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Literature summary 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

EC Number Activating Compound Comment Organism Structure
3.6.1.1 ATP CBS-PPases will consume diphosphate more efficiently at high ATP concentrations when biosynthetic reactions proceed faster and produce more diphosphate Clostridium perfringens
3.6.1.1 ATP CBS-PPases will consume diphosphate more efficiently at high ATP concentrations when biosynthetic reactions proceed faster and produce more diphosphate Desulfitobacterium hafniense
3.6.1.1 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
3.6.1.1 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
3.6.1.1 additional information ApnAs, the stress-associated alarmones containing 3-6 phosphate units, activate CBS-PPases several fold Clostridium perfringens
3.6.1.1 additional information ApnAs, the stress-associated alarmones containing 3-6 phosphate units, activate CBS-PPases several fold Desulfitobacterium hafniense

Crystallization (Commentary)

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

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.6.1.1 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
3.6.1.1 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
3.6.1.1 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
3.6.1.1 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
3.6.1.1 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
3.6.1.1 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
3.6.1.1 ADP
-
 Clostridium perfringens
3.6.1.1 ADP
-
 Desulfitobacterium hafniense
3.6.1.1 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
3.6.1.1 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
3.6.1.1 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
3.6.1.1 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
3.6.1.1 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
3.6.1.1 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]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.6.1.1 additional information
-
 additional information CBS-PPase activity shows positive cooperativity Clostridium perfringens
3.6.1.1 additional information
-
 additional information CBS-PPase activity shows positive cooperativity Desulfitobacterium hafniense

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.6.1.1 cytoplasm
-
 Desulfitobacterium hafniense 5737
-
3.6.1.1 soluble
-
 Streptococcus gordonii
-
-
3.6.1.1 soluble
-
 Bacillus subtilis
-
-
3.6.1.1 soluble
-
 Staphylococcus aureus
-
-
3.6.1.1 soluble
-
 Clostridium perfringens
-
-
3.6.1.1 soluble
-
 Desulfitobacterium hafniense
-
-
3.6.1.1 soluble
-
 Streptococcus agalactiae
-
-
3.6.1.1 soluble
-
 Papaver rhoeas
-
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.6.1.1 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
3.6.1.1 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
3.6.1.1 Co2+ required Streptococcus gordonii
3.6.1.1 Co2+ required Bacillus subtilis
3.6.1.1 Co2+ required Staphylococcus aureus
3.6.1.1 Co2+ required Streptococcus agalactiae
3.6.1.1 Co2+ required, cobalt-dependent enzyme Clostridium perfringens
3.6.1.1 Co2+ required, cobalt-dependent enzyme Desulfitobacterium hafniense
3.6.1.1 Mg2+ required Streptococcus gordonii
3.6.1.1 Mg2+ required Bacillus subtilis
3.6.1.1 Mg2+ required Staphylococcus aureus
3.6.1.1 Mg2+ required Clostridium perfringens
3.6.1.1 Mg2+ required Desulfitobacterium hafniense
3.6.1.1 Mg2+ required Streptococcus agalactiae
3.6.1.1 Mg2+ required Papaver rhoeas
3.6.1.1 Mn2+ required, a Mn2+-bound canonical Family II PPase Streptococcus gordonii
3.6.1.1 Mn2+ required, a Mn2+-bound canonical Family II PPase Bacillus subtilis
3.6.1.1 Mn2+ required, a Mn2+-bound canonical Family II PPase Staphylococcus aureus
3.6.1.1 Mn2+ required, a Mn2+-bound canonical Family II PPase Streptococcus agalactiae
3.6.1.1 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
3.6.1.1 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
3.6.1.1 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
3.6.1.1 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
3.6.1.1 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
3.6.1.1 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)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.6.1.1 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
3.6.1.1 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
3.6.1.1 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
3.6.1.1 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
3.6.1.1 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
3.6.1.1 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
3.6.1.1 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
3.6.1.1 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
3.6.1.1 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
3.6.1.1 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

EC Number Organism UniProt Comment Textmining
3.6.1.1 Bacillus subtilis P37487
-
-
3.6.1.1 Clostridium perfringens Q8XIQ9
-
-
3.6.1.1 Clostridium perfringens 13 Q8XIQ9
-
-
3.6.1.1 Clostridium perfringens type A Q8XIQ9
-
-
3.6.1.1 Desulfitobacterium hafniense A0A098B5G4
-
-
3.6.1.1 Papaver rhoeas Q2P9V0
-
-
3.6.1.1 Staphylococcus aureus W8TS62
-
-
3.6.1.1 Streptococcus agalactiae R4ZBK7
-
-
3.6.1.1 Streptococcus gordonii P95765
-
-
3.6.1.1 Streptococcus gordonii V288 P95765
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.6.1.1 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
3.6.1.1 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

EC Number Source Tissue Comment Organism Textmining
3.6.1.1 flower
-
 Papaver rhoeas
-
3.6.1.1 additional information inorganic pyrophosphatases (PPases) are present in all cell types Streptococcus gordonii
-
3.6.1.1 additional information inorganic pyrophosphatases (PPases) are present in all cell types Bacillus subtilis
-
3.6.1.1 additional information inorganic pyrophosphatases (PPases) are present in all cell types Staphylococcus aureus
-
3.6.1.1 additional information inorganic pyrophosphatases (PPases) are present in all cell types Clostridium perfringens
-
3.6.1.1 additional information inorganic pyrophosphatases (PPases) are present in all cell types Desulfitobacterium hafniense
-
3.6.1.1 additional information inorganic pyrophosphatases (PPases) are present in all cell types Streptococcus agalactiae
-
3.6.1.1 additional information inorganic pyrophosphatases (PPases) are present in all cell types Papaver rhoeas
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.6.1.1 diphosphate + H2O
-
 Streptococcus gordonii 2 phosphate
-
 r
3.6.1.1 diphosphate + H2O
-
 Bacillus subtilis 2 phosphate
-
 r
3.6.1.1 diphosphate + H2O
-
 Staphylococcus aureus 2 phosphate
-
 r
3.6.1.1 diphosphate + H2O
-
 Clostridium perfringens 2 phosphate
-
 r
3.6.1.1 diphosphate + H2O
-
 Desulfitobacterium hafniense 2 phosphate
-
 r
3.6.1.1 diphosphate + H2O
-
 Streptococcus agalactiae 2 phosphate
-
 r
3.6.1.1 diphosphate + H2O
-
 Papaver rhoeas 2 phosphate
-
 r
3.6.1.1 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
3.6.1.1 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
3.6.1.1 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
3.6.1.1 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
3.6.1.1 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
3.6.1.1 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
3.6.1.1 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
3.6.1.1 diphosphate + H2O
-
 Clostridium perfringens type A 2 phosphate
-
 r
3.6.1.1 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
3.6.1.1 diphosphate + H2O
-
 Streptococcus gordonii V288 2 phosphate
-
 r
3.6.1.1 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
3.6.1.1 diphosphate + H2O
-
 Clostridium perfringens 13 2 phosphate
-
 r
3.6.1.1 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

EC Number Subunits Comment Organism
3.6.1.1 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
3.6.1.1 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
3.6.1.1 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
3.6.1.1 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
3.6.1.1 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
3.6.1.1 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

EC Number Synonyms Comment Organism
3.6.1.1 AT727_13205
-
 Desulfitobacterium hafniense
3.6.1.1 CBS-PPase
-
 Clostridium perfringens
3.6.1.1 CBS-PPase
-
 Desulfitobacterium hafniense
3.6.1.1 cobalt-dependent inorganic pyrophosphatase UniProt Clostridium perfringens
3.6.1.1 CPE2055
-
 Clostridium perfringens
3.6.1.1 family I PPase
-
 Papaver rhoeas
3.6.1.1 family II PPase
-
 Streptococcus gordonii
3.6.1.1 family II PPase
-
 Bacillus subtilis
3.6.1.1 family II PPase
-
 Staphylococcus aureus
3.6.1.1 family II PPase
-
 Clostridium perfringens
3.6.1.1 family II PPase
-
 Desulfitobacterium hafniense
3.6.1.1 family II PPase
-
 Streptococcus agalactiae
3.6.1.1 inorganic pyrophosphatase
-
 Streptococcus gordonii
3.6.1.1 inorganic pyrophosphatase
-
 Bacillus subtilis
3.6.1.1 inorganic pyrophosphatase
-
 Staphylococcus aureus
3.6.1.1 inorganic pyrophosphatase
-
 Clostridium perfringens
3.6.1.1 inorganic pyrophosphatase
-
 Desulfitobacterium hafniense
3.6.1.1 inorganic pyrophosphatase
-
 Streptococcus agalactiae
3.6.1.1 inorganic pyrophosphatase
-
 Papaver rhoeas
3.6.1.1 manganese-dependent inorganic pyrophosphatase UniProt Streptococcus gordonii
3.6.1.1 manganese-dependent inorganic pyrophosphatase UniProt Bacillus subtilis
3.6.1.1 manganese-dependent inorganic pyrophosphatase UniProt Staphylococcus aureus
3.6.1.1 manganese-dependent inorganic pyrophosphatase UniProt Streptococcus agalactiae
3.6.1.1 Mn2+-bound canonical Family II PPase
-
 Streptococcus gordonii
3.6.1.1 Mn2+-bound canonical Family II PPase
-
 Bacillus subtilis
3.6.1.1 Mn2+-bound canonical Family II PPase
-
 Staphylococcus aureus
3.6.1.1 Mn2+-bound canonical Family II PPase
-
 Streptococcus agalactiae
3.6.1.1 PpaC
-
 Streptococcus gordonii
3.6.1.1 PpaC
-
 Bacillus subtilis
3.6.1.1 PpaC
-
 Staphylococcus aureus
3.6.1.1 PpaC
-
 Streptococcus agalactiae
3.6.1.1 PPase
-
 Streptococcus gordonii
3.6.1.1 PPase
-
 Bacillus subtilis
3.6.1.1 PPase
-
 Staphylococcus aureus
3.6.1.1 PPase
-
 Clostridium perfringens
3.6.1.1 PPase
-
 Desulfitobacterium hafniense
3.6.1.1 PPase
-
 Streptococcus agalactiae
3.6.1.1 PPase
-
 Papaver rhoeas

General Information

EC Number General Information Comment Organism
3.6.1.1 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
3.6.1.1 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
3.6.1.1 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
3.6.1.1 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
3.6.1.1 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
3.6.1.1 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
3.6.1.1 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
3.6.1.1 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
3.6.1.1 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
3.6.1.1 additional information metal-binding sites are found in the DHH domain, whereas the substrate recruits ligands from both domains Bacillus subtilis
3.6.1.1 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
3.6.1.1 additional information structure-function analysis of canonical Family II PPases, catalytic reaction mechanism, detailed, overview Clostridium perfringens
3.6.1.1 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
3.6.1.1 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
3.6.1.1 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
3.6.1.1 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
3.6.1.1 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
3.6.1.1 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
3.6.1.1 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
3.6.1.1 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
3.6.1.1 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
3.6.1.1 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