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Literature summary for 3.6.1.1 extracted from

  • Baykov, A.A.; Anashkin, V.A.; Salminen, A.; Lahti, R.
    Inorganic pyrophosphatases of family II - two decades after their discovery (2017), FEBS Lett., 591, 3225-3234 .
    View publication on PubMed

Activating Compound

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 (Commentary)

Crystallization (Comment) Organism
regulatory part of Clostridium perfringens CBS-PPase complexed with AMP, PDB ID 3L31 Clostridium perfringens

Inhibitors

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 [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

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

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/ Products (Substrates)

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

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

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

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 and Products (Substrate)

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

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

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

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