Information on EC 3.6.1.1 - inorganic diphosphatase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea

EC NUMBER
COMMENTARY
3.6.1.1
-
RECOMMENDED NAME
GeneOntology No.
inorganic diphosphatase
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
diphosphate + H2O = 2 phosphate
show the reaction diagram
-
-
-
-
diphosphate + H2O = 2 phosphate
show the reaction diagram
catalytic mechanism involving residues Lys28, Tyr140, Glu20, Asp64, Asp69, Asp96, and Asp101, active site structure
-
diphosphate + H2O = 2 phosphate
show the reaction diagram
active site structure
-
diphosphate + H2O = 2 phosphate
show the reaction diagram
substrate binding structure and catalytic mechanism
diphosphate + H2O = 2 phosphate
show the reaction diagram
the catalytic mechanism of the HAD superfamily including a phosphorylated enzyme intermediate, overview
diphosphate + H2O = 2 phosphate
show the reaction diagram
the catalytic mechanism of the HAD superfamily including a phosphorylated enzyme intermediate, overview
Arabidopsis thaliana Col-0
-
-
diphosphate + H2O = 2 phosphate
show the reaction diagram
catalytic mechanism involving residues Lys28, Tyr140, Glu20, Asp64, Asp69, Asp96, and Asp101, active site structure
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphorous acid anhydride hydrolysis
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
non-pathway related
-
-
Oxidative phosphorylation
-
-
SYSTEMATIC NAME
IUBMB Comments
diphosphate phosphohydrolase
Specificity varies with the source and with the activating metal ion. The enzyme from some sources may be identical with EC 3.1.3.1 (alkaline phosphatase) or EC 3.1.3.9 (glucose-6-phosphatase). A form of this enzyme with a molecular mass of about 90 kDa is found in tonoplasts of plants and fungi, where it imports protons from the cytosol into the vacuolar lumen.
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
acid PPase
Sulfolobus acidocaldarius 7
-
-
acidocalcisomal pyrophosphatase
-
acidocalcisomal pyrophosphatase
Leishmania amazonensis MHOM/BR/1987/BA125
-
-
acidocalcisomal pyrophosphatase
-
alkaline PPase
-
-
AtPPsPase1
Arabidopsis thaliana Col-0
-
-
BT2127
Bacteroides thetaiotaomicron ATCC 29148D
-
-
chloroplast inorganic pyrophosphatase 1
-
cytosolic PPase
-
D1C enzyme
Sulfolobus acidocaldarius 7
-
-
ER H+-pyrophosphatase
-
-
family I inorganic pyrophosphatase
-
family I inorganic pyrophosphatase
-
-
family I inorganic pyrophosphatase
-
family I inorganic pyrophosphatase
-
family I inorganic pyrophosphatase
Pyrococcus horikoshii OT-3
-
-
family I inorganic pyrophosphatase
-
family I PPase
Pyrococcus horikoshii OT-3
-
-
family I PPase
-
-
family II inorganic pyrophosphatase
-
-
family II inorganic pyrophosphatase
-
family II inorganic pyrophosphatase
-
family II inorganic pyrophosphatase
-
-
family II PPase
-
-
family II PPase
-
-
family II PPase
Streptococcus gordonii DL1
-
-
family II PPase
-
-
H(+)-pyrophosphatase
-
-
H(+)-pyrophosphatase
Rhodospirillum rubrum Esmarch
-
-
-
H+ -translocating PPase
-
H+-inorganic pyrophosphatase
-
-
H+-PPase
-
-
-
-
H+-PPase
Rhodospirillum rubrum Esmarch
-
-
-
H+-PPase
-
-
H+-PPase
Trypanosoma cruzi Y
-
-
H+-pyrophosphatase
-
H+-translocating inorganic pyrophosphatase
-
-
H+-translocating/vacuolar inorganic pyrophosphatase
-
hyperthermophilic inorganic pyrophosphatase
-
-
inorganic diphosphatase
-
-
-
-
inorganic pyrophosphatase
-
-
-
-
inorganic pyrophosphatase
-
-
inorganic pyrophosphatase
-
inorganic pyrophosphatase
-
inorganic pyrophosphatase
Arabidopsis thaliana Col-0
-
-
inorganic pyrophosphatase
-
inorganic pyrophosphatase
Bacteroides thetaiotaomicron ATCC 29148D
-
-
inorganic pyrophosphatase
-
inorganic pyrophosphatase
-
-
inorganic pyrophosphatase
-
-
inorganic pyrophosphatase
-
-
inorganic pyrophosphatase
-
inorganic pyrophosphatase
-
-
-
inorganic pyrophosphatase
;
-
inorganic pyrophosphatase
-
-
inorganic pyrophosphatase
-
-
inorganic pyrophosphatase
-
inorganic pyrophosphatase
-
-
inorganic pyrophosphatase
-
inorganic pyrophosphatase
-
-
inorganic pyrophosphatase
-
-
inorganic pyrophosphatase
-
-
inorganic pyrophosphatase
-
inorganic pyrophosphatase
Pyrococcus horikoshii ATCC 700860D-5
-
-
inorganic pyrophosphatase
Pyrococcus horikoshii OT-3
-
-
-
inorganic pyrophosphatase
-
-
inorganic pyrophosphatase
DQ978330
-
inorganic pyrophosphatase
-
-
inorganic pyrophosphatase
-
inorganic pyrophosphatase
Streptococcus gordonii DL1
-
-
inorganic pyrophosphatase
-
inorganic pyrophosphatase
Sulfolobus acidocaldarius 7, Sulfolobus acidocaldarius DSM 639
-
-
inorganic pyrophosphatase
-
-
inorganic pyrophosphatase
-
inorganic pyrophosphatase
-
-
inorganic pyrophosphatase
-
inorganic pyrophosphatase
Trypanosoma cruzi Y
-
-
inorganic pyrophosphatase
-
-
inorganic pyrophosphatase
-
-
Inorganic pyrophosphatases
-
IPPase
DQ978330
-
LHPPase
-
-
manganese-dependent inorganic pyrophosphatase
-
manganese-dependent inorganic pyrophosphatase
-
-
membrane-bound proton-translocating pyrophosphatase
-
membrane-bound proton-translocating pyrophosphatase
-
Mthe_0236
locus name
Mthe_0236
Methanosaeta thermophila DSM 6194
locus name
-
OVP1
gene name
p26.1a
-
-
p26.1b
-
-
PH1907
Pyrococcus horikoshii DSM 12428
gene name
-
phospholysine phosphohistidine inorganic pyrophosphate phosphatase
-
-
phosphoprotein p26.1
-
-
PPase
-
-
-
-
PPase
-
-
PPase
-
-
PPase
Pyrococcus horikoshii ATCC 700860D-5
-
-
PPase
Pyrococcus horikoshii OT-3
-
-
PPase
Streptococcus gordonii DL1
;
-
PPase1
-
-
PPase2
-
-
PPIase
Pyrococcus horikoshii DSM 12428
-
-
proton pumping pyrophosphatase
Herpetomonas sp.
-
-
proton-pumping inorganic pyrophosphatase
-
proton-pumping inorganic pyrophosphatase
-
proton-pumping inorganic pyrophosphatase
-
proton-pumping inorganic pyrophosphatase
-
proton-pumping inorganic pyrophosphatase
-
-
proton-pumping inorganic pyrophosphatase
-
proton-pumping inorganic pyrophosphatase
-
proton-pyrophosphatase
-
electrogenic proton-pump that couples diphosphate hydrolysis to the active transport of protons across membranes
proton-translocating inorganic pyrophosphatase
-
proton-translocating inorganic pyrophosphatase
Trypanosoma cruzi Y
-
-
proton-translocating vacuolar PPase
-
-
pyrophosphatase
-
-
pyrophosphatase
-
-
pyrophosphatase
-
-
pyrophosphatase, inorganic
-
-
-
-
Pyrophosphate phospho-hydrolase
-
-
-
-
pyrophosphate phospho-hydrolase 1
-
Pyrophosphate phosphohydrolase
-
-
-
-
Pyrophosphate-energized inorganic pyrophosphatase
-
-
-
-
Pyrophosphate-energized inorganic pyrophosphatase
-
Pyrophosphate-energized inorganic pyrophosphatase
-
pyrophosphate-energized proton pump
-
pyrophosphate-energized proton pump
-
single-subunit H+ -PPase
-
soluble inorganic pyrophosphatase
-
soluble inorganic pyrophosphatase
-
-
soluble inorganic pyrophosphatase
-
soluble inorganic pyrophosphatase
-
-
soluble inorganic pyrophosphatase
-
soluble inorganic pyrophosphatase
-
soluble inorganic pyrophosphatase
Streptococcus gordonii DL1
-
-
soluble inorganic pyrophosphatase
-
soluble inorganic pyrophosphatase 2
-
soluble pyrophosphatase
-
soluble pyrophosphatase
Leishmania amazonensis MHOM/BR/1987/BA125
-
-
soluble pyrophosphatase
-
-
sPPAse
-
-
ST2226
locus name
ST2226
Sulfolobus tokodaii 7
locus name
-
V-H+-PPase
Herpetomonas sp.
-
-
V-PPase
-
-
V-PPase
-
-
V-PPase
-
vacuolar H(+)-PPase
-
vacuolar H(+)-PPase
Malus domestica Fuji
-
-
vacuolar H(+)-pyrophosphatase
-
vacuolar H+ -ATPase
-
vacuolar H+-PPase
-
-
vacuolar H+-pyrophosphatase
-
vacuolar H+-pyrophosphatase
-
-
vacuolar H+-pyrophosphatase
-
-
vacuolar H+-translocating inorganic pyrophosphatase
-
vacuolar H+-translocating inorganic pyrophosphatase
Malus domestica Fuji
-
-
vacuolar H+-translocating inorganic pyrophosphatase
-
vacuolar H+-translocating inorganic pyrophosphatase
-
-
vacuolar H+-translocating inorganic pyrophosphatase
-
vacuolar proton pyrophosphatase 1
-
vacuolar proton pyrophosphatase 2
-
vacuolar pyrophosphatase
-
vacuolar-type proton translocating pyrophosphatase 1
-
VHP
Malus domestica Fuji
-
-
VP1
Trypanosoma cruzi Y
-
-
VSP1
Leishmania amazonensis MHOM/BR/1987/BA125
-
-
mitochondrial pyrophosphatase
-
additional information
the enzyme is a member of the sPPase family I
additional information
Helicobacter pylori is a family I PPase
additional information
Helicobacter pylori is a family I PPase
-
CAS REGISTRY NUMBER
COMMENTARY
9024-82-2
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain PCC 7120, gene ppa
SwissProt
Manually annotated by BRENDA team
hyperthermophilic bacterium
SwissProt
Manually annotated by BRENDA team
isozyme AVP1; isozyme AVP1, gene AVP1
SwissProt
Manually annotated by BRENDA team
isozyme AVP2, gene AVPL1
SwissProt
Manually annotated by BRENDA team
isozyme PPA1, chloroplast precursor; isozyme PPA1
SwissProt
Manually annotated by BRENDA team
PPase1; two isozymes PPase1 and PPase4
SwissProt
Manually annotated by BRENDA team
Arabidopsis thaliana Col-0
-
UniProt
Manually annotated by BRENDA team
Aranda Christine
orchid
-
-
Manually annotated by BRENDA team
soluble enzyme
SwissProt
Manually annotated by BRENDA team
Bacteroides thetaiotaomicron ATCC 29148D
-
UniProt
Manually annotated by BRENDA team
Bristol strain N2, gene C47E12.4 or pyp-1
SwissProt
Manually annotated by BRENDA team
obligately anaerobic firmicute
-
-
Manually annotated by BRENDA team
ppa1, chloroplast precursor; soluble inorganic pyrophosphatase isozyme I, plastidial isozyme sPPase-I, gene ppa1, is the major isozyme
SwissProt
Manually annotated by BRENDA team
ppa2; soluble inorganic pyrophosphatase isozyme II, minor isozyme
SwissProt
Manually annotated by BRENDA team
moderate thermophile green sulfur photosynthetic bacterium
-
-
Manually annotated by BRENDA team
a green non-sulfur photosynthetic bacterium
-
-
Manually annotated by BRENDA team
strain ATCC 8043
-
-
Manually annotated by BRENDA team
strain F24
-
-
Manually annotated by BRENDA team
Enterococcus faecium F24
strain F24
-
-
Manually annotated by BRENDA team
gene ppa
-
-
Manually annotated by BRENDA team
strain MRE-600
-
-
Manually annotated by BRENDA team
Escherichia coli MRE-600
strain MRE-600
-
-
Manually annotated by BRENDA team
cv. 108-F
-
-
Manually annotated by BRENDA team
var. 108-F
-
-
Manually annotated by BRENDA team
strain 26695
-
-
Manually annotated by BRENDA team
strain 26695
SwissProt
Manually annotated by BRENDA team
strain 26695, ATCC 700392D
SwissProt
Manually annotated by BRENDA team
strain 8823
-
-
Manually annotated by BRENDA team
strain 26695
SwissProt
Manually annotated by BRENDA team
strain 26695, ATCC 700392D
SwissProt
Manually annotated by BRENDA team
Helicobacter pylori 8823
strain 8823
-
-
Manually annotated by BRENDA team
Herpetomonas sp.
plant parasite
-
-
Manually annotated by BRENDA team
gene PPA1, isozyme PPase1; gene PPA1, isozyme PPase1
SwissProt
Manually annotated by BRENDA team
gene PPA2, isozyme PPase2, mitochondrial precursor; gene PPA2, isozyme PPase2
SwissProt
Manually annotated by BRENDA team
two genes HVP1 and HVP10 encoding the V-PPase
-
-
Manually annotated by BRENDA team
MHOM/BR/1987/BA125
SwissProt
Manually annotated by BRENDA team
Leishmania amazonensis MHOM/BR/1987/BA125
MHOM/BR/1987/BA125
SwissProt
Manually annotated by BRENDA team
strain 252
Uniprot
Manually annotated by BRENDA team
Leishmania major 252
strain 252
Uniprot
Manually annotated by BRENDA team
MdVHP1; genes MdVHP1 and MdVHP2
UniProt
Manually annotated by BRENDA team
Malus domestica Fuji
MdVHP1; genes MdVHP1 and MdVHP2
UniProt
Manually annotated by BRENDA team
Methanosaeta thermophila DSM 6194
-
SwissProt
Manually annotated by BRENDA team
Methanothermobacter thermautotrophicum
strain H
-
-
Manually annotated by BRENDA team
Methanothermobacter thermautotrophicum H
strain H
-
-
Manually annotated by BRENDA team
strain ATCC 35608
-
-
Manually annotated by BRENDA team
mouse
-
-
Manually annotated by BRENDA team
a deep-subsurface alpha-proteobacterium isolated from North Atlantic coastal sediments
-
-
Manually annotated by BRENDA team
gene OVP1
UniProt
Manually annotated by BRENDA team
hyperthermophilic bacterium
-
-
Manually annotated by BRENDA team
strain PCC 6903, gene ppa
SwissProt
Manually annotated by BRENDA team
a thermoproteal euryarchaeon
SwissProt
Manually annotated by BRENDA team
hyperthermophilic bacterium
-
-
Manually annotated by BRENDA team
strain OT3
-
-
Manually annotated by BRENDA team
strain OT3
SwissProt
Manually annotated by BRENDA team
Pyrococcus horikoshii ATCC 700860D-5
-
SwissProt
Manually annotated by BRENDA team
Pyrococcus horikoshii DSM 12428
-
SwissProt
Manually annotated by BRENDA team
Pyrococcus horikoshii OT-3
strain OT3
-
-
Manually annotated by BRENDA team
Pyrococcus horikoshii OT-3
strain OT3
SwissProt
Manually annotated by BRENDA team
var. sativa
-
-
Manually annotated by BRENDA team
-
DQ978330
GenBank
Manually annotated by BRENDA team
male Fisher 344 rats
-
-
Manually annotated by BRENDA team
Rhodopseudomonas palustris Dr2
strain Dr2
-
-
Manually annotated by BRENDA team
strain ATCC 11170, gene hppA
SwissProt
Manually annotated by BRENDA team
strain Esmarch, Molisch ATCC 17031
-
-
Manually annotated by BRENDA team
strain G-9
-
-
Manually annotated by BRENDA team
strain S1, soluble and membrane bound form present in anaerobic phototrophic batch cultures, only soluble and no membrane bound form present in aerobic, dark grown cultures, highest level of membrane bound form in aerobic cultures grown under acute salt stress (1 M NaCl)
SwissProt
Manually annotated by BRENDA team
Rhodospirillum rubrum Esmarch
strain Esmarch, Molisch ATCC 17031
-
-
Manually annotated by BRENDA team
Rhodospirillum rubrum G-9
strain G-9
-
-
Manually annotated by BRENDA team
Rhodospirillum rubrum S1
strain S1, soluble and membrane bound form present in anaerobic phototrophic batch cultures, only soluble and no membrane bound form present in aerobic, dark grown cultures, highest level of membrane bound form in aerobic cultures grown under acute salt stress (1 M NaCl)
SwissProt
Manually annotated by BRENDA team
Rubrivivax gelatinosus Dr2
strain Dr2
-
-
Manually annotated by BRENDA team
variety Desiree
-
-
Manually annotated by BRENDA team
strain A909
UniProt
Manually annotated by BRENDA team
strain DL1
SwissProt
Manually annotated by BRENDA team
Streptococcus gordonii DL1
-
SwissProt
Manually annotated by BRENDA team
Streptococcus gordonii DL1
strain DL1
SwissProt
Manually annotated by BRENDA team
Streptomyces aureofaciens RIA57
strain RIA57
-
-
Manually annotated by BRENDA team
gene hppA
SwissProt
Manually annotated by BRENDA team
Sulfolobus acidocaldarius 7
-
Uniprot
Manually annotated by BRENDA team
Sulfolobus acidocaldarius 7
strain 7
-
-
Manually annotated by BRENDA team
strain 7
-
-
Manually annotated by BRENDA team
Sulfolobus sp. 7
strain 7
-
-
Manually annotated by BRENDA team
Sulfolobus tokodaii 7
-
UniProt
Manually annotated by BRENDA team
strain PCC 6803, gene ppa
SwissProt
Manually annotated by BRENDA team
hyperthermophilic bacterium
-
-
Manually annotated by BRENDA team
cDNA; strain RH
SwissProt
Manually annotated by BRENDA team
cDNA; strain RH
SwissProt
Manually annotated by BRENDA team
hyperthermophilic bacterium
-
-
Manually annotated by BRENDA team
vacuolar-type proton translocating pyrophosphatase 1 precursor
SwissProt
Manually annotated by BRENDA team
Trypanosoma cruzi Y
-
SwissProt
Manually annotated by BRENDA team
human pathogen, attenuated strain O1, family I and family II isozymes
-
-
Manually annotated by BRENDA team
mung bean
-
-
Manually annotated by BRENDA team
VPP fragment; gene VPP, two vacuolar H(+)-pyrophosphatase isozymes
SwissProt
Manually annotated by BRENDA team
vpp2; gene vpp2, two vacuolar H(+)-pyrophosphatase isozymes
SwissProt
Manually annotated by BRENDA team
VVPP1; gene VVPP1
SwissProt
Manually annotated by BRENDA team
fragment; wild-type A188 and several mutants, overview
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
Mycobacterium tuberculosis and Mycobacterium leprae genomes include genes for the only two family I inorganic pyrophosphatases known to contain two histidines in the active site, structure comparison of family I enzymes, overview
evolution
enzyme BT2127 is a member of the haloalkanoate dehalogenase superfamily, HADSF
evolution
AtPPsPase1 belongs to the haloacid dehalogenase, HAD, superfamily
evolution
family II soluble inorganic pyrophosphatase
evolution
Arabidopsis thaliana Col-0
-
AtPPsPase1 belongs to the haloacid dehalogenase, HAD, superfamily
-
evolution
Bacteroides thetaiotaomicron ATCC 29148D
-
enzyme BT2127 is a member of the haloalkanoate dehalogenase superfamily, HADSF
-
evolution
-
Mycobacterium tuberculosis and Mycobacterium leprae genomes include genes for the only two family I inorganic pyrophosphatases known to contain two histidines in the active site, structure comparison of family I enzymes, overview
-
evolution
Streptococcus gordonii DL1
-
family II soluble inorganic pyrophosphatase
-
malfunction
the fugu5 mutant is defective in AVP1, i.e. vacuolar H+-pyrophosphatase, due to point mutations A709T, A553T, or E272K, and fails to support heterotrophic growth after germination. Exogenous supplementation of succinate or the specific removal of the cytosolic diphosphate by the heterologous expression of the cytosolic inorganic diphosphatase1, IPP1, gene from Saccharomyces cerevisiae rescues fugu5 phenotypes. Compared with the wild-type and AVP1Pro:IPP1 transgenic lines, hypocotyl elongation in the fugu5 mutant is severely compromised in the dark but recovers upon exogenous supply of succinate to the growth media. The peroxisomal beta-oxidation activity, dry seed contents of storage lipids, and their mobilization are unaffected in fugu5
malfunction
-
defects in PPase activity cause severe developmental defects and/or growth arrest in several organisms. The fugu5 mutant phenotype, caused by a defect in H+-PPase activity, shows a postgerminative growth phenotype, but is rescued by complementation with the yeast cytosolic PPase IPP1, overview. Increased cytosolic PPi levels Impaired postgerminative development in fugu5 by inhibiting gluconeogenesis
metabolism
PPase is an essential constitutive enzyme for energy metabolism and clearance of excess diphosphate
metabolism
-
implication of H+-PPase in postgerminative oilseed metabolism, overview
metabolism
the soluble pyrophosphatasem RNA exists in great copy numbers in cells of Methanosaeta thermophila
physiological function
vacuolar H+ -ATPases are a specific class of multisubunit pumps that play an essential role in the generation of proton gradients across eukaryotic endomembranes. The plant proton-pumping inorganic pyrophosphatase functionally complements the vacuolar ATPase transport activity and confers bafilomycin resistance when recombinantly expressed in yeast
physiological function
tight control of AtPPsPase1 gene expression underlines its important role in the phosphate starvation response, cleavage of diphosphate is an immediate metabolic adaptation reaction
physiological function
the vacuolar H+-translocating inorganic pyrophosphatase is an electrogenic proton pump, which is related to growth as well as abiotic stress tolerance in plants. MdVHP1 is an important regulator for plant tolerance to abiotic stresses by modulating internal stores of ions and solutes
physiological function
vacuolar H+-diphosphatase, AVP1, is a key enzyme in phosphate hydrolysis
physiological function
V-PPase is an important element in the survival strategies of plants under cold stress. OVP1-enhanced cold tolerance is related to cell membrane integrity and proline accumulation
physiological function
-
the soluble inorganic diphosphatases recycle the pyrophosphate produced by many biosynthetic reactions, and may play a role in the plant adaptation to phosphorus deficiency
physiological function
-
proton-translocating vacuolar PPase, H+-PPase, uses the energy of diphosphate hydrolysis to acidify the vacuole in higher plants. H+-PPase is a master regulator of cytosolic diphosphate homeostasis, another role of H+-PPase in plants is vacuolar acidification, the role of H+-PPase as a proton-pump is negligible
physiological function
Arabidopsis thaliana Col-0
-
tight control of AtPPsPase1 gene expression underlines its important role in the phosphate starvation response, cleavage of diphosphate is an immediate metabolic adaptation reaction
-
physiological function
Malus domestica Fuji
-
the vacuolar H+-translocating inorganic pyrophosphatase is an electrogenic proton pump, which is related to growth as well as abiotic stress tolerance in plants. MdVHP1 is an important regulator for plant tolerance to abiotic stresses by modulating internal stores of ions and solutes
-
metabolism
Methanosaeta thermophila DSM 6194
-
the soluble pyrophosphatasem RNA exists in great copy numbers in cells of Methanosaeta thermophila
-
additional information
His21 and His86 are not essential for diphosphate hydrolysis, but are responsible for a shift in the optimal pH for the reaction compared with the Escherichia coli enzyme
additional information
vacuolar proteases are involved in the processing of native AVP1 and its chimaeric derivatives targeted to the vacuolar membrane
additional information
the catalytic residues are Asp11, Asp13, Thr113, and Lys147, structure-guided site-directed mutagenesis coupled with kinetic analysis of the mutant enzymes identifies the residues required for catalysis, substrate binding, and domain-domain association
additional information
modelling of the active site
additional information
the hinge region plays an important role in opening and closing of the active site between the N- and C-terminal domains of PPase
additional information
MdVHP1 overexpression enhances tolerance to salt, PEG-mimic drought, cold and heat in transgenic apple calluses, which is related to an increased accumulation of proline and decreased MDA content compared with control calli. In addition, MdVHP1 overexpression confers improves tolerance to salt and drought in transgenic tomato, along with an increased ion accumulation, high RWC and low solute potential compared with wild-type, phenotypes, overview
additional information
OVP1 overexpression results in enhanced cold tolerance in transgenic rice, which is related to an increased integrity of cell membrane, decreased MDA content and accumulation of proline to higher level as compared with wild-type rice seedlings
additional information
Arabidopsis thaliana Col-0
-
modelling of the active site
-
additional information
Bacteroides thetaiotaomicron ATCC 29148D
-
the catalytic residues are Asp11, Asp13, Thr113, and Lys147, structure-guided site-directed mutagenesis coupled with kinetic analysis of the mutant enzymes identifies the residues required for catalysis, substrate binding, and domain-domain association
-
additional information
Malus domestica Fuji
-
MdVHP1 overexpression enhances tolerance to salt, PEG-mimic drought, cold and heat in transgenic apple calluses, which is related to an increased accumulation of proline and decreased MDA content compared with control calli. In addition, MdVHP1 overexpression confers improves tolerance to salt and drought in transgenic tomato, along with an increased ion accumulation, high RWC and low solute potential compared with wild-type, phenotypes, overview
-
additional information
-
His21 and His86 are not essential for diphosphate hydrolysis, but are responsible for a shift in the optimal pH for the reaction compared with the Escherichia coli enzyme
-
additional information
Streptococcus gordonii DL1
-
the hinge region plays an important role in opening and closing of the active site between the N- and C-terminal domains of PPase
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-phosphorylethanolamine + H2O
ethanolamine + phosphate
show the reaction diagram
low activity
-
?
3'-AMP + H2O
adenosine + phosphate
show the reaction diagram
-
4% activity compared to diphosphate
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
show the reaction diagram
Arabidopsis thaliana, Arabidopsis thaliana Col-0
low activity
-
?
ADP + H2O
?
show the reaction diagram
-
2.7% relative activity compared to diphosphate
-
-
?
ADP + H2O
?
show the reaction diagram
-
2.6% relative activity compared to diphosphate
-
-
?
ADP + H2O
?
show the reaction diagram
-
18% relative activity compared to diphosphate
-
-
?
ADP + H2O
?
show the reaction diagram
-
hydrolyzed at 36.2% of the rate compared to diphosphate
-
-
?
ADP + H2O
?
show the reaction diagram
Sulfolobus acidocaldarius 7
hydrolyzed at 36.2% of the rate compared to diphosphate
-
-
?
ADP + H2O
?
show the reaction diagram
Streptomyces aureofaciens RIA, Streptomyces aureofaciens RIA57
-
18% relative activity compared to diphosphate
-
-
?
ADP + H2O
?
show the reaction diagram
Rhodospirillum rubrum G-9
-
2.7% relative activity compared to diphosphate
-
-
?
ADP + H2O
AMP + phosphate
show the reaction diagram
-
5% activity compared to diphosphate
-
?
ADP + H2O
? + phosphate
show the reaction diagram
-
3-6% of the activity with diphosphate
-
?
AMP + H2O
?
show the reaction diagram
-
3.6% relative activity compared to diphosphate
-
-
?
ATP + H2O
?
show the reaction diagram
-
hydrolysis only with Zn2+ or Mn2+ as cofactors
-
-
?
ATP + H2O
?
show the reaction diagram
-
7.8% relative activity compared to diphosphate
-
-
?
ATP + H2O
?
show the reaction diagram
-
1.3% relative activity compared to diphosphate
-
-
?
ATP + H2O
?
show the reaction diagram
-
4.2% relative activity compared to diphosphate
-
-
?
ATP + H2O
?
show the reaction diagram
-
3% relative activity compared to diphosphate
-
-
?
ATP + H2O
?
show the reaction diagram
-
reaction only in the presence of Mn2+
-
-
?
ATP + H2O
?
show the reaction diagram
-
reaction only in the presence of Mn2+ or Zn2+
-
-
?
ATP + H2O
?
show the reaction diagram
-
hydrolyzed at 19.4% of the rate compared to diphosphate
-
-
?
ATP + H2O
?
show the reaction diagram
Sulfolobus acidocaldarius 7
hydrolyzed at 19.4% of the rate compared to diphosphate
-
-
?
ATP + H2O
?
show the reaction diagram
Streptomyces aureofaciens RIA
-
7.8% relative activity compared to diphosphate
-
-
?
ATP + H2O
?
show the reaction diagram
Escherichia coli MRE-600
-
reaction only in the presence of Mn2+
-
-
?
ATP + H2O
?
show the reaction diagram
Streptomyces aureofaciens RIA57
-
7.8% relative activity compared to diphosphate
-
-
?
ATP + H2O
?
show the reaction diagram
Rhodospirillum rubrum G-9
-
1.3% relative activity compared to diphosphate
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
1% activity compared to diphosphate
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
4% activity compared to diphosphate
-
?
ATP + H2O
? + phosphate
show the reaction diagram
-
3-6% of the activity with diphosphate
-
?
cyclic tripolyphosphate + H2O
?
show the reaction diagram
-
hydrolyzed at 32.3% of the rate compared to diphosphate
-
-
?
cyclic tripolyphosphate + H2O
?
show the reaction diagram
Sulfolobus acidocaldarius 7
hydrolyzed at 32.3% of the rate compared to diphosphate
-
-
?
D-fructose-6-phosphate + H2O
D-fructose + phosphate
show the reaction diagram
-
13% relative activity compared to diphosphate
-
?
D-glucose-1-phosphate + H2O
D-glucose + phosphate
show the reaction diagram
-
very weak substrate compared to diphosphate
-
?
D-glucose-1-phosphate + H2O
D-glucose + phosphate
show the reaction diagram
-
15% relative activity compared to diphosphate
-
?
D-glucose-6-phosphate + H2O
D-glucose + phosphate
show the reaction diagram
low activity
-
?
dATP + H2O
dADP + phosphate
show the reaction diagram
7% activity compared to diphosphate
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
r
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
r
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
r
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
r
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
r
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
-
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
-
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
-
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
r
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
r
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
r
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
r
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
-
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
Methanothermobacter thermautotrophicum
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
-
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
r
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
r
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
Aranda Christine
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
ir
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
Herpetomonas sp.
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
specific for
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
high specifity with Mg2+ as cofactor
-
r
diphosphate + H2O
2 phosphate
show the reaction diagram
-
reaction may be reversed by coupling to glucose-6-phosphate to 6-phospho-gluconate
-
?, r
diphosphate + H2O
2 phosphate
show the reaction diagram
-
no other substrates
-
-
diphosphate + H2O
2 phosphate
show the reaction diagram
-
actual substrate is magnesium diphosphate or dimagnesium diphosphate
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
actual substrate is magnesium diphosphate or dimagnesium diphosphate
-
-
diphosphate + H2O
2 phosphate
show the reaction diagram
-
actual substrate is magnesium diphosphate or dimagnesium diphosphate
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
actual substrate is magnesium diphosphate or dimagnesium diphosphate
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
actual substrate is magnesium diphosphate or dimagnesium diphosphate
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
actual substrate is magnesium diphosphate or dimagnesium diphosphate
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
actual substrate is magnesium diphosphate or dimagnesium diphosphate
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
actual substrate is magnesium diphosphate or dimagnesium diphosphate
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
actual substrate is magnesium diphosphate or dimagnesium diphosphate
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
actual substrate is magnesium diphosphate or dimagnesium diphosphate
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
actual substrate is magnesium diphosphate or dimagnesium diphosphate
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
high specificity
-
-
diphosphate + H2O
2 phosphate
show the reaction diagram
Methanothermobacter thermautotrophicum
-
high specificity
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
high specificity
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
high specificity
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
high specificity
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
high specificity
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
high specificity
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
high specificity
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
high specificity
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
anabolism
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
H+-pump
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
H+-pump
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
H+-pump
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
H+-pump
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
important for energy metabolism, provides energy for biosynthetic reactions
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
important for energy metabolism, provides energy for biosynthetic reactions
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
important for energy metabolism, provides energy for biosynthetic reactions
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
important for energy metabolism, provides energy for biosynthetic reactions
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
important for energy metabolism, provides energy for biosynthetic reactions
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
important for energy metabolism, provides energy for biosynthetic reactions
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
important for energy metabolism, provides energy for biosynthetic reactions
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
important for energy metabolism, provides energy for biosynthetic reactions
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
important for energy metabolism, provides energy for biosynthetic reactions
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
important for energy metabolism, provides energy for biosynthetic reactions
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
important for energy metabolism, provides energy for biosynthetic reactions, central enzyme of phosphorus metabolism
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
important for energy metabolism, provides energy for biosynthetic reactions, diphosphate hydrolysis dependent proton translocation
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
important for energy metabolism, provides energy for biosynthetic reactions, diphosphate hydrolysis dependent proton translocation
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
important for energy metabolism, provides energy for biosynthetic reactions, diphosphate hydrolysis dependent proton translocation
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
important for energy metabolism, provides energy for biosynthetic reactions, diphosphate hydrolysis dependent proton translocation
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
important for energy metabolism, provides energy for biosynthetic reactions, diphosphate hydrolysis dependent proton translocation
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
important for energy metabolism, provides energy for biosynthetic reactions, diphosphate hydrolysis dependent proton translocation
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
important for energy metabolism, provides energy for biosynthetic reactions, diphosphate hydrolysis dependent proton translocation
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
important for energy metabolism, provides energy for biosynthetic reactions, diphosphate hydrolysis dependent proton translocation
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
important for energy metabolism, provides energy for biosynthetic reactions, diphosphate hydrolysis dependent proton translocation from cytosol to vacuole lumen
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
important for energy metabolism, provides energy for biosynthetic reactions, essential for growth of bloodstream forms in mammalian host
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
important for energy metabolism, provides energy for biosynthetic reactions, proton translocation through membrane provides a source of energy
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
important for energy metabolism, provides energy for biosynthetic reactions, reaction coupled with proton pumping through the vacuole membrane
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
the enzyme and its proton pumping activity have important roles in the accumulation of sugars in vacuoles, the enzyme expression is regulated by phytohormones in a complex manner
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
the enzyme has two distinct roles depending on its location acting as an intracellular proton pump in acidocalcisomes but in diphosphate synthesis in the chromatophore membranes
-
r
diphosphate + H2O
2 phosphate
show the reaction diagram
-
the enzyme plays an essential role in the worms molting and development, and in larval survival in the host, overview
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
Mg2+ is absolutely required for determination of substrate specificity
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
MgPPi
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
an essential and ubiquitous metal-dependent enzyme
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
an essential and ubiquitous metal-dependent enzyme
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
an essential and ubiquitous metal-dependent enzyme
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
an essential and ubiquitous metal-dependent enzyme
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
diphosphate hydrolysis provides a thermodynamic driving force for important biosynthetic reactions, PYP-1 is required for larval development and intestinal function, overview
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
intracellular diphosphate is a by-product of multiple biosynthetic reactions and its hydrolysis by cytosolic iPPase is an important homeostatic mechanism favoring biosynthesis, overview
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
LHPPase is associated with hyperthyroidism
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
PPase plays an essential role in energy conservation and provides the energy for many biosynthetic pathways controlling the intracellular diphosphate levels
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
the enzyme is regulated by reversible phosphorylation, another mechanism in regulation of several physiological processes, e.g. self-incompatibility-mediated pollen tube inhibition, overview
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
V-PPase, localized in plant vacuolar membranes, translocates H+ into the vacuoles in conjunction with the vacuolar H+-ATPase, VATPase, EC 3.6.1.3, regulation, overview
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
diphosphate binding does not cause a significant conformational change in the diphosphate-PPase complex, structure, overview
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
high activity with magnesium diphosphate, low activity with lanthanum diphosphate
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
Lys112 is supposed to play a key role in forming contacts with the phosphate groups of the three studied effectors, overview
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
residues Arg43, Lys148, and Lys115 are involved in binding of diphosphate
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
the enzyme is very specific for diphosphate as substrate, substrate specificity, overview
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
the rate-determining step for the forward reaction with Mg2+ is hydrolysis of PPi, the wild-type active site shows a closed comformation with one of the two product phosphates already dissociated, active site residues Tyr93 and Asp115 are important, six-state catalytic mechanism, overview
in the reverse, net synthesis direction, the rate-determining step is not the condensation of the two phosphate ions but the previous step, which involves isomerization of the enzyme
r
diphosphate + H2O
2 phosphate
show the reaction diagram
the rate-limiting step of Mn2+-supported hydrolysis of the phosphoanhydride bond is followed by a fast release of the leaving phosphate from the P1 site, overview
Mg- or Mn-bound substrate for the synthesis reaction
r
diphosphate + H2O
2 phosphate
show the reaction diagram
in vivo function as an inorganic diphosphatase. Substrate discrimination is based, in part, on active site space restrictions imposed by the cap domain, specifically by residues Tyr76 and Glu47
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
as far as the release of phosphate, is concerned, diphosphate, is the best substrate
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
AtPPsPase1 catalyzes the specific cleavage
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
development and evaluation of a phosphate-based colorimetric assay to measure progress of PCR using the PPase-coupled enzyme assay, overview
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
structure-function analysis, overview. BT2127 conserves the His23-Lys79 diad, and in both the cap-open and -closed conformations, the Asp13 side chain is in the same conformation, engaged in a hydrogen bond with linker residue Ser15
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
the pyrophosphatase hydrolyzes the major part of diphosphate that is produced in the acetate activation reaction
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
pronounced specificity for diphosphate
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
the enzyme shows high specificity for diphosphate but low reactivity to sodium tripolyphosphate and sodium tetrapolyphosphate. ADP and ATP can not serve as substrates
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
important for energy metabolism, provides energy for biosynthetic reactions, diphosphate hydrolysis dependent proton translocation
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
Bacteroides thetaiotaomicron ATCC 29148D
in vivo function as an inorganic diphosphatase. Substrate discrimination is based, in part, on active site space restrictions imposed by the cap domain, specifically by residues Tyr76 and Glu47, structure-function analysis, overview. BT2127 conserves the His23-Lys79 diad, and in both the cap-open and -closed conformations, the Asp13 side chain is in the same conformation, engaged in a hydrogen bond with linker residue Ser15
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
Rhodospirillum rubrum S1
important for energy metabolism, provides energy for biosynthetic reactions, diphosphate hydrolysis dependent proton translocation
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
Pyrococcus horikoshii DSM 12428
the enzyme shows high specificity for diphosphate but low reactivity to sodium tripolyphosphate and sodium tetrapolyphosphate. ADP and ATP can not serve as substrates
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
Sulfolobus tokodaii 7
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
Sulfolobus acidocaldarius 7
-
actual substrate is magnesium diphosphate or dimagnesium diphosphate, high specificity
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
Sulfolobus acidocaldarius 7
as far as the release of phosphate, is concerned, diphosphate, is the best substrate
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
Streptomyces aureofaciens RIA
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
Streptococcus gordonii DL1
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
Methanothermobacter thermautotrophicum H
-
high specificity
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
Leishmania amazonensis MHOM/BR/1987/BA125
Mg2+ is absolutely required for determination of substrate specificity
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
Escherichia coli MRE-600
-
important for energy metabolism, provides energy for biosynthetic reactions
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
Arabidopsis thaliana Col-0
AtPPsPase1 catalyzes the specific cleavage
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
Rhodopseudomonas palustris Dr2
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
PPase plays an essential role in energy conservation and provides the energy for many biosynthetic pathways controlling the intracellular diphosphate levels, diphosphate binding does not cause a significant conformational change in the diphosphate-PPase complex, structure, overview
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
Streptomyces aureofaciens RIA57
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
Rhodospirillum rubrum G-9
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
Pyrococcus horikoshii ATCC 700860D-5
development and evaluation of a phosphate-based colorimetric assay to measure progress of PCR using the PPase-coupled enzyme assay, overview
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
Enterococcus faecium F24
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
Rhodospirillum rubrum Esmarch
-
the enzyme has two distinct roles depending on its location acting as an intracellular proton pump in acidocalcisomes but in diphosphate synthesis in the chromatophore membranes
-
r
diphosphate + H2O
2 phosphate
show the reaction diagram
Rubrivivax gelatinosus Dr2
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
Pyrococcus horikoshii OT-3
specific for
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
Methanosaeta thermophila DSM 6194
the pyrophosphatase hydrolyzes the major part of diphosphate that is produced in the acetate activation reaction
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
Helicobacter pylori 8823
-
actual substrate is magnesium diphosphate or dimagnesium diphosphate, high specificity
-
?
diphosphate + H2O
phosphate + phosphate
show the reaction diagram
-
-
?
diphosphate + H2O
phosphate + phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
phosphate + phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
phosphate + phosphate
show the reaction diagram
-
-
?
diphosphate + H2O
phosphate + phosphate
show the reaction diagram
-
-
?
diphosphate + H2O
phosphate + phosphate
show the reaction diagram
-
100% activity
-
?
diphosphate + H2O
phosphate + phosphate
show the reaction diagram
100% activity
-
?
diphosphate + H2O
phosphate + phosphate
show the reaction diagram
Trypanosoma cruzi Y
-
-
?
diphosphates + H2O
?
show the reaction diagram
-
hydrolysis of organic diphosphates in the presence of Zn2+
-
-
?
GDP + H2O
?
show the reaction diagram
-
20% relative activity compared to diphosphate
-
-
?
GMP + H2O
?
show the reaction diagram
-
18% relative activity compared to diphosphate
-
-
?
imidodiphosphate + H2O
phosphate + NH3
show the reaction diagram
-
hydrolysis even in the absence of divalent cations
-
ir
imidodiphosphate + H2O
phosphate + phosphoramidic acid
show the reaction diagram
active site and substrate binding structure determination and analysis, overview
-
?
phosphoenolpyruvate + H2O
pyruvate + phosphate
show the reaction diagram
-
12% relative activity compared to diphosphate
-
?
phosphoenolpyruvate + H2O
pyruvate + phosphate
show the reaction diagram
-
1-2% of the activity with diphosphate
-
?
phosphoenolpyruvate + H2O
pyruvate + phosphate
show the reaction diagram
Streptomyces aureofaciens RIA, Streptomyces aureofaciens RIA57
-
12% relative activity compared to diphosphate
-
?
polyphosphate + H2O
?
show the reaction diagram
polyphosphate of 28 residues, hydrolyzed only in the presence of Zn2+, central role in the regulation of polyphosphate metabolism, supports recovery from hypoosmotic stress, polyphosphate of 28 residues, poor substrate, hydrolyzed only in the presence of Zn2+
-
-
?
polyphosphate + H2O
?
show the reaction diagram
-
polyphosphate of 28 residues, poor substrate, hydrolyzed only in the presence of Zn2+
-
-
?
polyphosphate + H2O
?
show the reaction diagram
-
less than 1% activity compared to diphosphate
-
-
?
polyphosphate-n28 + H2O
?
show the reaction diagram
-
-
-
?
polyphosphate-n28 + H2O
?
show the reaction diagram
chain length of 28 phosphates
-
-
?
polyphosphate-n28 + H2O
?
show the reaction diagram
Leishmania amazonensis MHOM/BR/1987/BA125
chain length of 28 phosphates
-
-
?
tetrapolyphosphate + H2O
?
show the reaction diagram
-
-
-
-
?
tetrapolyphosphate + H2O
?
show the reaction diagram
-
very weak substrate compared to diphosphate
-
-
?
tetrapolyphosphate + H2O
?
show the reaction diagram
-
25.2% activity compared to the activity with diphosphate
-
-
?
tetrapolyphosphate + H2O
?
show the reaction diagram
Pyrococcus horikoshii DSM 12428
25.2% activity compared to the activity with diphosphate
-
-
?
thiamine diphosphate + H2O
?
show the reaction diagram
Arabidopsis thaliana, Arabidopsis thaliana Col-0
low activity
-
-
?
triphosphate + H2O
3 phosphate
show the reaction diagram
-
-
-
?
triphosphate + H2O
3 phosphate
show the reaction diagram
-
-
?
triphosphate + H2O
? + phosphate
show the reaction diagram
-
3-6% of the activity with diphosphate
-
?
tripolyphosphate + H2O
?
show the reaction diagram
-
-
-
-
?
tripolyphosphate + H2O
?
show the reaction diagram
-
very weak substrate compared to diphosphate
-
-
?
tripolyphosphate + H2O
?
show the reaction diagram
-
hydrolysis only with Zn2+ or Mn2+ as cofactors
-
-
?
tripolyphosphate + H2O
?
show the reaction diagram
hydrolyzed only in the presence of Zn2+
-
-
?
tripolyphosphate + H2O
?
show the reaction diagram
-
reaction only in the presence of Mn2+ or Zn2+
-
-
?
tripolyphosphate + H2O
?
show the reaction diagram
-
hydrolyzed at 44.3% of the rate compared to diphosphate
-
-
?
tripolyphosphate + H2O
?
show the reaction diagram
-
40.3% activity compared to the activity with diphosphate
-
-
?
tripolyphosphate + H2O
?
show the reaction diagram
Pyrococcus horikoshii DSM 12428
40.3% activity compared to the activity with diphosphate
-
-
?
tripolyphosphate + H2O
?
show the reaction diagram
Sulfolobus acidocaldarius 7
hydrolyzed at 44.3% of the rate compared to diphosphate
-
-
?
TTP + H2O
? + phosphate
show the reaction diagram
-
10% of the activity with diphosphate
-
?
UTP + H2O
?
show the reaction diagram
Streptomyces aureofaciens, Streptomyces aureofaciens RIA, Streptomyces aureofaciens RIA57
-
32% relative activity compared to diphosphate
-
-
?
ITP + H2O
? + phosphate
show the reaction diagram
-
10% of the activity with diphosphate
-
?
additional information
?
-
-
enzyme may be identical with EC 3.1.3.1 or EC 3.1.3.9
-
-
-
additional information
?
-
-
no hydrolysis of ATP and traces of activity with tripolyphosphate in the presence of Mg2+
-
-
-
additional information
?
-
-
no hydrolysis of ATP in the presence of Mg2+
-
-
-
additional information
?
-
polyphosphates and ATP are not hydrolyzed
-
-
-
additional information
?
-
-
trimetaphosphate and tripolyphosphate are hydrolyzed with 2% of the rate with diphosphate, no other phosphorylated compounds are hydrolyzed
-
-
-
additional information
?
-
Herpetomonas sp.
-
the enzyme acts as diphosphate-dependent H+-translocation pump, the organism regulates the intracellular distribution of H+ and Ca2+ in the plant host cell, mechanism
-
-
-
additional information
?
-
-
the enzyme is a V-type vacuolar H+-pump and responsible for phosphate uptake across the vacuolar membrane, mechanism of activation of phosphate uptake into the vacuole under low phosphate status, overview
-
-
-
additional information
?
-
VSP1 is not essential for Leishmania promastigote growth and macrophage infection but for metacyclogenesis, VSP1 is essential to maintain virulence in mice
-
-
-
additional information
?
-
-
the enzyme acts as diphosphate-dependent H+-translocation pump
-
-
-
additional information
?
-
Herpetomonas sp.
-
the enzyme acts as diphosphate-dependent H+-translocation pump dependent on K+ in acidic vacuoles
-
-
-
additional information
?
-
-
the enzyme also shows H+-translocation activity
-
-
-
additional information
?
-
-
the enzyme is a membrane H+-pump
-
-
-
additional information
?
-
triphosphate, ATP, and ADP are poor substrates, AMP, phosphoenolpyruvate, and 4-nitrophenyl phosphate are no substrates
-
-
-
additional information
?
-
-
enzyme is specific for diphosphate and does not cleave nucleotide-polyphosphates
-
-
-
additional information
?
-
-
cytosolic phosphoproteins p26.1 from incompatible pollen show rapid, self-incompatibility-induced Ca2+-dependent hyperphosphorylation in vivo, overview
-
-
-
additional information
?
-
-
the hormones abscisic acid, auxin, and 2,4-dinitrophenol are responsible for regulation of the inorganic pyrophosphatase enzyme activity, overview
-
-
-
additional information
?
-
active site residues are His9, Arg13, Asp15, Asp77, His99, His100, Asp151, Lys207, Arg297 and Lys298
-
-
-
additional information
?
-
-
no activity with sodium triphosphate, ADP, ATP, and glucose-6-phosphate
-
-
-
additional information
?
-
-
the enzyme contains an extra binding site for the substrate magnesium diphosphate or its non-hydrolyzable analogue magnesium methylenediphosphonate, binding of substrate at the effector site of pyrophosphatase increases the rate of its hydrolysis at the active site, overview
-
-
-
additional information
?
-
dCTP, ADP, dAMP, phosphoglycolate, phosphoserine, polyphosphate, and 4-nitrophenyl phosphate are no substrates for PPase
-
-
-
additional information
?
-
-
no activity with PAP, PAPS, 3'-CMP, fructose 1,6-bisphosphate, and D-myo-inositol 1-monophosphate
-
-
-
additional information
?
-
BT2127 substrate specificity profile, overview
-
-
-
additional information
?
-
proton-translocation activities are assayed by monitoring the fluorescence quenching of 9-amino-6-chloro-2-methoxyacridine
-
-
-
additional information
?
-
substrate specificity, overview. The enzyme is highly specific, no or poor activity with ribose-5-phosphate, phospho-L-serine, o-phosphocholine, phosphoenolpyruvate, L-glycerol-3-phosphate, beta-glycerol-phosphate, and phospho-L-tyrosine
-
-
-
additional information
?
-
Bacteroides thetaiotaomicron ATCC 29148D
BT2127 substrate specificity profile, overview
-
-
-
additional information
?
-
Leishmania amazonensis MHOM/BR/1987/BA125
VSP1 is not essential for Leishmania promastigote growth and macrophage infection but for metacyclogenesis, VSP1 is essential to maintain virulence in mice
-
-
-
additional information
?
-
Escherichia coli MRE-600
-
no hydrolysis of ATP in the presence of Mg2+
-
-
-
additional information
?
-
Arabidopsis thaliana Col-0
substrate specificity, overview. The enzyme is highly specific, no or poor activity with ribose-5-phosphate, phospho-L-serine, o-phosphocholine, phosphoenolpyruvate, L-glycerol-3-phosphate, beta-glycerol-phosphate, and phospho-L-tyrosine
-
-
-
additional information
?
-
Rhodospirillum rubrum Esmarch
-
the enzyme is a membrane H+-pump
-
-
-
additional information
?
-
Pyrococcus horikoshii OT-3
triphosphate, ATP, and ADP are poor substrates, AMP, phosphoenolpyruvate, and 4-nitrophenyl phosphate are no substrates
-
-
-
additional information
-
-
Sulfolobus tokodaii, Sulfolobus tokodaii 7
the enzyme is possibly involved in glycoprotein biosynthesis
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
diphosphate + H2O
2 phosphate
show the reaction diagram
P37487
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
r
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
r
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
r
diphosphate + H2O
2 phosphate
show the reaction diagram
P0A7A9
-
-
r
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
-
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
-
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
-
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
r
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
r
diphosphate + H2O
2 phosphate
show the reaction diagram
P00817
-
-
r
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
-
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
Methanothermobacter thermautotrophicum
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
-
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
Aranda Christine
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
Q41758
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
Q84L25, Q84L28, Q9M4S1
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
O59570
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
O59570
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
Q93Y52, Q949J1
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
Q9LXC9
-
-
ir
diphosphate + H2O
2 phosphate
show the reaction diagram
Q7Z031
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
Q15181, Q9H2U2
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
P95765
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
Herpetomonas sp.
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
P31414
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
P56153
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
Q8DYS6
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
A8MQH1
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
P9WI55
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
Q67YC0
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
actual substrate is magnesium diphosphate or dimagnesium diphosphate
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
actual substrate is magnesium diphosphate or dimagnesium diphosphate
-
-
diphosphate + H2O
2 phosphate
show the reaction diagram
-
actual substrate is magnesium diphosphate or dimagnesium diphosphate
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
actual substrate is magnesium diphosphate or dimagnesium diphosphate
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
actual substrate is magnesium diphosphate or dimagnesium diphosphate
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
actual substrate is magnesium diphosphate or dimagnesium diphosphate
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
actual substrate is magnesium diphosphate or dimagnesium diphosphate
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
actual substrate is magnesium diphosphate or dimagnesium diphosphate
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
actual substrate is magnesium diphosphate or dimagnesium diphosphate
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
actual substrate is magnesium diphosphate or dimagnesium diphosphate
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
actual substrate is magnesium diphosphate or dimagnesium diphosphate
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
anabolism
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
H+-pump
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
H+-pump
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
H+-pump
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
H+-pump
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
important for energy metabolism, provides energy for biosynthetic reactions
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
important for energy metabolism, provides energy for biosynthetic reactions
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
important for energy metabolism, provides energy for biosynthetic reactions
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
important for energy metabolism, provides energy for biosynthetic reactions
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
important for energy metabolism, provides energy for biosynthetic reactions
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
Q6UQ31
important for energy metabolism, provides energy for biosynthetic reactions
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
important for energy metabolism, provides energy for biosynthetic reactions
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
important for energy metabolism, provides energy for biosynthetic reactions
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
important for energy metabolism, provides energy for biosynthetic reactions
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
O67501
important for energy metabolism, provides energy for biosynthetic reactions
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
important for energy metabolism, provides energy for biosynthetic reactions, central enzyme of phosphorus metabolism
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
important for energy metabolism, provides energy for biosynthetic reactions, diphosphate hydrolysis dependent proton translocation
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
important for energy metabolism, provides energy for biosynthetic reactions, diphosphate hydrolysis dependent proton translocation
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
important for energy metabolism, provides energy for biosynthetic reactions, diphosphate hydrolysis dependent proton translocation
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
important for energy metabolism, provides energy for biosynthetic reactions, diphosphate hydrolysis dependent proton translocation
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
Q9BK08
important for energy metabolism, provides energy for biosynthetic reactions, diphosphate hydrolysis dependent proton translocation
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
Q86M43
important for energy metabolism, provides energy for biosynthetic reactions, diphosphate hydrolysis dependent proton translocation
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
important for energy metabolism, provides energy for biosynthetic reactions, diphosphate hydrolysis dependent proton translocation
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
O68460
important for energy metabolism, provides energy for biosynthetic reactions, diphosphate hydrolysis dependent proton translocation
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
important for energy metabolism, provides energy for biosynthetic reactions, diphosphate hydrolysis dependent proton translocation from cytosol to vacuole lumen
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
Q7Z029
important for energy metabolism, provides energy for biosynthetic reactions, essential for growth of bloodstream forms in mammalian host
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
important for energy metabolism, provides energy for biosynthetic reactions, proton translocation through membrane provides a source of energy
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
important for energy metabolism, provides energy for biosynthetic reactions, reaction coupled with proton pumping through the vacuole membrane
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
the enzyme and its proton pumping activity have important roles in the accumulation of sugars in vacuoles, the enzyme expression is regulated by phytohormones in a complex manner
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
the enzyme has two distinct roles depending on its location acting as an intracellular proton pump in acidocalcisomes but in diphosphate synthesis in the chromatophore membranes
-
r
diphosphate + H2O
2 phosphate
show the reaction diagram
-
the enzyme plays an essential role in the worms molting and development, and in larval survival in the host, overview
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
an essential and ubiquitous metal-dependent enzyme
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
P80507
an essential and ubiquitous metal-dependent enzyme
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
P80562
an essential and ubiquitous metal-dependent enzyme
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
P58733
an essential and ubiquitous metal-dependent enzyme
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
Q18680
diphosphate hydrolysis provides a thermodynamic driving force for important biosynthetic reactions, PYP-1 is required for larval development and intestinal function, overview
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
intracellular diphosphate is a by-product of multiple biosynthetic reactions and its hydrolysis by cytosolic iPPase is an important homeostatic mechanism favoring biosynthesis, overview
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
LHPPase is associated with hyperthyroidism
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
P56153
PPase plays an essential role in energy conservation and provides the energy for many biosynthetic pathways controlling the intracellular diphosphate levels
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
the enzyme is regulated by reversible phosphorylation, another mechanism in regulation of several physiological processes, e.g. self-incompatibility-mediated pollen tube inhibition, overview
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
V-PPase, localized in plant vacuolar membranes, translocates H+ into the vacuoles in conjunction with the vacuolar H+-ATPase, VATPase, EC 3.6.1.3, regulation, overview
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
Q8A5V9
in vivo function as an inorganic diphosphatase. Substrate discrimination is based, in part, on active site space restrictions imposed by the cap domain, specifically by residues Tyr76 and Glu47
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
A0B5R0
the pyrophosphatase hydrolyzes the major part of diphosphate that is produced in the acetate activation reaction
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
Q9BK08
important for energy metabolism, provides energy for biosynthetic reactions, diphosphate hydrolysis dependent proton translocation
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
Bacteroides thetaiotaomicron ATCC 29148D
Q8A5V9
in vivo function as an inorganic diphosphatase. Substrate discrimination is based, in part, on active site space restrictions imposed by the cap domain, specifically by residues Tyr76 and Glu47
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
Rhodospirillum rubrum S1
O68460
important for energy metabolism, provides energy for biosynthetic reactions, diphosphate hydrolysis dependent proton translocation
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
Sulfolobus acidocaldarius 7
-
actual substrate is magnesium diphosphate or dimagnesium diphosphate
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
Streptomyces aureofaciens RIA
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
Streptococcus gordonii DL1
P95765
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
Methanothermobacter thermautotrophicum H
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
Leishmania amazonensis MHOM/BR/1987/BA125
Q7Z031
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
Escherichia coli MRE-600
-
important for energy metabolism, provides energy for biosynthetic reactions
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
Arabidopsis thaliana Col-0
Q67YC0
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
Rhodopseudomonas palustris Dr2
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
P56153
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
P56153
PPase plays an essential role in energy conservation and provides the energy for many biosynthetic pathways controlling the intracellular diphosphate levels
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
Streptomyces aureofaciens RIA57
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
Rhodospirillum rubrum G-9
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
P9WI55
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
Pyrococcus horikoshii ATCC 700860D-5
O59570
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
Enterococcus faecium F24
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
Rhodospirillum rubrum Esmarch
-
the enzyme has two distinct roles depending on its location acting as an intracellular proton pump in acidocalcisomes but in diphosphate synthesis in the chromatophore membranes
-
r
diphosphate + H2O
2 phosphate
show the reaction diagram
Rubrivivax gelatinosus Dr2
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
Pyrococcus horikoshii OT-3
O59570
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
Methanosaeta thermophila DSM 6194
A0B5R0
the pyrophosphatase hydrolyzes the major part of diphosphate that is produced in the acetate activation reaction
-
?
polyphosphate + H2O
?
show the reaction diagram
Q7Z029
polyphosphate of 28 residues, hydrolyzed only in the presence of Zn2+, central role in the regulation of polyphosphate metabolism, supports recovery from hypoosmotic stress
-
-
?
polyphosphate-n28 + H2O
?
show the reaction diagram
Leishmania amazonensis, Leishmania amazonensis MHOM/BR/1987/BA125
Q7Z031
-
-
-
?
triphosphate + H2O
3 phosphate
show the reaction diagram
Q7Z031
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
Helicobacter pylori 8823
-
actual substrate is magnesium diphosphate or dimagnesium diphosphate
-
?
additional information
?
-
Herpetomonas sp.
-
the enzyme acts as diphosphate-dependent H+-translocation pump, the organism regulates the intracellular distribution of H+ and Ca2+ in the plant host cell, mechanism
-
-
-
additional information
?
-
-
the enzyme is a V-type vacuolar H+-pump and responsible for phosphate uptake across the vacuolar membrane, mechanism of activation of phosphate uptake into the vacuole under low phosphate status, overview
-
-
-
additional information
?
-
Q7Z031
VSP1 is not essential for Leishmania promastigote growth and macrophage infection but for metacyclogenesis, VSP1 is essential to maintain virulence in mice
-
-
-
additional information
?
-
-
cytosolic phosphoproteins p26.1 from incompatible pollen show rapid, self-incompatibility-induced Ca2+-dependent hyperphosphorylation in vivo, overview
-
-
-
additional information
?
-
-
the hormones abscisic acid, auxin, and 2,4-dinitrophenol are responsible for regulation of the inorganic pyrophosphatase enzyme activity, overview
-
-
-
additional information
-
-
Sulfolobus tokodaii, Sulfolobus tokodaii 7
F9VPB8
the enzyme is possibly involved in glycoprotein biosynthesis
-
-
-
additional information
?
-
Leishmania amazonensis MHOM/BR/1987/BA125
Q7Z031
VSP1 is not essential for Leishmania promastigote growth and macrophage infection but for metacyclogenesis, VSP1 is essential to maintain virulence in mice
-
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
-
most potent activator
Ca2+
-
hydrolysis of nucleoside triphosphates stimulated
Ca2+
-
alkaline enzyme activated
Ca2+
CaCl2 at 0.1 mM favors the formation of large complexes
Ca2+
-
2% of the activity with Mg2+
Ca2+
-
activates at up to 1 mM, inhibits at higher concentrations, complete inhibition at 2 mM, overview
Ca2+
-
can displace Mg2+
Cd2+
-
4 Cd2+ sites per subunit, enzyme activity lower compared to Mg2+
CdCl2
-
20 mM, 155% stimulation
Co2+
-
6.7% relative activity compared to Mg2+, no activity in the absence of divalent cations
Co2+
-
about 20% relative activity to Mg2+ when above 3 mM
Co2+
-
lower activation than Mg2+
Co2+
-
24% relative activity compared to Mg2+
Co2+
-
25% relative activity compared to Mg2+
Co2+
-
activation of enzyme with acid pH
Co2+
-
alkaline enzyme activated
Co2+
-
protects against fluoride inhibition
Co2+
-
activating
Co2+
-
increases hydrolysis of imidophosphate
Co2+
Methanothermobacter thermautotrophicum
-
can partially replace Mg2+, 15%
Co2+
-
supports the hydrolysis of ATP and tripolyphosphate, very weak activation of diphosphate hydrolysis
Co2+
-
35% of the activity with Mg2+
Co2+
minor activation
Co2+
can substitute for Mg2+ at concentrations up to 0.5 mM, inhibitory above
Co2+
-
88% of the activity with Mg2+
Co2+
-
activates at up to 1 mM, inhibits at higher concentrations, overview
Co2+
-
CBS-PPase requires transition metal ions, Co2+ or Mn2+, for activity
Co2+
-
activates 25%
Co2+
-
60.1% of the activity with Mg2+
Co2+
Mg2+ is 72% less effective when compared with Ni2+, maximum activity occurs at 0.5 mM Co2+
Co2+
-
about 15% activity in the presence of 50 mM Co2+ compared to 50 mM Mg2+
Co2+
activates to 50% of the activity with Mg2+ at 2 mM
Co2+
-
absolute requirement for divalent cations, 2.5 mM Mn2+ activates 37% compared to 2.5 mM Mg2+
Cu2+
-
35% of the activity with Mg2+
Cu2+
can partially, upt to 30%, substitute for Mg2+; can partially, upt to 30%, substitute for Mg2+
Cu2+
-
activates
Fe2+
can partially, upt to 30%, substitute for Mg2+; can partially, upt to 30%, substitute for Mg2+
Fe2+
-
activates 34%
Fe2+
activates to 88% of the activity with Mg2+ at 2 mM
Fe3+
bound in in sites M1 and M2, the Fe3+:Mn2+ ratio is about 6:1 in site M1 and about 2:1 in site M2
K+
-
required for activity
K+
-
required for activity
K+
-
slight activation
K+
2-3fold activation
K+
-
required, highly activating
K+
stimulates the normophilic isozyme AVP1
K+
-
required, preferred monovalent cation
K+
Herpetomonas sp.
-
required for diphosphate-dependent H+-uptake
K+
determination of K+-binding sites
lanthanum
-
results in a slow substrate binding to diphosphate
Mg2+
-
no other divalent cations can substitute for Mg2+
Mg2+
-
-
Mg2+
Aranda Christine
-
no other divalent cations can substitute for Mg2+; required for activity and stability
Mg2+
-
activity enhanced of the mitochondrial enzyme
Mg2+
-
maximum activity
Mg2+
-
no other divalent cations can substitute for Mg2+
Mg2+
-
required for activity
Mg2+
-
maximum activation compared to other divalent ion activators
Mg2+
-
maximum activity at 3 mM
Mg2+
-
maximum activation at 4 mM; no other divalent cations can substitute for Mg2+
Mg2+
-
required for activity
Mg2+
-
maximum activation compared to other divalent ion activators
Mg2+
-
required for activity
Mg2+
-
required for activity
Mg2+
-
no other divalent cations can substitute for Mg2+; required for activity and stability
Mg2+
-
maximum activity
Mg2+
-
required for activity
Mg2+
-
-
Mg2+
-
required for activity
Mg2+
-
activation of enzyme with alkaline pH
Mg2+
-
activation of enzyme with alkaline pH; alkaline enzyme activated
Mg2+
-
required for activity
Mg2+
-
required for activity; required for activity and stability
Mg2+
-
maximum activity
Mg2+
-
required for activity and stability
Mg2+
-
free Mg2+ ions are not required
Mg2+
-
no other divalent cations can substitute for Mg2+; required for activity
Mg2+
-
increases hydrolysis of imidophosphate; or other divalent cation required for hydrolysis of diphosphate
Mg2+
-
no other divalent cations can substitute for Mg2+; required for activity
Mg2+
-
stabilization of the hexameric E20D enzyme; wild type: two Mg2+ ions per active site required for catalysis
Mg2+
-
four Mg2+ ions per active site required for catalysis
Mg2+
-
required for activity
Mg2+
-
no other divalent cations can substitute for Mg2+; required for activity
Mg2+
Methanothermobacter thermautotrophicum
-
required for activity
Mg2+
-
no other divalent cations can substitute for Mg2+; required for activity
Mg2+
-
required for activity
Mg2+
-
required for activity
Mg2+
-
required, highest activity with a Mg2+/diphosphate ratio of 2
Mg2+
-
required, three binding sites in the absence of substrate
Mg2+
-
required, serves as physiological cofactor
Mg2+
-
required, inhibitory for the native hexamer above 5 mM, no inhibition of the dimeric form
Mg2+
-
required
Mg2+
required, highest activity at 5 mM, decrease of activity at higher concentrations
Mg2+
-
required
Mg2+
much less effective than Ca2+, 20% of the activity with Ca2+
Mg2+
-
required
Mg2+
-
required for activity and stability
Mg2+
-
required
Mg2+
-
required, highest activity at 5 mM
Mg2+
-
required, best divalent cation, binding site structure
Mg2+
required, best divalent cation, 5 mM, Km is 0.303 mM
Mg2+
required, best divalent cation; required, best divalent cation
Mg2+
-
required, substrate is magnesium diphoshate
Mg2+
-
preferred by family I PPase, 20 mM
Mg2+
the enzyme requires divalent cations, 5 mM
Mg2+
required, optimal at 5 mM; required, optimal at 5 mM
Mg2+
VSP1 is dependent on divalent cations Mg2+ or Zn2+, Mg2+ is absolutely required for determination of substrate specificity and cannot be substituted by other metal ions
Mg2+
-
required, the ER H+-pyrophosphatase requires higher concentrations as the vacuolar H+-pyrophosphatase
Mg2+
-
required
Mg2+
-
preferred divalent cation, Km value 0.9 mM
Mg2+
-
one Mg2+ per active site
Mg2+
binding structure, overview
Mg2+
-
7-8fold activation
Mg2+
dependent on, other divalent cations substituted poorly for Mg2+
Mg2+
the pyrophosphatase requires four divalent metal cations for catalysis, magnesium provides the highest activity
Mg2+
-
dependent on, bound to the enzyme
Mg2+
-
dependent on, activates, bound to the substrate as magnesium diphosphate
Mg2+
activates, Mg2+ is the highly preferred cofactor for family I sPPases
Mg2+
-
activates, Mg2+ is the preferred cofactor for family I sPPases
Mg2+
activates, Mg2+ is the highly preferred cofactor for family I sPPases
Mg2+
activates, Mg2+ is the highly preferred cofactor for family I sPPases
Mg2+
-
binding depends highly on the pH, binds to the active site, binding structure, overview
Mg2+
-
most effetive divalent cation, can partially be replaced by other divalent cations
Mg2+
-
dependent on, cannot be substituted by Mn2+ or Ca2+
Mg2+
dependent on, can be partially substituted by Mn2+, both isozymes show similar catalytic constants and affinities for the Mg-pyrophosphate complex, while differed in their affinity for free Mg2+,
Mg2+
required, binds to diphosphate, effects on enzyme activity and kinetics, pH-dependence, overview
Mg2+
-
activates by decreasing the value of the Michaelis-Menten constant, dependent on, highest activity at pH 7.4 and 5.0 mM, Mg2+ shifts the pH optimum, Mg2+ associates rather weakly with the pyrophosphatase active center and can be readily displaced by Ca2+ , overview
Mg2+
-
dependent on, maximum activity is obtained in the presence of 5 mM Mg2+, no diphosphate hydrolysis is detected in the absence of Mg2+
Mg2+
-
dependent on, the active site contains four Mg2+ ions
Mg2+
-
required for activity
Mg2+
the activity of the enzyme is strongly dependent on Mg2+. High enzyme activity is found between 1 and 100 mM Mg2+ with a maximum activity at 10 mM. At pH 7.5, the maximum PPase activity is at 50 mM Mg2+
Mg2+
Mg2+ is 9% less effective when compared with Ni2+, maximum activity occurs at 2 mM Mg2+
Mg2+
-
maximal activity in the presence of 0.2 mM Mg2+
Mg2+
required for catalysis
Mg2+
-
required
Mg2+
required, functions in catalysis and binding structure, overview
Mg2+
dependent on, 10 mM
Mg2+
-
required, one of the three active site Mg2+ ions is bound along with phosphate
Mg2+
-
absolute requirement for divalent cations for catalytic action, Mg2 + (2.5 mM) conferring the highest activity. KM for Mg2+ is approximately 1.7 mM
Mg2+
-
maximum activity in the presence of Mg2+, influence of other metal cations is negligible
MgCl2
-
20 mM, 163% stimulation
Mn2+
-
7.3% relative activity compared to Mg2+, no activity in the absence of divalent cations
Mn2+
-
lower activation than Mg2+
Mn2+
-
10.6% relative activity compared to Mg2+
Mn2+
-
protects against fluoride inhibition
Mn2+
-
activating; conversion of the enzyme from inactive dimer to active trimer
Mn2+
-
increases hydrolysis of imidophosphate
Mn2+
-
supports the hydrolysis of ATP and tripolyphosphate, very weak activation of diphosphate hydrolysis
Mn2+
-
can partially replace Mg2+
Mn2+
-
can partially replace for Mg2+
Mn2+
minor activation
Mn2+
can substitute for Mg2+ at concentrations up to 0.5 mM, inhibitory above
Mn2+
can partially, upt to 30%, substitute for Mg2+; can partially, upt to 30%, substitute for Mg2+
Mn2+
-
preferred by family II PPase, 50 mM
Mn2+
the enzyme requires divalent cations
Mn2+
-
32% of the activity with Mg2+
Mn2+
-
activates at up to 1 mM, inhibits at higher concentrations, overview
Mn2+
-
CBS-PPase requires transition metal ions, Co2+ or Mn2+, for activity
Mn2+
-
activates
Mn2+
bound in in sites M1 and M2, the Fe3+:Mn2+ ratio is about 6:1 in site M1 and about 2:1 in site M2
Mn2+
-
binding depends highly on the pH, four ions bound per enzyme molecule, binds to the active site, binding structure, overview
Mn2+
-
32.8% of the activity with Mg2+
Mn2+
can partially substitute for Mg2+
Mn2+
-
required for activity
Mn2+
substitution of Mg2+ cations with Mn2+ results in significantly lower activity of 25.34% of the Mg2+-induced activity
Mn2+
activates to 39% of the activity with Mg2+ at 2 mM
Mn2+
required, activates at 2 mM
Ni2+
-
3% of the activity with Mg2+
Ni2+
dependent on, divalent metal cation with highest efficiency on enzymatic activity, maximum activity occurs at 0.5 mM Ni2+
Ni2+
activates to 83% of the activity with Mg2+ at 2 mM
NiCl2
-
20 mM, 156% stimulation
Zn2+
-
higher activation than Co2+, Mn2+
Zn2+
-
alkaline enzyme activated
Zn2+
-
supports the hydrolysis of ATP and tripolyphosphate, very weak activation of diphosphate hydrolysis
Zn2+
required for the hydrolysis of tripolyphosphate and polyphosphate
Zn2+
about the same activation as with Mg2+
Zn2+
can substitute for Mg2+ at concentrations up to 0.5 mM, inhibitory above
Zn2+
can partially, upt to 30%, substitute for Mg2+; can partially, upt to 30%, substitute for Mg2+
Zn2+
VSP1 is dependent on divalent cations Mg2+ or Zn2+
Zn2+
-
95% of the activity with Mg2+
Zn2+
-
highly activates at up to 1 mM, inhibits at higher concentrations, overview
Zn2+
-
activates 40%
Zn2+
13% of the activity with Mg2+
Zn2+
substitution of Mg2+ cations with Zn2+ results in significantly lower activity of 14.3% of the Mg2+-induced activity
Zn2+
-
absolute requirement for divalent cations, 2.5 mM Mn2+ activates 21% compared to 2.5 mM Mg2+
Mn2+
-
absolute requirement for divalent cations, 2.5 mM Mn2+ activates 17% compared to 2.5 mM Mg2+
additional information
-
no activity in the absence of divalent cations
additional information
-
no divalent cations required for activity
additional information
-
no divalent cations required for activity
additional information
other metal ions can partially replace Ca+, activation decreases in the order Ca2+> Cu2+> Mn2+> Fe2+> Mg2+> Zn2+> Co2+
additional information
-
other metal ions can partially replace Mg2+, activation decreases in the order Mg2+, Co2+, Cu2+, Fe2+, Zn2+, Mn2+
additional information
no activation by Ni2+
additional information
isozyme AVP2 is K+-insensitive
additional information
-
divalent cation required. Activity in decreasing order: Mg2+, Zn2+, Co2+, Mn2+, Ni2+, Ca2+
additional information
-
no divalent cation required
additional information
no effect by Ca2+, Cd2+, and Ni2+
additional information
the enzyme is absolutely dependent on divalent cations, poor activity with Mn2+, Cu2+, Fe2+, Zn2+, and Co2+
additional information
-
the enzyme is absolutely dependent on divalent cations
additional information
the enzyme is absolutely dependent on divalent cations, poor activity with Mn2+, Cu2+, Fe2+, Zn2+, and Co2+
additional information
the enzyme is absolutely dependent on divalent cations, poor activity with Mn2+, Cu2+, Fe2+, and Co2+
additional information
the enzyme contains a unique trinuclear metal center, detailed structure analysis, overview. Mn2+ and Fe3+ do not exchange for Mg2+ even in the presence of a large excess of Mg2+
additional information
-
no effect by Ca2+, Cu2+, and Fe2+
additional information
-
the enzyme retains measurable activity up to 0.7-0.8 M NaCl, KCl, or NH4Cl
additional information
little or no activity is observed in the presence of Cu2+, Zn2+, Ca2+, or Mn2+; PPase has an absolute dependence on divalent metal cations because no measurable activity is observed in their absence
additional information
-
not affected by 50 mM Mn2+, Ni2+, Ca2+, Zn2+, and Cu2+
additional information
the metal binding residues are Asp171, Asn172, and Glu47
additional information
-
divalent cations are not essential for the acid PPase activity
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1,1,1,1-azodimethyl diamide
-
-
-
2,3-Butanedione
-
-
2,4,6-Trinitrobenzenesulfonic acid
-
-
2,4,6-Trinitrobenzenesulfonic acid
-
-
2,4,6-Trinitrobenzenesulfonic acid
-
-
2-phosphoglyceric acid
-
in the absence of free Mg2+
4-bromophenacyl bromide
-
-
4-hydroxymercuribenzoate
-
-
4-hydroxymercuribenzoate
-
-
4-hydroxymercuribenzoate
-
-
7-Chloro-4-nitrobenzo-2-oxa-1,3-diazole
-
-
7-Chloro-4-nitrobenzo-2-oxa-1,3-diazole
-
-
ADP
-
partially inhibited
ADP
-
complete inhibition at 0.1 mM
ADP
-
above 10 mM
aminomethylenediphosphonate
IC50: 0.0009 mM
AMP
-
partially inhibited
AMP
-
96% inhibition at 0.1 mM
ATP
-
partially inhibited
ATP
-
above 3 mM
ATP
-
competitive
ATP
-
competes with methylenediphosphonate and diphosphate for binding at the allosteric regulatory site involving Lys112
ATP
50% inhibition at 2 mM, 90% at 3 mM ATP
ATP
-
above 10 mM
bisphosphonates
-
weak inhibition
Ca2+
Aranda Christine
-
most effective inhibitor among the cations tested
Ca2+
-
50% inhibition at 0.1 mM, no effect at physiological concentrations
Ca2+
-
-
Ca2+
-
-
Ca2+
-
-
Ca2+
-
-
Ca2+
-
strong, potent
Ca2+
-
less effective than Cd2+
Ca2+
-
strong inhibitor
Ca2+
-
50% at 0.012 mM: Mg2+ 0.4 mM
Ca2+
very potent inhibitor
Ca2+
competitive
Ca2+
over 90% inhibition at 0.12 mM; over 90% inhibition at 0.12 mM
Ca2+
-
activates at up to 1 mM, inhibits at higher concentrations, complete inhibition at 2 mM, overview
Ca2+
-
inhibits sPPase activity of the enzyme, 62% inhibition of p26.1a, 49% of p26.1b
Ca2+
enzymatic activity is inhibited more than 95% in the presence of 5 mM Ca2+
Ca2+
-
inhibits the cleavage of diphosphate in the presence of 2.5 mM Mg2+. 0.01 mM CaCl2 inhibits the enzyme by about 50%
Ca2+-diphosphate
-
nonhydrolyzable substrate analogue
CaCl2
-
inhibitory form is the Ca2+diphosphate complex
cAMP
-
58% inhibition at 0.1 mM
Cd2+
Aranda Christine
-
-
Cd2+
-
-
CDP
-
50% inhibition at 0.1 mM
Co2+
Aranda Christine
-
-
Co2+
-
-
Co2+
-
-
Co2+
-
-
Co2+
-
less effective than Ca2+
Co2+
can substitute for Mg2+ at concentrations up to 0.5 mM, inhibitory above
Co2+
-
activates at up to 1 mM, inhibits at higher concentrations, overview
Cu2+
-
-
Cu2+
-
-
Cu2+
-
less effective then Mn2+
Cyanate
-
-
D-glucose
-
non-competitive
D-Glucose-6-phosphate
-
competitive
Diazonium-1H-tetrazole
-
-
diethyldicarbonate
-
-
Diethylpyrocarbonate
-
-
diphosphate
-
above 1 mM
diphosphate
-
hydrolysis of imidophosphate competitively inhibited in the absence of divalent cations
diphosphate
-
free
diphosphate
-
competes with ATP and methylenediphosphonate for binding at the allosteric regulatory site involving Lys112
diphosphate
high substrate inhibition at low levels of Mg2+
diphosphate
-
above 10 mM
EDTA
Aranda Christine
-
-
EDTA
-
-
EDTA
-
Na2SO4, Li2SO4 enhance deactivation, Mn2+ is protective
EDTA
-
89% activation at 0.9 mM, complete inhibition at 5 mM
EDTA
enzymatic activity is inhibited more than 70% in the presence of 5 mM EDTA
F-
-
IC50: 1-2 mM
F-
Aranda Christine
-
-
F-
-
-
F-
-
Co2+ and Mn2+ protect against fluoride inhibition
F-
-
inhibits the H+-translocation activity in endoplasmic reticulum vesicles
F-
Herpetomonas sp.
-
-
F-
-
20 mM, 80% inhibition
Fluorescein 5'-isothiocyanate
-
-
Fluorescein 5'-isothiocyanate
-
-
fluoride
potent inhibition, IC50: 0.1 mM
fluoride
-
50% inhibition at 0.5 mM, 70-80% at 1.0 mM
fluoride
inhibition of wild-type and mutant enzyme
fluoride
-
reversible inhibition, binds to the active site, binding structure, overview
fluoride
-
-
free divalent cations
-
-
-
fructose-1,6-bisphosphate
-
-
GDP
-
19% inhibition at 0.1 mM
glutathione
-
oxidized
GMP
-
18% inhibition at 0.1 mM
GSH
activates up to 4 mM, and inhibits at higher concentrations
Guanidine HCl
-
-
Guanidine nucleotides
-
-
-
Hg2+
-
-
Hg2+
-
-
hydroxymethylbisphosphonate
-
competitive with diphosphate
Imidodiphosphate
-
-
Imidodiphosphate
-
-
Imidodiphosphate
slight inhibition
Imidodiphosphate
Herpetomonas sp.
-
-
Imidodiphosphate
-
when diphosphate concentration in the medium is adjusted to 0.05 mM, the enzyme is totally inhibited by 0.5 mM imidodiphosphate, the same concentration of imidodiphosphate only decreases the enzyme activity by 70% and 50% when diphosphate concentration in the medium is increased to 0.15 mM and 0.3 mM, respectively
imidodiphosphoric acid
a nonhydrolyzable PPi analogue, inhibits by 50% at 2 mM
iodoacetamide
-
-
iodoacetate
-
-
iodoacetate
-
-
KF
Methanothermobacter thermautotrophicum
-
50% at 0.9 mM
KF
-
90% at 0.5 mM
L-Malate
-
allosteric mechanism
Maleic anhydride
-
-
methylene diphosphate-Mg complex
-
competitive inhibition of MgPPi hydrolysis, binds at the active site
Methylenediphosphonate
-
competes with ATP and diphosphate for binding at the allosteric regulatory site involving Lys112
Mg2+
-
-
Mn2+
Aranda Christine
-
-
Mn2+
-
-
Mn2+
-
-
Mn2+
-
less effective than Zn2+
Mn2+
Methanothermobacter thermautotrophicum
-
60% inhibition at 1 mM Mn2+: 24 mM Mg2+
Mn2+
can substitute for Mg2+ at concentrations up to 0.5 mM, inhibitory above
Mn2+
-
activates at up to 1 mM, inhibits at higher concentrations, overview
N,N'-dicyclohexyl-carbodiimide
-
-
N-ethylmaleimide
-
-
N-ethylmaleimide
-
-
N-ethylmaleimide
-
-
N-ethylmaleimide
-
-
N-ethylmaleimide
-
-
N-ethylmaleimide
-
-
N-ethylmaleimide
-
-
N-ethylmaleimide
inhibits 38% of PPase activity at 37.5 mM
N-Phenylmaleimide
-
-
Na+
Herpetomonas sp.
-
inhibits diphosphate-dependent H+-uptake
NaF
-
-
NaF
Methanothermobacter thermautotrophicum
-
-
NaF
inhibits 46% and 91.4% of the activity at 0.04 mM and 0.5 mM, respectively
p-chloromercuribenzenesulfonic acid
-
-
p-chloromercuribenzoate
-
-
p-chloromercuribenzoate
-
-
p-chloromercuribenzoate
-
-
p-Chloromercuriphenyl sulfonate
-
50% inhibition of hydrolysis of diphosphate at 25 M
Phenylglyoxal
-
-
Phenylglyoxal
-
the inhibitory effect of phenylglyoxal is higher at 56C than at room temperature. With 5 mM phenylglyoxal almost complete inhibition can be observed after 15 min incubation at 56C
phenylmercuric acetate
-
-
phenylmethanesulfonyl fluoride
-
-
Phosphonates
-
-
Phosphonates
-
-
risedronate
-
IC50: 0.123 mM
risedronate
-
IC50: 0.002 mM
risedronate
-
IC50: 0.123 mM
Salts
-
neutral salts
-
SDS
SDS acts as a mixed-type reversible inhibitor of PPase, PPase can be fully inactivated at SDS concentration of 2 mM
Sodium cholate
-
-
Sodium fluoride
-
-
Succinic anhydride
-
-
Triton X-100
-
-
UDP
-
35% inhibition at 0.1 mM
Zn2+
-
-
Zn2+
-
-
Zn2+
-
-
Zn2+
-
-
Zn2+
-
inhibition caused at a separate site rather than as Zn-diphosphate substrate
Zn2+
-
less effective then Co2+
Zn2+
can substitute for Mg2+ at concentrations up to 0.5 mM, inhibitory above
Zn2+
-
activates at up to 1 mM, inhibits at higher concentrations, overview
additional information
-
insensitive to KF
-
additional information
-
poor inhibition by adenosine and UTP, no inhibition by cytidine, guanosine, uridine, CMP, CTP, GTP, cGMP, and UMP
-
additional information
-
the enzyme is inhibited by phosphorylation
-
additional information
-
no effect on gene expression by gibberellic acid
-
additional information
-
not inhibited by K+
-
additional information
-
the enzyme is not inhibited by Na+
-
additional information
-
addition of EDTA up to 0.5 mM to the assay mixture does not result in any change in the PPase activity
-
additional information
not inhibited by nucleotides or its end product phosphate: neither addition of 0.75 mM AMP or 0.005 mM ADP nor addition of up to 1.5 mM phosphate led to a reduced reaction rate
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2,4-Dinitrophenol
-
2,4-dinitrophenol increases the expression of HVP1, treatment with abscisic acid and 2,4-dinitrophenol increases Na+/H+ antiport activity and proton translocating activities by H+-PPase and H+-ATPase in tonoplast vesicles, and treatment with abscisic acid also increases the amount of V-PPase protein of tonoplast vesicles, overview
abscisic acid
-
abscisic acid markedly induces the expression of HVP1 and slightly increased the expression of HVP10, treatment with abscisic acid and 2,4-dinitrophenol increases Na+/H+ antiport activity and proton translocating activities by H+-PPase and H+-ATPase in tonoplast vesicles, and treatment with abscisic acid also increases the amount of V-PPase protein of tonoplast vesicles, overview
ATP
-
1.6fold activation at 0.1 mM
ATP
-
ATP activates hydrolysis of MgPPi by E-PPase, molecular docking and kinetic analysis involving Lys112 and Lys115, activation mechanism, and regulatory function of ATP, modelling, overview
diphosphate
diphosphate binds Mg2+ to form a true substrate that activates the enzyme
dithiothreitol
-
EDTA
-
89% activation at 0.9 mM, complete inhibition at 5 mM
gibberellic acid
-
phytohormone gibberellic acid increases V-PPase expression and activity by 20%
GSH
activates up to 4 mM, and inhibits at higher concentrations
KCl
-
3.5fold increase at 50 mM
magnesium methylenediphosphonate
-
a non-hydrolyzable analogue, the enzyme contains an extra binding site for the substrate magnesium diphosphate or its non-hydrolyzable analogue magnesium methylenediphosphonate, binding of substrate at the effector site of pyrophosphatase increases the rate of its hydrolysis at the active site, overview
methylene diphosphate
-
noncompetitive activation of magnesium diphosphate hydrolysis
NaBH4
activates at above 12 mM
methylenebisphosphonate
-
activates the hexameric but not the dimeric form of the enzyme at pH 6
additional information
-
insensitive to stimulation with K+
-
additional information
-
no activation with NaCl at 50 mM
-
additional information
-
phytohormones indole acetic acid and 6-benzyladenine increase V-PPase expression, but not the enzyme activity
-
additional information
vpp2 expression is slightly cold stress inducible; VVPP1 is highly cold stress inducible
-
additional information
-
enzyme is stimulated by presence of membrane lipids from Sulfolobus acidocaldarius
-
additional information
-
no activation by ADP and AMP
-
additional information
-
HVP1 transcripts also increase 5 h after treatment with another synthetic auxin, 1-naphthaleneacetic acid, and native auxin, 3-indoleacetic acid, while the level of HVP10 transcript does not increase after treatment with the two auxins, no effect on gene expression by gibberellic acid, salt stress increases the levels of HVP and HVP10 transcripts in the roots of barley seedlings, osmotic stress also increases the levels of HVP1 transcripts in the roots
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.189
ATP
-
pH 3.0, 55C
0.237
ATP
-
pH 3.0, 55C
0.19
Ca-diphosphate
-
-
-
0.29
Co-diphosphate
-
-
-
0.0011
diphosphate
-
-
0.0016
diphosphate
-
pH 7.2, E20D
0.0016
diphosphate
-
pH 6.5, wild type, hydrolysis of diphosphate
0.0018
diphosphate
-
pH 7.2, D97E, hydrolysis of diphosphate
0.0024
diphosphate
-
pH 8, D97E, hydrolysis of diphosphate
0.0024
diphosphate
-
pH 7.5, 25C, recombinant PPase1, in presence of Mg2+
0.0026
diphosphate
-
in the presence of 5 mM Mg2+, in 50 mM Tris-HCl, at pH 9.0 and 25C
0.0027
diphosphate
-
pH 7.5, 25C, mutant K112Q/K148Q
0.0028
diphosphate
native enzyme
0.0028
diphosphate
-
in the presence of 0.005 mM Mn2+, in 50 mM HEPES-NaOH, at pH 7.5 and 25C
0.0029
diphosphate
-
0.003
diphosphate
-
0.003
diphosphate
recombinant enzyme
0.0032
diphosphate
-
pH 7.5, 25C, wild-type enzyme and mutant K112Q/K115A
0.0034
diphosphate
-
pH 8, wild type, hydrolysis of diphosphate
0.0035
diphosphate
-
pH 7.2, wild type, hydrolysis of diphosphate
0.004
diphosphate
-
in the presence of 2 mM Mg2+, in 50 mM HEPES-NaOH,at pH 7.5 and 25C
0.0045
diphosphate
-
pH 7.5, 25C, mutant K112Q
0.005
diphosphate
-
-
0.005
diphosphate
-
-
0.0053
diphosphate
-
pH 7.5, 25C, trimeric mutant K112Q
0.0054
diphosphate
-
pH 7.0, 75C
0.0065
diphosphate
-
in the presence of Mg2+, at 25C, pH not specified in the publication
0.007
diphosphate
-
in the presence of 10 mM Mg2+, in 50 mM Mes-NaOH, at pH 6.5 and 25C
0.007
diphosphate
-
pH 6.2, 56C
0.008
diphosphate
-
pH 8.0, 37C, mutant Y230A
0.01
diphosphate
-
-
0.0143
diphosphate
-
pH 8.0, 90C
0.015
diphosphate
-
-
0.015
diphosphate
-
pH 7.8, 30C
0.016
diphosphate
-
pH 8.0, 37C, mutant G231A
0.0188
diphosphate
-
pH and temperature not specified in the publication
0.019
diphosphate
in the presence of Mg2+, pH 7.5, 25C
0.022
diphosphate
-
pH 8.0, 37C, mutant R242A
0.0274
diphosphate
-
-
0.034
diphosphate
-
pH 7.5, 25C, recombinant PPase2, in presence of Mn2+
0.035
diphosphate
-
-
0.035
diphosphate
-
pH 8.0, 37C, mutant L232A
0.0388
diphosphate
pH 8.0, 37C
0.039
diphosphate
pH 7.5, in the presence of Ca2+
0.041
diphosphate
recombinant mutant I260D, pH 9.0, 25C
0.047
diphosphate
-
presence of MgSO4
0.054
diphosphate
-
pH 8.0, 37C, mutant E225A
0.054
diphosphate
recombinant mutants I260V and I260E, pH 9.0, 25C
0.055
diphosphate
recombinant mutant I259V, pH 9.0, 25C
0.057
diphosphate
-
isoform 1
0.059
diphosphate
pH 7.5, 25C, isozyme PPa4 in a complex with Mg2+
0.06
diphosphate
-
Mg2+ at 5 mM, enzyme from astroblasts
0.06
diphosphate
pH 7.2, 25C, wild-type enzyme
0.062
diphosphate
pH 9.0, 25C, 5 mM Mg2+, wild-type enzyme
0.062
diphosphate
recombinant wild-type enzyme, pH 9.0, 25C
0.068
diphosphate
-
pH 8.0, 37C, mutant G229A
0.069
diphosphate
pH 7.5, 25C, isozyme PPa1 in a complex with Mg2+
0.07
diphosphate
-
Mg2+ at 5 mM, enzyme from neuroblasts
0.07
diphosphate
-
pH 8.0, 37C, mutant G234A
0.07
diphosphate
pH 9.0, 25C, 5 mM Mg2+, mutant G190W
0.072
diphosphate
-
isoform 2
0.074
diphosphate
-
pH 8.0, 37C, mutant G233A
0.081
diphosphate
pH 9.0, 25C, 5 mM Mg2+, mutant T191G
0.083
diphosphate
pH 8.0, 37C, recombinant wild-type enzyme
0.092
diphosphate
25C
0.098
diphosphate
pH 8.0, 37C, recombinant mutant C16S
0.099
diphosphate
-
pH 8.0, 37C, mutant F240A
0.1
diphosphate
-
-
0.105
diphosphate
-
pH 8.0, 37C, mutant S236A
0.112
diphosphate
-
pH 8.0, 37C, mutant M237A
0.113
diphosphate
pH 7.5, 60C, recombinat enzyme
0.117
diphosphate
recombinant protein, pH 7.5, 55C
0.123
diphosphate
pH 9.0, 25C, 5 mM Mg2+, mutant G190A
0.13
diphosphate
-
wild type hexamer, pH 7.5
0.14
diphosphate
-
-
0.14
diphosphate
-
pH 8.0, 37C, mutant I227A
0.146
diphosphate
-
pH 8.0, 37C, mutant T228A
0.148
diphosphate
-
pH 8.0, 37C, mutant G221A
0.154
diphosphate
-
pH 8.0, 37C, wild-type enzyme
0.16
diphosphate
Methanothermobacter thermautotrophicum
-
-
0.161
diphosphate
-
pH 3.0, 55C
0.163
diphosphate
recombinant mutant I259D, pH 9.0, 25C
0.173
diphosphate
pH 8.0, 37C, recombinant mutant Y140F
0.185
diphosphate
-
pH 8.0, 37C, mutant A226S
0.196
diphosphate
-
pH 8.0, 37C, mutant A238S
0.199
diphosphate
-
pH 8.0, 37C, mutant S235A
0.214
diphosphate
recombinant enzyme
0.221
diphosphate
-
pH 8.0, 37C, mutant L239A
0.248
diphosphate
recombinant mutant I259E, pH 9.0, 25C
0.25 - 1.67
diphosphate
-
varying Mg2+ and EDTA concentrations
0.27
diphosphate
pH 8.0, 37C, with Mn2+ as metal cofactor
0.305
diphosphate
-
pH 8.0, 37C, mutant F224A
0.318
diphosphate
-
pH 8.0, 37C, mutant G222A
0.32
diphosphate
pH 7.5, 25C, recombinant wild-type BT2127
0.332
diphosphate
-
pH 8.0, 37C, mutant G241A
0.35
diphosphate
wild type enzyme, in 50 mM MOPS (pH 6.5), in the presence of Mg2+, at 80C
0.37
diphosphate
pH 7.5, in the presence of Mg2+
0.438
diphosphate
-
pH 8.0, 37C, mutant L223A
0.47
diphosphate
-
P69A mutant enzyme, pH 8.0, 37C; wild type enzyme, pH 8.0, 37C
0.48
diphosphate
wild type enzyme, in 50 mM MOPS (pH 6.5), in the presence of Ni2+, at 80C
0.49
diphosphate
wild type enzyme, in 50 mM MOPS (pH 6.5), in the presence of Co2+, at 80C
0.55
diphosphate
-
pH 3
0.55
diphosphate
-
P146A mutant enzyme, pH 8.0, 37C
0.6
diphosphate
-
P39A mutant enzyme, pH 8.0, 37C
0.64
diphosphate
-
P116A mutant enzyme, pH 8.0, 37C
0.768
diphosphate
-
pH 8.6, 37C
0.8
diphosphate
-
wild type dimer, pH 7.5
0.82
diphosphate
-
P14A mutant enzyme, pH 8.0, 37C
0.88
diphosphate
-
P100A mutant enzyme, pH 8.0, 37C
0.96
diphosphate
-
P59A mutant enzyme, pH 8.0, 37C
1
diphosphate
-
P104A mutant enzyme, pH 8.0, 37C; P43A mutant enzyme, pH 8.0, 37C
1.2
diphosphate
-
pH 6
1.25
diphosphate
-
-
1.3
diphosphate
-
E145Q hexamer, pH 7.5
1.32
diphosphate
-
pH 6.9
1.8
diphosphate
-
E145Q dimer, pH 7.5
1.98
diphosphate
-
pH 7.0, 50C, in presence of 5 mM Mg2+
0.12
Imidodiphosphate
-
-
0.012
imidodiphosphoric acid
pH 7.2, 25C, wild-type enzyme
4
K+
-
-
0.00045
Mg-diphosphate
-
pH 7.2, 1 mM Mg2+, 0.1 M TES/KOH
0.00053
Mg-diphosphate
-
pH 7.2, 1 mM Mg2+, 0.1 M MOPS/KOH
0.00116
Mg-diphosphate
-
pH 7.2, 1 mM Mg2+, 0.08 M monoethalamine/HCl + 0.02 M Tes/KOH
0.00133
Mg-diphosphate
-
pH 7.2, 1 mM Mg2+, 0.1 M Tris-HCl + 0.05 M KCl
0.00144
Mg-diphosphate
-
pH 7.2, 1 mM Mg2+, 0.08 M Tes/Tris + 0.02 M Tes/KOH
0.00168
Mg-diphosphate
-
pH 7.2, 1 mM Mg2+, 0.2 M Tes/Tris
0.00196
Mg-diphosphate
-
pH 7.2, 1 mM Mg2+, 0.15 M Tris-HCl or 0.08 M 2-amino-2-methyl-1,3-propanediol/HCl + 0.02 M Tes/KOH
0.002
Mg-diphosphate
-
-
0.0023
Mg-diphosphate
-
pH 7.2, hexameric, H136Q enzyme
0.0027
Mg-diphosphate
-
pH 7.2, H140Q enzyme, hexameric
0.0034
Mg-diphosphate
-
pH 8, wild type enzyme
0.0055
Mg-diphosphate
-
pH 7.2, 1 mM Mg2+, 0.08 M NH4Cl + 0.02 M TES/KOH
0.008
Mg-diphosphate
-
pH 8, hexameric, H136Q enzyme
0.016
Mg-diphosphate
-
-
0.09
Mg-diphosphate
-
-
0.13
Mg-diphosphate
-
-
0.198
Mg-diphosphate
-
pH 7.2, H136Q enzyme, trimeric
0.23
Mg-diphosphate
-
-
0.44
Mg-diphosphate
-
pH 8, H140Q enzyme, trimeric
4.2
Mg-diphosphate
-
pH 7.2, H140Q enzyme, trimeric
0.02 - 0.023
Mg2+
-
-
1.65
Mg2+
-
-
2.27
Mg2+
-
diphosphate at 1 mM, enzyme from astroblasts
3.15
Mg2+
-
diphosphate at 1 mM, enzyme from neuroblasts
4.9
Mg2+
Methanothermobacter thermautotrophicum
-
-
0.014
Polyphosphate
in the presence of Zn2+, pH 7.5, 25C
0.123
polyphosphate-n28
25C
-
1.153
Triphosphate
25C
0.373
tripolyphosphate
in the presence of Zn2+, pH 7.5, 25C
0.37
Mn-diphosphate
-
-
additional information
additional information
-
detailed kinetics of hexameric, trimeric enzyme, and enzyme mutants, overview, the active trimeric enzyme, formed under acidic conditions, does not obey Michaelis-Menten kinetics, overview
-
additional information
additional information
-
kinetics of wild-type and mutant enzymes
-
additional information
additional information
kinetics of wild-type and mutant enzymes
-
additional information
additional information
the structural orientation of Lys78 is very important for the kinetic properties of the enzyme
-
additional information
additional information
effects of cysteine, homocysteine, and NaBH4 on kinetics of wild-type and mutant C16S enzymes, overview
-
additional information
additional information
-
kinetic analysis of wild-type and mutant enzymes in presence of different nucleotides, overview
-
additional information
additional information
metal binding affinities and kinetics of wild-type and mutant enzymes, overview
-
additional information
additional information
-
kinetic analysis of wild-type and mutant enzymes, Mg2+ binding kinetics, overview
-
additional information
additional information
-
kinetic analysis of wild-type and mutant enzymes with different substrates, detailed overview
-
additional information
additional information
-
kinetic analysis of wild-type and mutant enzymes, Mg2+ binding kinetics, overview
-
additional information
additional information
ordered binding of free Mg2+ and of the Mg-diphosphate complex. Both isozymes show similar catalytic constants and affinities for the Mg-diphosphate complex, while differed in their affinity for free Mg2+, kinetics, overview
-
additional information
additional information
kinetics
-
additional information
additional information
wild-type and mutant BT2127 steady-state kinetics, overview
-
additional information
additional information
-
kinetics and thermodynamics, detailed overview
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.005
ATP
Saccharomyces cerevisiae
-
less than 0.005/sec, pH 7.2, 25C, in the presence of Mg2+
0.16
diphosphate
Thermococcus onnurineus
B6YSF3
wild type enzyme, in 50 mM MOPS (pH 6.5), in the presence of Mg2+, at 80C
0.21
diphosphate
Thermococcus onnurineus
B6YSF3
wild type enzyme, in 50 mM MOPS (pH 6.5), in the presence of Ni2+, at 80C
0.22
diphosphate
Thermococcus onnurineus
B6YSF3
wild type enzyme, in 50 mM MOPS (pH 6.5), in the presence of Co2+, at 80C
0.34
diphosphate
Escherichia coli
-
pH 7.2, D97E, resynthesis of diphosphate
0.67
diphosphate
Escherichia coli
-
pH 8, D97E, resynthesis of diphosphate
1.3
diphosphate
Bacillus sp. PS3
-
P104A mutant enzyme, pH 8.0, 37C
1.64
diphosphate
Moorella thermoacetica
-
pH 7.2, 25C
2.1
diphosphate
Thermococcus onnurineus
-
pH and temperature not specified in the publication
2.8
diphosphate
Bacillus sp. PS3
-
P100A mutant enzyme, pH 8.0, 37C
3.6
diphosphate
Bacteroides thetaiotaomicron
Q8A5V9
pH 7.5, 25C, recombinant wild-type BT2127
7.7
diphosphate
Escherichia coli
-
E145Q mutant dimer, pH 7.5
11
diphosphate
Streptococcus gordonii
P95765
recombinant mutant I259D, pH 9.0, 25C
11.9
diphosphate
Arabidopsis thaliana
Q9LXC9
pH 7.5, 25C, isozyme PPa4
12
diphosphate
Escherichia coli
-
pH 7.2, D97E, hydrolysis of diphosphate
12.1
diphosphate
Arabidopsis thaliana
Q9LXC9
pH 7.5, 25C, isozyme PPa1
19
diphosphate
Bacillus sp. PS3
-
P146A mutant enzyme, pH 8.0, 37C
38
diphosphate
Vibrio cholerae
-
in the presence of 10 mM Mg2+, in 50 mM Mes-NaOH, at pH 6.5 and 25C
48
diphosphate
Streptococcus gordonii
P95765
recombinant mutant I259E, pH 9.0, 25C
51
diphosphate
Vibrio cholerae
-
in the presence of 0.005 mM Mn2+, in 50 mM HEPES-NaOH, at pH 7.5 and 25C
55
diphosphate
Escherichia coli
-
pH 8, D97E, hydrolysis of diphosphate
56
diphosphate
Trypanosoma brucei
Q7Z029
in the presence of Zn2+, pH 7.5, 25C
74.3
diphosphate
Bacillus sp. PS3
-
P14A mutant enzyme, pH 8.0, 37C
76
diphosphate
Escherichia coli
-
wild type dimer, pH 7.5
78.4
diphosphate
Helicobacter pylori
P56153
pH 8.0, 37C, recombinant mutant Y140F
83
diphosphate
Escherichia coli
-
E145Q mutant hexamer, pH 7.5
83
diphosphate
Escherichia coli
-
pH 7.5, 25C, hexameric mutant E145Q, 5 mM Mg2+
86
diphosphate
Escherichia coli
-
pH 6.5, wild type, hydrolysis of diphosphate
93
diphosphate
Vibrio cholerae
-
in the presence of 2 mM Mg2+, in 50 mM HEPES-NaOH, at pH 7.5 and 25C
104
diphosphate
Escherichia coli
-
pH 6.5, wild type, resynthesis of diphosphate
109
diphosphate
Vibrio cholerae
-
pH 7.5, 25C, recombinant PPase1, in presence of Mg2+
114
diphosphate
Escherichia coli
-
pH 8, wild type, resynthesis of diphosphate
116
diphosphate
Escherichia coli
-
pH 7.2, wild type, resynthesis of diphosphate
125
diphosphate
Leishmania amazonensis
Q7Z031
25C
155
diphosphate
Escherichia coli
-
pH 7.2, wild type, hydrolysis of diphosphate
173.1
diphosphate
Helicobacter pylori
P56153
pH 8.0, 37C, recombinant mutant C16S
177
diphosphate
Vibrio cholerae
-
in the presence of 5 mM Mg2+, in 50 mM Tris-HCl, at pH 9.0 and 25C
187
diphosphate
Escherichia coli
-
pH 8, wild type, hydrolysis of diphosphate
236.7
diphosphate
Bacillus sp. PS3
-
P116A mutant enzyme, pH 8.0, 37C
260
diphosphate
Saccharomyces cerevisiae
-
pH 7.2, 25C, in the presence of Mg2+
288.7
diphosphate
Bacillus sp. PS3
-
P43A mutant enzyme, pH 8.0, 37C
343.9
diphosphate
Helicobacter pylori
P56153
pH 8.0, 37C, recombinant wild-type enzyme
369
diphosphate
Leishmania major
Q6UQ31
pH 7.5, in the presence of Mg2+
385
diphosphate
Trypanosoma brucei
Q7Z029
in the presence of Mg2+, pH 7.5, 25C
390
diphosphate
Escherichia coli
-
wild type hexamer, pH 7.5
390
diphosphate
Escherichia coli
-
pH 7.5, 25C, wild-type enzyme, 5 mM Mg2+
413.3
diphosphate
Bacillus sp. PS3
-
P59A mutant enzyme, pH 8.0, 37C
560
diphosphate
Streptococcus gordonii
P95765
recombinant mutant I260D, pH 9.0, 25C
570
diphosphate
Streptococcus gordonii
P95765
recombinant mutant I260E, pH 9.0, 25C
638
diphosphate
Ascaris suum
Q86M43
recombinant protein, pH 7.5, 55C
744
diphosphate
Pyrococcus horikoshii
O59570
pH 7.5, 60C, recombinat enzyme
744.3
diphosphate
Bacillus sp. PS3
-
P69A mutant enzyme, pH 8.0, 37C
800
diphosphate
Synechocystis sp.
P80507
recombinant enzyme
817
diphosphate
Bacillus sp. PS3
-
wild type enzyme, pH 8.0, 37C
850
diphosphate
Anabaena sp.
P80562
-
850
diphosphate
Pseudanabaena sp.
P58733
-
916
diphosphate
Synechocystis sp.
P80507
native enzyme
1098
diphosphate
Bacillus sp. PS3
-
P39A mutant enzyme, pH 8.0, 37C
1600
diphosphate
Vibrio cholerae
-
pH 7.5, 25C, recombinant PPase2, in presence of Mn2+
1700
diphosphate
Sulfolobus acidocaldarius
-
pH 7.0, 75C
2130
diphosphate
Streptococcus gordonii
P95765
pH 9.0, 25C, 5 mM Mg2+, mutant T191G
2200
diphosphate
Thermoplasma acidophilum
-
pH 6.2, 56C
3270
diphosphate
Streptococcus gordonii
P95765
pH 9.0, 25C, 5 mM Mg2+, mutant G190A
3436
diphosphate
Pyrococcus horikoshii
-
pH 8.0, 90C
3460
diphosphate
Streptococcus gordonii
P95765
pH 9.0, 25C, 5 mM Mg2+, mutant G190W
3693
diphosphate
Leishmania major
Q6UQ31
pH 7.5, in the presence of Ca2+
4420
diphosphate
Streptococcus gordonii
P95765
recombinant mutant I259V, pH 9.0, 25C
6290
diphosphate
Streptococcus gordonii
P95765
pH 9.0, 25C, 5 mM Mg2+, wild-type enzyme
6290
diphosphate
Streptococcus gordonii
P95765
recombinant wild-type enzyme, pH 9.0, 25C
6480
diphosphate
Streptococcus gordonii
P95765
recombinant mutant I260V, pH 9.0, 25C
0.014
imidodiphosphoric acid
Bacillus subtilis
P37487
pH 7.2, 25C, wild-type enzyme
3.5
Polyphosphate
Trypanosoma brucei
Q7Z029
in the presence of Zn2+, pH 7.5, 25C
8
polyphosphate-n28
Leishmania amazonensis
Q7Z031
25C
-
131
Triphosphate
Leishmania amazonensis
Q7Z031
25C
0.05
tripolyphosphate
Saccharomyces cerevisiae
-
pH 7.2, 25C, in the presence of Mg2+
52
tripolyphosphate
Trypanosoma brucei
Q7Z029
in the presence of Zn2+, pH 7.5, 25C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0026
diphosphate
Vibrio cholerae
-
in the presence of Mg2+, at pH 7.5 and 25C
17
0.44
diphosphate
Thermococcus onnurineus
B6YSF3
wild type enzyme, in 50 mM MOPS (pH 6.5), in the presence of Ni2+, at 80C
17
0.45
diphosphate
Thermococcus onnurineus
B6YSF3
wild type enzyme, in 50 mM MOPS (pH 6.5), in the presence of Co2+, at 80C
17
0.46
diphosphate
Thermococcus onnurineus
B6YSF3
wild type enzyme, in 50 mM MOPS (pH 6.5), in the presence of Mg2+, at 80C
17
67.5
diphosphate
Streptococcus gordonii
P95765
recombinant mutant I259D, pH 9.0, 25C
17
89
diphosphate
Bacteroides thetaiotaomicron
Q8A5V9
pH 7.5, 25C, recombinant wild-type BT2127
17
193.5
diphosphate
Streptococcus gordonii
P95765
recombinant mutant I259E, pH 9.0, 25C
17
10560
diphosphate
Streptococcus gordonii
P95765
recombinant mutant I260E, pH 9.0, 25C
17
13660
diphosphate
Streptococcus gordonii
P95765
recombinant mutant I260D, pH 9.0, 25C
17
80360
diphosphate
Streptococcus gordonii
P95765
recombinant mutant I259V, pH 9.0, 25C
17
101500
diphosphate
Streptococcus gordonii
P95765
recombinant wild-type enzyme, pH 9.0, 25C
17
120000
diphosphate
Streptococcus gordonii
P95765
recombinant mutant I260V, pH 9.0, 25C
17
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.014
Ca2+
hydrolysis of diphosphate, pH 7.5, 25C, no inhibition of tripolyphosphate and polyphosphate hydrolysis
0.0028
fluoride
-
pH 7.4, 25C, with 0.05 mM Mn2+
0.012
fluoride
pH 7.2, 25C, wild-type enzyme, kinetics
0.0358
fluoride
-
pH 7.4, 25C, with 5 mM Mn2+
0.033
hydroxymethylbisphosphonate
-
pH 7.2
0.025
p-Chloromercuriphenyl sulfonate
-
-
0.33
Methylenediphosphonate
-
pH 7.5, 25C, wild-type mutant
additional information
additional information
-
inhibition kinetics
-
0.42
additional information
-
pH 7.2, 37C, fluoride inhibition kinetics
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0009
aminomethylenediphosphonate
Toxoplasma gondii
Q9BK08
IC50: 0.0009 mM
1 - 2
F-
Avena sativa
-
IC50: 1-2 mM
0.1
fluoride
Pyrococcus horikoshii
O59570
potent inhibition, IC50: 0.1 mM
17.2
GSH
Helicobacter pylori
P56153
pH 8.0, 37C, recombinant wild-type enzyme
0.002
risedronate
Toxoplasma gondii
-
IC50: 0.002 mM
0.123
risedronate
Plasmodium falciparum, Trypanosoma cruzi
-
IC50: 0.123 mM
1.11
SDS
Thermus thermophilus
P38576
at 25C, pH not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.00705
purified recombinant wild-type enzyme, pH 8.0, 37C
0.5
-
liver enzyme in absence of NaCl
1.13
purified enzyme, pH 8.0, 80C
1.3
-
isolated vesicles, pH 7.8, 30C
2.1
-
diphosphate
2.52
-
purified native enzyme
2.7
Aranda Christine
-
-
2.7
-
isoform 1
7.75
-
lung stage L3 cultured for 5 days
11.66
-
purified enzyme, pH 8.6, 37C
13
-
crystallized enzyme
15
-
hexameric mutant E145Q
30.8
-
pH 3.0, 55C
79.75
-
-
82
-
0.0025 mM substrate Mg-diphosphate, in absence of magnesium methylenediphosphonate
101.6
-
pH 8.0, 90C
142
-
0.0025 mM substrate Mg-diphosphate, in presence of 0.0075 mM magnesium methylenediphosphonate
154.3
purified enzyme, pH 7.5
157
pH 8.0, 37C, with Mg2+ as metal cofactor
240
-
purified native enzyme
280
-
wild-type enzyme
360
-
0.015 mM substrate Mg-diphosphate, in presence or absence of 0.0075 mM magnesium methylenediphosphonate
415
-
purified native enzyme
592
-
-
600 - 700
-
-
617
-
56C; pH 6.5, 56C
650
-
pH 3.3, 70C
672.2
-
pH 7.0, 70C
726
pH 8.0, 37C, with Mn2+ as metal cofactor
860
-
pH 7.0, 75C
937
recombinant protein, pH 7.5, 55C
940
-
purified recombinant His-tagged enzyme
1200
-
pH 6.2, 56C
1233
Methanothermobacter thermautotrophicum
-
-
1570
recombinant enzyme
1986
-
-
2170
-
purified p26.1b
2320
-
purified p26.1a
additional information
-
-
additional information
-
the activity of PPase2 measured in the presence of Mn2+ is greater than that of PPase1 measured in the presence of Mg2+
additional information
-
additional information
-
native activity at different developmental stages, highest activity at lung stage L3 cultured for 5 days, overview
additional information
-
activity of H+-PPase measured as K+/Na+-dependent diphosphate hydrolysis activity, phosphate uptake of vacuoles isolated from high phosphate and low phosphate cells, activity profiles, cellular phosphate content, overview
additional information
-
0.0185 mMol/g of tissue after 2 days of seed bud development
additional information
-
tissue-specific activities in absence and presence of salts, overview
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5
-
microsomal enzyme
6
-
pH optimum in absence of Mg2+
6
recombinant enzyme
6 - 7
-
-
6.1
-
Mn2+ activated enzyme
6.1 - 6.2
-
-
6.2
-
in the presence of Co2+
6.5
in the presence of Zn2+
6.5 - 6.7
Herpetomonas sp.
-
-
6.5 - 7.5
-
assay at
6.8
DQ978330
assay at
7
-
mitochondrial enzyme
7
-
activity optimum at pH around 7.0
7 - 8
-
-
7.2
-
assay at
7.2 - 7.5
-
assay at
7.2 - 8.6
-
broad optimum, the pH optimum shifts with binding of Mg2+, overview
7.3
-
-
7.4
-
assay at, the pH heavily influences the metal binding of the enzyme, hydrolysis
7.4 - 8.1
-
pH optima of mutant enzymes, overview
7.5
-
-
7.5
in the presence of Mg2+
7.5
-
assay at
7.5 - 9
-
-
7.6
-
narrow pH spectrum of iPPase
7.7
Methanothermobacter thermautotrophicum
-
60C
8
-
hydrolysis of diphosphate
8
-
in the presence of Mg2+ or Mn2+
8
-
pH optimum of the wild-type enzyme
8
-
assay at, synthesis
8 - 10
-
in the presence of Mg2+
8.2 - 8.5
-
-
8.3 - 8.8
-
-
8.4
-
assay at
8.5
-
-
8.5
-
isoform 2, 6 mM MgCl2, 1mM diphosphate, isoform 1 in presence of 10 mM MgCl2
8.6
-
pH optimum in presence of Mg2+
9
Aranda Christine
-
in the presence of MgCl
9
-
isoform 1, 6 mM MgCl2, 1mM diphosphate
9
-
in the presence of 5 mM Mg2+
9.8
-
in the presence of Mn2+
additional information
-
pH-dependence of wild-type and mutant activity, overview
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2.5 - 4.5
-
at pH 2.5 and 4.5, about 50% of the maximal activity is observed
5 - 8
-
Mn2+ activated enzyme
5.5 - 10
-
-
5.5 - 10
-
no activity below 5.5, about 75% activity at pH 10
5.5 - 10
-
no activity below 5.5, about 75% activity at pH 10
5.9 - 9.5
-
4.5% and 72.2% relative activity at pH 5.9 and 9.5 respectively
6 - 12
-
-
6 - 7.2
Herpetomonas sp.
-
drastic loss of activity above pH 7.2
6 - 9
-
about 8% and 40% relative activity at pH 6 and 9 respectively, 5 mM diphosphate
6 - 9
-
about 45% and 85% relative activity at pH 6 and 9 respectively, 5 mM diphosphate, 3.2 mM Mg2+
6 - 9.7
-
-
7 - 11
-
20% relative activity at pH 7 and 11
7.5 - 10
at conditions below pH 7.5 and above pH 10.0 activity decreases considerably
8.5 - 11.5
-
pH 8.5: about 50% of maximal activity, pH 11.5: about 55% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
22
assay at room temperature; assay at room temperature
25
-
assay at
25
-
assay at
25
-
assay at
25
Herpetomonas sp.
-
assay at
25
-
assay at
37
-
assay at
37
DQ978330
assay at
70
Methanothermobacter thermautotrophicum
-
-
85
-
growth optimum for organism and highest activity
additional information
-
optimal growth at 88C
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 65
-
-
25 - 90
activity range, high activity at 60-75C
30 - 60
-
-
30 - 65
-
-
37 - 95
-
active at
70 - 100
-
70C: about 70% of maximal activity, 100C: about 80% of maximal activity
70 - 100
-
70C: about 50% of maximal activity, 100C: about 50% of maximal activity
80
-
70% of maximum activity, rapid decline in activity above
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.7
column chromatofocusing
4.7
calculated from amino acid sequence
5.1
-
isoelectric focusing
5.2
sequence calculation
5.26
isozyme PPa4
5.73
isozyme PPa1
6
calculated from predicted amino acid sequence
6
calculated from predicted amino acid sequence
6.03
-
p26.1b, sequence calculation
6.11
-
p26.1a, sequence calculation
7.1
calculated from predicted amino acid sequence and detected in isoelectric focusing