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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
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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
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family II soluble inorganic pyrophosphatase
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evolution
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the enzyme belongs to the CBS-PPases
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evolution
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enzyme BT2127 is a member of the haloalkanoate dehalogenase superfamily, HADSF
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evolution
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AtPPsPase1 belongs to the haloacid dehalogenase, HAD, superfamily
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evolution
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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
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evolution
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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
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evolution
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the enzyme belongs to the CBS-PPases
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evolution
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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
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evolution
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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
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evolution
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the enzyme belongs to the CBS-PPases
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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
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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
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malfunction
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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
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malfunction
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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
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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
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PPase is an essential constitutive enzyme for energy metabolism and clearance of excess diphosphate
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metabolism
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the soluble pyrophosphatasem RNA exists in great copy numbers in cells of Methanosaeta thermophila
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physiological function
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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
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enzyme-overexpressing parasites show a significant growth defect in fibroblasts, less responsiveness to hyperosmotic stress, and reduced persistence in tissues of mice
physiological function
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the enzyme can pump protons through membranes
physiological function
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the membrane-integral enzyme uses binding of diphosphate to drive pumping H+
physiological function
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the membrane-integral enzyme uses binding of diphosphate to drive pumping Na+
physiological function
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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
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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
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tight control of AtPPsPase1 gene expression underlines its important role in the phosphate starvation response, cleavage of diphosphate is an immediate metabolic adaptation reaction
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physiological function
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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
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physiological function
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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
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physiological function
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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
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physiological function
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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
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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
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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
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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
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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
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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
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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
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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
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active site structure analysis
additional information
active site structure analysis
additional information
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active site structure analysis
additional information
AtPPA1 three-dimensional structure analysis and modelling, overview
additional information
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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
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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
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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
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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
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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
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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
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structure-function analysis of canonical Family II PPases, catalytic reaction mechanism, detailed, overview
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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
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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
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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
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ThPP1 protein is a hydrolase with the sites of metal binding protein, but having a tight single domain without the transmembrane structure
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ThPP1 protein is a hydrolase with the sites of metal binding protein, but having a tight single domain without the transmembrane structure
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the hinge region plays an important role in opening and closing of the active site between the N- and C-terminal domains of PPase
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structure comparisons of CBS-PPases and molecular dynamic simulations, overview
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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
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modelling of the active site
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structure-function analysis of canonical Family II PPases, catalytic reaction mechanism, detailed, overview
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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
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structure comparisons of CBS-PPases and molecular dynamic simulations, overview
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additional information
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structure-function analysis of canonical Family II PPases, catalytic reaction mechanism, detailed, overview
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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
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comparison of the primary structure of ehPPase with those of five other CBS-PPases. Molecular dynamic simulations, overview
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