wild-type, negative co-operativity is retained in the R276A variant in the presence of mononucleotides but is reversed by diadenosine tetraphosphate. The R276A substitution abolishes activation by ATP and diadenosine tetraphosphate, while preserving the ability to bind them
R276E
site-directed mutagenesis, the mutant retains about 50% catalytic efficiency and exhibits reduced kinetic cooperativity compared to wild-type
R276K
site-directed mutagenesis, the mutant retains about 50% catalytic efficiency and exhibits reduced kinetic cooperativity compared to wild-type
D102N
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
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
D70E
-
strongly decreased affinity for diphosphate
D70N
site-directed mutagenesis, the active site residue mutation does only marginally influence the pH-dependence of fluoride inhibition
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
C16S
site-directed mutagenesis, the mutant shows a loss of 50% activity and a reduction in sensitivity to reductants and oxidized glutathione compared to the wild-type enzyme. In addition, the replacement causes a considerable disruption in thermostability, C16S substitution destabilizes PPase through impairing trimer-trimer interactions
D69G
site-directed mutagenesis, inactive mutant
K103A
site-directed mutagenesis, inactive mutant
Y140F
site-directed mutagenesis, the mutant shows 78% reduced activity compared to the wild-type enzyme
D103N
site-directed mutagenesis
D135N
site-directed mutagenesis
D98N
site-directed mutagenesis
Y169A
-
site-directed mutagenesis of the CBS domain residue, the mutant shows altered kinetics with adenine nucleotides compared to the wild-type enzyme
D54N
site-directed mutagenesis, the mutant behaves similar to the wild-type enzyme
D57N
site-directed mutagenesis, the mutant shows reduced activity and altered kinetics compared to wild-type
D89N
site-directed mutagenesis, the mutant shows reduced activity and altered kinetics compared to wild-type
D198N
site-directed mutagenesis, the mutant shows 5fold reduced kcat compared to wild-type
D203N
site-directed mutagenesis, the mutant shows 600fold reduced activity compared to wild-type
D235N
site-directed mutagenesis, the mutant shows 6fold reduced kcat compared to wild-type
K136R
site-directed mutagenesis, the mutant shows a 40fold increased Km for diphosphate compared to wild-type
R158K
site-directed mutagenesis, the mutant shows a moderately altered kcat and Km for diphosphate compared to wild-type
D115E
site-directed mutagenesis, the mutation affects metal binding and the hydrogen bonding network in the active, in contrary to the wild-type enzyme, the mutant shows an open conformation variant of the hitherto unobserved two-phosphate and two bridging water active site, crystal structure determination with bound phosphate and Mg2+, and comparison to the wild-type enzyme structure
D117E
site-directed mutagenesis, crystal structure determination with bound phosphate and Mg2+, and comparison to the wild-type enzyme structure
D120E
site-directed mutagenesis, crystal structure determination with bound phosphate and Mg2+, and comparison to the wild-type enzyme structure
D120N
site-directed mutagenesis, crystal structure determination with bound phosphate and Mg2+, and comparison to the wild-type enzyme structure
D152E
site-directed mutagenesis, crystal structure determination with bound phosphate and Mg2+, and comparison to the wild-type enzyme structure
E48D
site-directed mutagenesis, crystal structure determination with bound phosphate and Mg2+, and comparison to the wild-type enzyme structure
K193R
-
decrease in activity
K56R
-
large decrease in activity
R78K
-
increased activity
G190A
site-directed mutagenesis, the mutant shows altered kinetic parameters and reduced activity compared to the wild-type enzyme
G190W
site-directed mutagenesis, the mutant shows altered kinetic parameters and reduced activity compared to the wild-type enzyme
I259D
site-directed mutagenesis, almost inactive mutant
I259E
site-directed mutagenesis, almost inactive mutant
I259V
site-directed mutagenesis, the mutant shows 20% reduced activity compared to the wild-type enzyme
I260D
site-directed mutagenesis, the mutant shows 86% reduced activity compared to the wild-type enzyme
I260E
site-directed mutagenesis, the mutant shows 89% reduced activity compared to the wild-type enzyme
I260V
site-directed mutagenesis, the mutant shows 20% increased activity compared to the wild-type enzyme, the mutant is activable by NaF in contrast to the wild-type enzyme
T191G
site-directed mutagenesis, the mutant shows altered kinetic parameters and reduced activity compared to the wild-type enzyme
G190A
-
site-directed mutagenesis, the mutant shows altered kinetic parameters and reduced activity compared to the wild-type enzyme
-
G190W
-
site-directed mutagenesis, the mutant shows altered kinetic parameters and reduced activity compared to the wild-type enzyme
-
I259D
-
site-directed mutagenesis, almost inactive mutant
-
I259E
-
site-directed mutagenesis, almost inactive mutant
-
I259V
-
site-directed mutagenesis, the mutant shows 20% reduced activity compared to the wild-type enzyme
-
I260D
-
site-directed mutagenesis, the mutant shows 86% reduced activity compared to the wild-type enzyme
-
I260E
-
site-directed mutagenesis, the mutant shows 89% reduced activity compared to the wild-type enzyme
-
T191G
-
site-directed mutagenesis, the mutant shows altered kinetic parameters and reduced activity compared to the wild-type enzyme
-
D169A
mutant enzyme shows 1.8% of wild-type pyrophosphatase activity
G163A
mutant enzyme shows 3.1% of wild-type pyrophosphatase activity
H125A
mutant enzyme shows 7.5% of wild-type pyrophosphatase activity
H165A
mutant enzyme shows 0.4% of wild-type pyrophosphatase activity
P103A
mutant enzyme shows 3.3% of wild-type pyrophosphatase activity
P122A
mutant enzyme shows 8.0% of wild-type pyrophosphatase activity
P167A
mutant enzyme shows 1.8% of wild-type pyrophosphatase activity
R159A
mutant enzyme shows 1.1% of wild-type pyrophosphatase activity
S123A
mutant enzyme shows 16% of wild-type pyrophosphatase activity
S158A
mutant enzyme shows 2.0% of wild-type pyrophosphatase activity
D169A
-
mutant enzyme shows 1.8% of wild-type pyrophosphatase activity
-
H125A
-
mutant enzyme shows 7.5% of wild-type pyrophosphatase activity
-
R159A
-
mutant enzyme shows 1.1% of wild-type pyrophosphatase activity
-
S123A
-
mutant enzyme shows 16% of wild-type pyrophosphatase activity
-
S158A
-
mutant enzyme shows 2.0% of wild-type pyrophosphatase activity
-
G119A
the mutant shows less than 50% activity towards diphosphate and increased activity towards ATP compared to the wild type enzyme
G119S
the mutant shows about 140% activity towards diphosphate and increased activity towards ATP and dATP compared to the wild type enzyme
D190A
the Na+ dose dependency of the D190A variant closely resembles that of the wild-type enzyme
D703N
the variant exhibits a much lower slope on the rate vs [Na+] plot than the wild-type enzyme at all of the K+ concentrations examined
E41Q/E42Q
significant decrease in the nucleoside triphosphate pyrophosphohydrolase activity and concomitant increases in the pyrophosphatase activity
E45Q
significant decrease in the nucleoside triphosphate pyrophosphohydrolase activity and concomitant increases in the pyrophosphatase activity
E61Q
significant decrease in the nucleoside triphosphate pyrophosphohydrolase activity and concomitant increases in the pyrophosphatase activity
K118A
significant decrease in the nucleoside triphosphate pyrophosphohydrolase activity and concomitant increases in the pyrophosphatase activity
R97A/R98A
significant decrease in the nucleoside triphosphate pyrophosphohydrolase activity and concomitant increases in the pyrophosphatase activity
D190A
-
the Na+ dose dependency of the D190A variant closely resembles that of the wild-type enzyme
-
D703N
-
the variant exhibits a much lower slope on the rate vs [Na+] plot than the wild-type enzyme at all of the K+ concentrations examined
-
E41Q/E42Q
-
significant decrease in the nucleoside triphosphate pyrophosphohydrolase activity and concomitant increases in the pyrophosphatase activity
-
E45Q
-
significant decrease in the nucleoside triphosphate pyrophosphohydrolase activity and concomitant increases in the pyrophosphatase activity
-
E61Q
-
significant decrease in the nucleoside triphosphate pyrophosphohydrolase activity and concomitant increases in the pyrophosphatase activity
-
K118A
-
significant decrease in the nucleoside triphosphate pyrophosphohydrolase activity and concomitant increases in the pyrophosphatase activity
-
R97A/R98A
-
significant decrease in the nucleoside triphosphate pyrophosphohydrolase activity and concomitant increases in the pyrophosphatase activity
-
A226S
-
site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme
A238S
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
E225A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
F224A
-
site-directed mutagenesis, the mutant shows slightly increased activity compared to the wild-type enzyme
F240A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
G221A
-
site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme
G222A
-
site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme
G229A
-
site-directed mutagenesis, the mutant shows 50% reduced activity compared to the wild-type enzyme
G231A
-
site-directed mutagenesis, the mutant shows 50% reduced activity compared to the wild-type enzyme
G233A
-
site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme
G234A
-
site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme
G241A
-
site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme
I227A
-
site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme
L223A
-
site-directed mutagenesis, the mutant shows slightly increased activity compared to the wild-type enzyme
L232A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
L239A
-
site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme
M237A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
R242A
-
site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme
S235A
-
site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme
S236A
-
site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme
T228A
-
site-directed mutagenesis, the mutant shows slightly increased activity compared to the wild-type enzyme
Y230A
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
N312S
-
site-directed mutagenesis, the mutant shows altered Mg2+ dependence and kinetics compared to wild-type. The N312S substitution in dhPPase abolishes kinetic cooperativity and reverses the effect of Ap4A on it. In the presence of 0.05 mMATP and 5 mM Mg2+, the hydrolysis kinetics of N312S-dhPPase remains non-cooperative, the catalytic constant increases 1.5fold, and the average Km value increases about 5.5fold
-
N312S
-
site-directed mutagenesis, the mutant shows altered Mg2+ dependence and kinetics compared to wild-type. The N312S substitution in dhPPase abolishes kinetic cooperativity and reverses the effect of Ap4A on it. In the presence of 0.05 mMATP and 5 mM Mg2+, the hydrolysis kinetics of N312S-dhPPase remains non-cooperative, the catalytic constant increases 1.5fold, and the average Km value increases about 5.5fold
-
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, crystal structure determination and analysis and comparison to the wild-type structure
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
Y55F
site-directed mutagenesis, the active site residue mutation does only marginally influence the pH-dependence of fluoride inhibition
S213N
site-directed mutagenesis, the substitution confers significant negative cooperativity on the enzyme, decreasing the Hill coefficient to 0.7, and the Km2/Km1 ratio increases to approximately 13 over the entire range of Mg2+ concentrations. The catalytic constant decreases by a factor of 4.5 upon Ser213 replacement
S213N
-
site-directed mutagenesis, the substitution confers significant negative cooperativity on the enzyme, decreasing the Hill coefficient to 0.7, and the Km2/Km1 ratio increases to approximately 13 over the entire range of Mg2+ concentrations. The catalytic constant decreases by a factor of 4.5 upon Ser213 replacement
-
Y93F
-
large decrease in activity
Y93F
site-directed mutagenesis, the mutation affects metal binding and the hydrogen bonding network in the active, crystal structure determination with bound phosphate and Mg2+, and comparison to the wild-type enzyme structure
R295A
inactive
additional information
construction of an N-truncated variant of AtPPA1 with residues 1-29 deleted (DELTA(1-29)) produced using construct pMCSG48-AtPPA1-DELTA(1-29)
additional information
-
construction of an N-truncated variant of AtPPA1 with residues 1-29 deleted (DELTA(1-29)) produced using construct pMCSG48-AtPPA1-DELTA(1-29)
additional information
construction of the vacuolar H+-translocating pyrophosphatase (H+-PPase) loss-of-function fugu5 mutant that is susceptible to drought and displays pleotropic postgerminative growth defects due to excess diphosphate. Specific removal of PPi from a fugu5 mutant background (i.e. in the pAVP1::IPP1 transgenic line) rescues all recognized developmental defects and vigorously enhances growth. The GC1 promoter is properly expressed in guard cells in the fugu5-1 background. Construction and phenotypic analyses of the pGC1::IPP1 line in the fugu5-1 background expressing the soluble PPase from Saccharomyces cerevisiae strain 288c. pGC1::IPP1/fugu5-1 displays typical oblong cotyledons reminiscent of fugu5 mutants, but expression of IPP1 in the guard cells of the pGC1::IPP1/fugu5-1 lines does not affect the palisade cell phenotype, phenotypes, overview
additional information
-
PPase gene silencing by RNA interference, RNAi-mediated gene disruption suppressed native protein expression and mRNA levels in worm lung-stage larvae, recombinant AsPPase-immunized mice are protected from migration of challenge Ascaris suum larvae through the lungs
additional information
isolation of pyp-1 deletion mutant, a constructed null mutant of pyp-1 reveals a developmental arrest at early larval stages and exhibits gross defects in intestinal morphology and function, phenotype, overview
additional information
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isolation of pyp-1 deletion mutant, a constructed null mutant of pyp-1 reveals a developmental arrest at early larval stages and exhibits gross defects in intestinal morphology and function, phenotype, overview
additional information
naturally occuring ehPPase mutant containing an inherent mutation in an otherwise conserved asparagine residue in a loop near the active site exhibits noncooperative hydrolysis kinetics
additional information
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naturally occuring ehPPase mutant containing an inherent mutation in an otherwise conserved asparagine residue in a loop near the active site exhibits noncooperative hydrolysis kinetics
-
additional information
-
naturally occuring ehPPase mutant containing an inherent mutation in an otherwise conserved asparagine residue in a loop near the active site exhibits noncooperative hydrolysis kinetics
-
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
additional information
naturally occuring ehPPase mutant containing an inherent mutation in an otherwise conserved asparagine residue in a loop near the active site exhibits noncooperative hydrolysis kinetics
additional information
-
naturally occuring ehPPase mutant containing an inherent mutation in an otherwise conserved asparagine residue in a loop near the active site exhibits noncooperative hydrolysis kinetics
-
additional information
isolated soluble inorganic diphosphatase gene ThPP1 from Thellungiella halophila is transformed this gene into the Oryza sativa subsp. japonica cv. Kitaake to investigate the functional roles of the ThPP1 gene under saline-alkali stresses. Two independent transgenic lines of T3 generation are subjected to the alkali stress by NaHCO3 and Na2CO3, then the profiles of physiological changes and the transcriptome-based differentially expressions in the transgenic rice are evaluated. Rice transcriptome sequencing, phenotypes, overview. The transgenic rice shows beneficial physiological changes under alkali stress. The accumulations of sucrose and starch in the leaves of the transgenic lines are significantly higher than those of the wild-type rice plants
additional information
-
isolated soluble inorganic diphosphatase gene ThPP1 from Thellungiella halophila is transformed this gene into the Oryza sativa subsp. japonica cv. Kitaake to investigate the functional roles of the ThPP1 gene under saline-alkali stresses. Two independent transgenic lines of T3 generation are subjected to the alkali stress by NaHCO3 and Na2CO3, then the profiles of physiological changes and the transcriptome-based differentially expressions in the transgenic rice are evaluated. Rice transcriptome sequencing, phenotypes, overview. The transgenic rice shows beneficial physiological changes under alkali stress. The accumulations of sucrose and starch in the leaves of the transgenic lines are significantly higher than those of the wild-type rice plants
additional information
-
immobilization of the purified enzyme on hydrophobic supports polycephamide and lysopolycephamide allows preservation of 24.2% and 17.3% of the starting catalytic activities with activity of imMobilized enzymes per gram support of 507 and 285 U/g, respectively
additional information
no mutations of isozyme PPase2 are involved in the human disease mictochondrial DNA depletion syndrome, MDS
additional information
no mutations of isozyme PPase2 are involved in the human disease mictochondrial DNA depletion syndrome, MDS
additional information
-
no mutations of isozyme PPase2 are involved in the human disease mictochondrial DNA depletion syndrome, MDS
additional information
MdVHP1 overexpression in apple shoot culture, phenotypes, overview
additional information
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MdVHP1 overexpression in apple shoot culture, phenotypes, overview
additional information
construction of the truncated version of MtPPA1-DELTA(1-30), which is not possible to express
additional information
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construction of the truncated version of MtPPA1-DELTA(1-30), which is not possible to express
additional information
OVP1 overexpression in rice seedlings, phenotypes, overview
additional information
-
OVP1 overexpression in rice seedlings, phenotypes, overview
additional information
construction and analysis of the pGC1::IPP1 line, in which the soluble-type yeast PPase inorganic pyrophosphatase (IPP1) is specifically expressed in Arabidopsis thaliana guard cells in the H+-PPase loss-of-function mutant fugu5 background. pGC1::IPP1/fugu5-1 displays typical oblong cotyledons reminiscent of fugu5 mutants, but recombinant expression of IPP1 in the guard cells of the pGC1::IPP1/fugu5-1 lines does not affect the palisade cell phenotype. Effect of pGC1::IPP1 expression on palisade tissue development and hypocotyl elongation, overview
additional information
-
construction and analysis of the pGC1::IPP1 line, in which the soluble-type yeast PPase inorganic pyrophosphatase (IPP1) is specifically expressed in Arabidopsis thaliana guard cells in the H+-PPase loss-of-function mutant fugu5 background. pGC1::IPP1/fugu5-1 displays typical oblong cotyledons reminiscent of fugu5 mutants, but recombinant expression of IPP1 in the guard cells of the pGC1::IPP1/fugu5-1 lines does not affect the palisade cell phenotype. Effect of pGC1::IPP1 expression on palisade tissue development and hypocotyl elongation, overview
additional information
-
construction and analysis of the pGC1::IPP1 line, in which the soluble-type yeast PPase inorganic pyrophosphatase (IPP1) is specifically expressed in Arabidopsis thaliana guard cells in the H+-PPase loss-of-function mutant fugu5 background. pGC1::IPP1/fugu5-1 displays typical oblong cotyledons reminiscent of fugu5 mutants, but recombinant expression of IPP1 in the guard cells of the pGC1::IPP1/fugu5-1 lines does not affect the palisade cell phenotype. Effect of pGC1::IPP1 expression on palisade tissue development and hypocotyl elongation, overview
-
additional information
construction of several deletion and insertion mutants, overview, mutants with altered interdomain region display 2-265fold decreased catalytic efficiency, overview
additional information
-
construction of several deletion and insertion mutants, overview, mutants with altered interdomain region display 2-265fold decreased catalytic efficiency, overview
additional information
-
construction of several deletion and insertion mutants, overview, mutants with altered interdomain region display 2-265fold decreased catalytic efficiency, overview
-
additional information
knockdown of Tc-SPPase in the genome of Tribolium castaneum via pRNAi. Injection of Tc-sPPase dsRNA completely inhibits its expression when compared to the control, confirming that Tc-sPPase transcription is largely reduced
additional information
-
knockdown of Tc-SPPase in the genome of Tribolium castaneum via pRNAi. Injection of Tc-sPPase dsRNA completely inhibits its expression when compared to the control, confirming that Tc-sPPase transcription is largely reduced
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At1g73010, DNA and amino acid sequence determination and analysis, expression of His6-tagged enzyme in Escherichia coli strain Bl21 (DE3)
DNA and amino acid sequence determination and analysis, expression in Escherichia coli
DNA and amino acid sequence determination and analysis, expression in Escherichia coli strain BL21 pLysS(DE3)
DNA and amino acid sequence determination and analysis, genetic structure, functional expression of the His-tagged liver enzyme in Escherichia coli, transcription start site determination by primer extension analysis, protein-DNA interaction analysis of putative transcription factors and binding sites, overview
DQ978330
expressed as a chimaeric protein (fused with secreted invertase precursor SUC2) in Saccharomyces cerevisiae mutant strain YPC3
expressed in Escherichia coli
expressed in Escherichia coli BL21(DE3)
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21(DE3) cells as a fusion protein with a C-terminal polyhistidine tag
-
expressed in Escherichia coli BL21(DE3) cells as a His-tagged protein
-
expressed in Escherichia coli MV1184
expressed in Escherichia coli Rosetta 2 cells
expressed in Escherichia coli Rosetta(DE3)pLysS cells
-
expressed in Escherichia coli XL2
-
expressed in Escherichia LMG194 cells
expressed in Escherichia Rosetta(DE3)pLysS cells
expresses in Escherichia coli
-
expression in Escherichia coli
expression in Escherichia coli strain BL21
-
expression in Escherichia coli. Co-expression of tRNA-ARG, cognate for the rare codon AGA in Escherichia coli, improves yield
-
expression of GST-tagged enzyme in Escherichia coli strain BL21 (DE3)
expression of GST-tagged isozymes in Escherichia coli
expression of His-tagged enzyme
-
expression of His-tagged enzyme in Escherichia coli
expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
-
expression of mutant enzymes: P103A, P122A, S123A, H125A, S158A, R159A, G163A, H165A, P167A, and D169A in Escherichia coli. The expression level varies from 49 to 165% of that of the wild type enzyme
expression of the enzyme in Escherichia coli BL21(DE3)
-
expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
family I and family II isozymes, phylogenetic analysis, family II PPase is laterally transferred to the Vibrionales ancestor and partially degenerated due to functional redundancy, but nevertheless remains fixed as an adjunct to the family I enzyme, overexpression of PPase1 and PPase2 in Escherichia coli
-
gene AT727_13205, recombinant expression of wild-type and mutant enzymes in Escherichia coli strain BL21
gene Hp0620, structure-based phylogenetic tree of diphosphatases, expression of His-tagged enzyme in Escherichia coli strain B834(DE3) resulting in a selenomethionine-enzyme
-
gene ipp, sequence comparisons and phylogenetic analysis, recombinant expression of N-terminally His6-tagged enzyme in Haloferax volcanii strain H26-pJAM2920
gene IPP1, recombinant expression in Arabidopsis thaliana fugu5 mutant guard cells
gene OVP1, transformation into rice calli, driven by the maize ubiquitin promoter, with both GUS gene and hygromycin-resistance gene as selection markers by an Agrobacterium-mediated transformation approach
gene ppa, DNA and amino acid sequence determination and analysis, phylogenetic analysis, functional complmentation of a slow-growing Escherichia coli JP5 mutant strain containing a very low level of soluble inorganic pyrophosphatase activity
gene ppa, DNA and amino acid sequence determination and analysis, phylogenetic analysis, functional complmentation of a slow-growing Escherichia coli JP5 mutant strain containing a very low level of soluble inorganic pyrophosphatase activity, expression in Escherichia coli strain XL1-blue
gene ppa, DNA and amino acid sequence determination and analysis,phylogenetic analysis, functional complmentation of a slow-growing Escherichia coli JP5 mutant strain containing a very low level of soluble inorganic pyrophosphatase activity
gene ppa, expression in rosette source leaf cytosol of Arabidopsis thaliana
-
gene ppa, phylogenetic analysis, functional complmentation of a slow-growing Escherichia coli JP5 mutant strain containing a very low level of soluble inorganic pyrophosphatase activity
-
gene ppa, recombinant expression of the His-tagged enzyme in Escherichia coli strain Rosetta-Gami B (DE3)pLysS
gene ppa1, isozyme PPase 1, DNA and amino acid sequence determination and analysis, subcloning in Escherichia coli
gene PPA1, isozyme PPase1, DNA and amino acid sequence determination and anaylsis
gene ppa1, isozyme sPPase-I, DNA and amino acid sequence determination and analysis, phylogenetic analysis
gene PPA2, isozyme PPase2, DNA and amino acid sequence determination and anaylsis, localization on chromosome 4q25, expression of a GFP-atgged PPase2 fragment in HeLa cells
gene ppa2, isozyme sPPase-II, DNA and amino acid sequence determination and analysis, phylogenetic analysis
gene pyp-1, DNA and amino acid sequence determination and analysis, genomic organization, expression in transformed adult progeny worms using the promoterless GFP vector, pPD95.75 vector
gene TcasGA2_TC004566, real-time PCR expression analysis
gene ThPP1, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, recombinant expression in Oryza sativa subsp. japonica cv. Kitaake shoot and root using the transfection method via Agrobacterium tumefaciens strain GV3101, stable integration of the ThPP1 gene in the transgenic rice genome, construction of a ThPP1::16318hGFP protein expression vector and expression in in onion epidermal cells, quantitative RT-PCR expression analysis
gene VPP, DNA from leaves, DNA and amino acid sequence analysis and transcriptional profiling
gene vpp2, DNA from leaves, DNA and amino acid sequence analysis and transcriptional profiling
gene VVPP1, DNA from leaves, DNA and amino acid sequence analysis and transcriptional profiling
genes MdVHP1 and MdVHP2, phylogenetic analysis, overexpression of MdVHP1 in Solanum lycopersicum cv. Tianjinbaiguo and in Malus domesticus callus tissue, both using the Agrobacterium tumefaciens strain LBA4404 transfection method
heterologous expression in Saccharomyces cerevisiae
MdPPa is transiently expressed in Malus domestica cv. Ralls Janet pollen as GFP fusion protein driven by the tomato pollen-specific promoter Lat52, the MdPPa-GFP constructis transformed into pollen by particle bombardment. Recombinant transient expression of coding sequences (CDSs) of MdPPa and S1-, S2-, S3- and S9-RNase from pEZS-NL vector driven by CaMV 35S promoter in Zea mays protoplasts. Recombinant coexpression of MBP-tagged S1, S2, S3, S9-RNase and His6-tagged A14 in Escherichia coli
XM_008360526
overexpression of soluble wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
phylogenetic analysis, expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21 (DE3)
quantitative RT-PCR expression analysis, recombinant expression of His6-tagged enzyme in Escherichia coli strain BL21
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quantitative RT-PCR expression analysis, recombinant expression of MBP-His6-tagged wild-type and mutant enzymes in Escherichia coli strain BL21
quantitative tissue-specific expression analysis
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recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli
recombinant expression of N-terminally His10-tagged enzyme in Escherichia coli strain BL21(DE3)
subcloning in Escherichia coli strain XL1-blue, expression of wild-type and mutant enzymes in enzyme-deficient Saccharomyces cerevisiae strain BJ268
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expressed in Escherichia coli
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expressed in Escherichia coli
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expressed in Escherichia coli BL21(DE3) cells
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expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21(DE3) cells
expression in Escherichia coli
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expression in Escherichia coli
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expression in Escherichia coli
expression in Escherichia coli
expression in Escherichia coli
expression in Escherichia coli
expression in Escherichia coli
expression of His-tagged enzyme in Escherichia coli
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expression of His-tagged enzyme in Escherichia coli
recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli
recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli
recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli
recombinant expression of N-terminally His10-tagged enzyme in Escherichia coli strain BL21(DE3)
recombinant expression of N-terminally His10-tagged enzyme in Escherichia coli strain BL21(DE3)
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