Activating Compound | Comment | Organism | Structure |
---|---|---|---|
ATP | CBS-PPases will consume diphosphate more efficiently at high ATP concentrations when biosynthetic reactions proceed faster and produce more diphosphate | Clostridium perfringens | |
ATP | CBS-PPases will consume diphosphate more efficiently at high ATP concentrations when biosynthetic reactions proceed faster and produce more diphosphate | Desulfitobacterium hafniense | |
Diadenosine tetraphosphate | 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 | Clostridium perfringens | |
Diadenosine tetraphosphate | 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 | Desulfitobacterium hafniense | |
additional information | ApnAs, the stress-associated alarmones containing 3-6 phosphate units, activate CBS-PPases several fold | Clostridium perfringens | |
additional information | ApnAs, the stress-associated alarmones containing 3-6 phosphate units, activate CBS-PPases several fold | Desulfitobacterium hafniense |
Crystallization (Comment) | Organism |
---|---|
regulatory part of Clostridium perfringens CBS-PPase complexed with AMP, PDB ID 3L31 | Clostridium perfringens |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
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) | Bacillus subtilis | |
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) | Clostridium perfringens | |
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) | Desulfitobacterium hafniense | |
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) | Staphylococcus aureus | |
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) | Streptococcus agalactiae | |
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) | Streptococcus gordonii | |
ADP | - |
Clostridium perfringens | |
ADP | - |
Desulfitobacterium hafniense | |
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 | Clostridium perfringens | |
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 | Desulfitobacterium hafniense | |
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 | Bacillus subtilis | |
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 | Streptococcus gordonii | |
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 | Bacillus subtilis | |
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 | Streptococcus gordonii |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | CBS-PPase activity shows positive cooperativity | Clostridium perfringens | |
additional information | - |
additional information | CBS-PPase activity shows positive cooperativity | Desulfitobacterium hafniense |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
cytoplasm | - |
Desulfitobacterium hafniense | 5737 | - |
soluble | - |
Streptococcus gordonii | - |
- |
soluble | - |
Bacillus subtilis | - |
- |
soluble | - |
Staphylococcus aureus | - |
- |
soluble | - |
Clostridium perfringens | - |
- |
soluble | - |
Desulfitobacterium hafniense | - |
- |
soluble | - |
Streptococcus agalactiae | - |
- |
soluble | - |
Papaver rhoeas | - |
- |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
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 | Streptococcus gordonii | |
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 | Bacillus subtilis | |
Co2+ | required | Streptococcus gordonii | |
Co2+ | required | Bacillus subtilis | |
Co2+ | required | Staphylococcus aureus | |
Co2+ | required | Streptococcus agalactiae | |
Co2+ | required, cobalt-dependent enzyme | Clostridium perfringens | |
Co2+ | required, cobalt-dependent enzyme | Desulfitobacterium hafniense | |
Mg2+ | required | Streptococcus gordonii | |
Mg2+ | required | Bacillus subtilis | |
Mg2+ | required | Staphylococcus aureus | |
Mg2+ | required | Clostridium perfringens | |
Mg2+ | required | Desulfitobacterium hafniense | |
Mg2+ | required | Streptococcus agalactiae | |
Mg2+ | required | Papaver rhoeas | |
Mn2+ | required, a Mn2+-bound canonical Family II PPase | Streptococcus gordonii | |
Mn2+ | required, a Mn2+-bound canonical Family II PPase | Bacillus subtilis | |
Mn2+ | required, a Mn2+-bound canonical Family II PPase | Staphylococcus aureus | |
Mn2+ | required, a Mn2+-bound canonical Family II PPase | Streptococcus agalactiae | |
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 | Streptococcus gordonii | |
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 | Staphylococcus aureus | |
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 | Clostridium perfringens | |
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 | Desulfitobacterium hafniense | |
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 | Streptococcus agalactiae | |
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 | Bacillus subtilis |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
diphosphate + H2O | Streptococcus gordonii | the enzyme can also catalyze the reverse reaction of diphosphate synthesis from phosphate, but this activity does not seem physiologically important | 2 phosphate | - |
r | |
diphosphate + H2O | Bacillus subtilis | the enzyme can also catalyze the reverse reaction of diphosphate synthesis from phosphate, but this activity does not seem physiologically important | 2 phosphate | - |
r | |
diphosphate + H2O | Staphylococcus aureus | the enzyme can also catalyze the reverse reaction of diphosphate synthesis from phosphate, but this activity does not seem physiologically important | 2 phosphate | - |
r | |
diphosphate + H2O | Clostridium perfringens | the enzyme can also catalyze the reverse reaction of diphosphate synthesis from phosphate, but this activity does not seem physiologically important | 2 phosphate | - |
r | |
diphosphate + H2O | Desulfitobacterium hafniense | the enzyme can also catalyze the reverse reaction of diphosphate synthesis from phosphate, but this activity does not seem physiologically important | 2 phosphate | - |
r | |
diphosphate + H2O | Streptococcus agalactiae | the enzyme can also catalyze the reverse reaction of diphosphate synthesis from phosphate, but this activity does not seem physiologically important | 2 phosphate | - |
r | |
diphosphate + H2O | Papaver rhoeas | the enzyme can also catalyze the reverse reaction of diphosphate synthesis from phosphate, but this activity does not seem physiologically important | 2 phosphate | - |
r | |
diphosphate + H2O | Clostridium perfringens type A | the enzyme can also catalyze the reverse reaction of diphosphate synthesis from phosphate, but this activity does not seem physiologically important | 2 phosphate | - |
r | |
diphosphate + H2O | Streptococcus gordonii V288 | the enzyme can also catalyze the reverse reaction of diphosphate synthesis from phosphate, but this activity does not seem physiologically important | 2 phosphate | - |
r | |
diphosphate + H2O | Clostridium perfringens 13 | the enzyme can also catalyze the reverse reaction of diphosphate synthesis from phosphate, but this activity does not seem physiologically important | 2 phosphate | - |
r |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Bacillus subtilis | P37487 | - |
- |
Clostridium perfringens | Q8XIQ9 | - |
- |
Clostridium perfringens 13 | Q8XIQ9 | - |
- |
Clostridium perfringens type A | Q8XIQ9 | - |
- |
Desulfitobacterium hafniense | A0A098B5G4 | - |
- |
Papaver rhoeas | Q2P9V0 | - |
- |
Staphylococcus aureus | W8TS62 | - |
- |
Streptococcus agalactiae | R4ZBK7 | - |
- |
Streptococcus gordonii | P95765 | - |
- |
Streptococcus gordonii V288 | P95765 | - |
- |
Posttranslational Modification | Comment | Organism |
---|---|---|
phosphoprotein | phosphorylation of the Family I PPase from the flowering plant, Papaver rhoeas, suppresses PPase activity and is a key event in preventing self-fertilization | Papaver rhoeas |
phosphoprotein | the canonical Family II PPase of Streptococcus agalactiae is reversibly phosphorylated by endogenous Stk1/Stp1 protein kinase/phosphatase producing effects on cell behavior | Streptococcus agalactiae |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
flower | - |
Papaver rhoeas | - |
additional information | inorganic pyrophosphatases (PPases) are present in all cell types | Streptococcus gordonii | - |
additional information | inorganic pyrophosphatases (PPases) are present in all cell types | Bacillus subtilis | - |
additional information | inorganic pyrophosphatases (PPases) are present in all cell types | Staphylococcus aureus | - |
additional information | inorganic pyrophosphatases (PPases) are present in all cell types | Clostridium perfringens | - |
additional information | inorganic pyrophosphatases (PPases) are present in all cell types | Desulfitobacterium hafniense | - |
additional information | inorganic pyrophosphatases (PPases) are present in all cell types | Streptococcus agalactiae | - |
additional information | inorganic pyrophosphatases (PPases) are present in all cell types | Papaver rhoeas | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
diphosphate + H2O | - |
Streptococcus gordonii | 2 phosphate | - |
r | |
diphosphate + H2O | - |
Bacillus subtilis | 2 phosphate | - |
r | |
diphosphate + H2O | - |
Staphylococcus aureus | 2 phosphate | - |
r | |
diphosphate + H2O | - |
Clostridium perfringens | 2 phosphate | - |
r | |
diphosphate + H2O | - |
Desulfitobacterium hafniense | 2 phosphate | - |
r | |
diphosphate + H2O | - |
Streptococcus agalactiae | 2 phosphate | - |
r | |
diphosphate + H2O | - |
Papaver rhoeas | 2 phosphate | - |
r | |
diphosphate + H2O | the enzyme can also catalyze the reverse reaction of diphosphate synthesis from phosphate, but this activity does not seem physiologically important | Streptococcus gordonii | 2 phosphate | - |
r | |
diphosphate + H2O | the enzyme can also catalyze the reverse reaction of diphosphate synthesis from phosphate, but this activity does not seem physiologically important | Bacillus subtilis | 2 phosphate | - |
r | |
diphosphate + H2O | the enzyme can also catalyze the reverse reaction of diphosphate synthesis from phosphate, but this activity does not seem physiologically important | Staphylococcus aureus | 2 phosphate | - |
r | |
diphosphate + H2O | the enzyme can also catalyze the reverse reaction of diphosphate synthesis from phosphate, but this activity does not seem physiologically important | Clostridium perfringens | 2 phosphate | - |
r | |
diphosphate + H2O | the enzyme can also catalyze the reverse reaction of diphosphate synthesis from phosphate, but this activity does not seem physiologically important | Desulfitobacterium hafniense | 2 phosphate | - |
r | |
diphosphate + H2O | the enzyme can also catalyze the reverse reaction of diphosphate synthesis from phosphate, but this activity does not seem physiologically important | Streptococcus agalactiae | 2 phosphate | - |
r | |
diphosphate + H2O | the enzyme can also catalyze the reverse reaction of diphosphate synthesis from phosphate, but this activity does not seem physiologically important | Papaver rhoeas | 2 phosphate | - |
r | |
diphosphate + H2O | - |
Clostridium perfringens type A | 2 phosphate | - |
r | |
diphosphate + H2O | the enzyme can also catalyze the reverse reaction of diphosphate synthesis from phosphate, but this activity does not seem physiologically important | Clostridium perfringens type A | 2 phosphate | - |
r | |
diphosphate + H2O | - |
Streptococcus gordonii V288 | 2 phosphate | - |
r | |
diphosphate + H2O | the enzyme can also catalyze the reverse reaction of diphosphate synthesis from phosphate, but this activity does not seem physiologically important | Streptococcus gordonii V288 | 2 phosphate | - |
r | |
diphosphate + H2O | - |
Clostridium perfringens 13 | 2 phosphate | - |
r | |
diphosphate + H2O | the enzyme can also catalyze the reverse reaction of diphosphate synthesis from phosphate, but this activity does not seem physiologically important | Clostridium perfringens 13 | 2 phosphate | - |
r |
Subunits | Comment | Organism |
---|---|---|
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 | Streptococcus gordonii |
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 | Bacillus subtilis |
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 | Staphylococcus aureus |
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 | Desulfitobacterium hafniense |
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 | Streptococcus agalactiae |
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 | Clostridium perfringens |
Synonyms | Comment | Organism |
---|---|---|
AT727_13205 | - |
Desulfitobacterium hafniense |
CBS-PPase | - |
Clostridium perfringens |
CBS-PPase | - |
Desulfitobacterium hafniense |
cobalt-dependent inorganic pyrophosphatase | UniProt | Clostridium perfringens |
CPE2055 | - |
Clostridium perfringens |
family I PPase | - |
Papaver rhoeas |
family II PPase | - |
Streptococcus gordonii |
family II PPase | - |
Bacillus subtilis |
family II PPase | - |
Staphylococcus aureus |
family II PPase | - |
Clostridium perfringens |
family II PPase | - |
Desulfitobacterium hafniense |
family II PPase | - |
Streptococcus agalactiae |
inorganic pyrophosphatase | - |
Streptococcus gordonii |
inorganic pyrophosphatase | - |
Bacillus subtilis |
inorganic pyrophosphatase | - |
Staphylococcus aureus |
inorganic pyrophosphatase | - |
Clostridium perfringens |
inorganic pyrophosphatase | - |
Desulfitobacterium hafniense |
inorganic pyrophosphatase | - |
Streptococcus agalactiae |
inorganic pyrophosphatase | - |
Papaver rhoeas |
manganese-dependent inorganic pyrophosphatase | UniProt | Streptococcus gordonii |
manganese-dependent inorganic pyrophosphatase | UniProt | Bacillus subtilis |
manganese-dependent inorganic pyrophosphatase | UniProt | Staphylococcus aureus |
manganese-dependent inorganic pyrophosphatase | UniProt | Streptococcus agalactiae |
Mn2+-bound canonical Family II PPase | - |
Streptococcus gordonii |
Mn2+-bound canonical Family II PPase | - |
Bacillus subtilis |
Mn2+-bound canonical Family II PPase | - |
Staphylococcus aureus |
Mn2+-bound canonical Family II PPase | - |
Streptococcus agalactiae |
PpaC | - |
Streptococcus gordonii |
PpaC | - |
Bacillus subtilis |
PpaC | - |
Staphylococcus aureus |
PpaC | - |
Streptococcus agalactiae |
PPase | - |
Streptococcus gordonii |
PPase | - |
Bacillus subtilis |
PPase | - |
Staphylococcus aureus |
PPase | - |
Clostridium perfringens |
PPase | - |
Desulfitobacterium hafniense |
PPase | - |
Streptococcus agalactiae |
PPase | - |
Papaver rhoeas |
General Information | Comment | Organism |
---|---|---|
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 | Streptococcus gordonii |
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 | Bacillus subtilis |
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 | Staphylococcus aureus |
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 | Clostridium perfringens |
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 | Desulfitobacterium hafniense |
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 | Streptococcus agalactiae |
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 | Papaver rhoeas |
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 | Desulfitobacterium hafniense |
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 | Streptococcus agalactiae |
additional information | metal-binding sites are found in the DHH domain, whereas the substrate recruits ligands from both domains | Bacillus subtilis |
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 | Streptococcus gordonii |
additional information | structure-function analysis of canonical Family II PPases, catalytic reaction mechanism, detailed, overview | Clostridium perfringens |
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 | Desulfitobacterium hafniense |
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 | Streptococcus agalactiae |
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 | Staphylococcus aureus |
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 | Streptococcus gordonii |
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 | Bacillus subtilis |
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 | Staphylococcus aureus |
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 | Streptococcus agalactiae |
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 | Clostridium perfringens |
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 | Desulfitobacterium hafniense |
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 | Papaver rhoeas |