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Literature summary extracted from

  • Ramponi, G.
    1,3-Diphosphoglycerate phosphatase (1975), Methods Enzymol., 42C, 409-426.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.6.1.7
-
Oryctolagus cuniculus

General Stability

EC Number General Stability Organism
3.6.1.7 brain enzyme, unusually stable to prolonged storage, lyophilization and to acid treatment Bos taurus
3.6.1.7 enzyme is very stable Gallus gallus
3.6.1.7 enzyme is very stable Sus scrofa
3.6.1.7 enzyme is very stable Bos taurus
3.6.1.7 enzyme is very stable Oryctolagus cuniculus
3.6.1.7 enzyme is very stable Equus caballus
3.6.1.7 liver enzyme, stable to acid treatment Equus caballus
3.6.1.7 muscle enzyme, stable to various denaturating agents Equus caballus

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.6.1.7 2,3-diphosphoglycerate
-
Bos taurus
3.6.1.7 2,3-diphosphoglycerate
-
Homo sapiens
3.6.1.7 2,3-diphosphoglycerate heart enzyme, 2 mM: 12% inhibition, substrate: 1,3-diphosphoglycerate Sus scrofa
3.6.1.7 3-phosphoglycerate
-
Bos taurus
3.6.1.7 3-phosphoglycerate heart enzyme, 5 mM: 8% inhibition, substrate: 1,3-diphosphoglycerate Sus scrofa
3.6.1.7 ATP noncompetitive inhibition, Ki: 0.57 mM Equus caballus
3.6.1.7 ATP erythrocyte enzyme, competitive inhibition, Ki: 4.4 mM Homo sapiens
3.6.1.7 ATP heart enzyme, 5 mM: 11% inhibition, substrate: 1,3-diphosphoglycerate Sus scrofa
3.6.1.7 benzyl phosphate moderate competitive inhibition, Ki: 11 mM Equus caballus
3.6.1.7 Carbamoyl phosphate erythrocyte enzyme, competitive inhibition, Ki: 6.9 mM Homo sapiens
3.6.1.7 fructose 1,6-diphosphate noncompetitive inhibition, Ki: 3.2 mM Equus caballus
3.6.1.7 iodoacetate brain enzyme, 4 mM: no inhibition Bos taurus
3.6.1.7 iodoacetate heart enzyme, 10 mM: very low, less than 5%, inhibition Sus scrofa
3.6.1.7 methyl phosphate moderate competitive inhibition, Ki: 3.5 mM Equus caballus
3.6.1.7 additional information brain enzyme, no inhibition by 0.04 mM HgCl2 and 4 mM iodoacetate Bos taurus
3.6.1.7 additional information no inhibition by adenosine monophosphate, phosphoethanolamine and alpha-glycerophosphate Equus caballus
3.6.1.7 additional information
-
Gallus gallus
3.6.1.7 additional information heart enzyme, no inhibition by 2.0 mM HgCl2 Sus scrofa
3.6.1.7 Orotic acid liver enzyme, noncompetitive inhibition Equus caballus
3.6.1.7 p-chloromercuribenzoate heart enzyme, 1 mM: very low, less than 5%, inhibition Sus scrofa
3.6.1.7 phosphate
-
Bos taurus
3.6.1.7 phosphate phosphate: high competitive inhibition, mechanism of inhibition Equus caballus
3.6.1.7 phosphate eryhrocyte enzyme, competitive inhibition, Ki: 3.4 mM Homo sapiens
3.6.1.7 phosphate heart enzyme, 5 mM: 37% inhibition, substrate: 1,3-diphosphoglycerate; heart enzyme, competitive inhibition Sus scrofa
3.6.1.7 Phosphorylated compounds
-
Equus caballus
3.6.1.7 pyridoxal 5'-phosphate muscle enzyme, pH-dependent competitive, reversible inhibition, Ki: 0.32 mM Equus caballus
3.6.1.7 sulfate Si, heart enzyme, competitive inhibition Sus scrofa
3.6.1.7 Urea 8 M: 100% inhibition Bos taurus
3.6.1.7 Urea 8 M: 100% inhibition Homo sapiens

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.6.1.7 0.12
-
1,3-diphosphoglycerate erythrocyte enzyme Homo sapiens
3.6.1.7 1.6
-
1,3-diphosphoglycerate muscle Equus caballus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.6.1.7 KCl brain enzyme, 15 mM: activation, substrate: Tris salt of acetyl phosphate Bos taurus
3.6.1.7 MgCl2
-
Homo sapiens
3.6.1.7 MgCl2 brain enzyme, 5 mM: activation, substrate: Tris salt of acetyl phosphate Bos taurus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.6.1.7 8300
-
liver, gel filtration Equus caballus
3.6.1.7 9400
-
muscle, low speed sedimentation equilibrium, Archibald method, and gel filtration Equus caballus
3.6.1.7 11100
-
heart, gel filtration Sus scrofa
3.6.1.7 12000
-
-
Gallus gallus
3.6.1.7 12000
-
brain, gel filtration Bos taurus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.6.1.7 1,3-diphosphoglycerate + H2O Gallus gallus possible role in preventing the intracellular accumulation of 1,3-diphosphoglycerate by catalyzing the hydrolysis of this substrate to 3-phosphoglycerate 3-phosphoglycerate + phosphate
-
?
3.6.1.7 1,3-diphosphoglycerate + H2O Homo sapiens possible role in preventing the intracellular accumulation of 1,3-diphosphoglycerate by catalyzing the hydrolysis of this substrate to 3-phosphoglycerate 3-phosphoglycerate + phosphate
-
?
3.6.1.7 1,3-diphosphoglycerate + H2O Sus scrofa possible role in preventing the intracellular accumulation of 1,3-diphosphoglycerate by catalyzing the hydrolysis of this substrate to 3-phosphoglycerate 3-phosphoglycerate + phosphate
-
?
3.6.1.7 1,3-diphosphoglycerate + H2O Saccharomyces cerevisiae possible role in preventing the intracellular accumulation of 1,3-diphosphoglycerate by catalyzing the hydrolysis of this substrate to 3-phosphoglycerate 3-phosphoglycerate + phosphate
-
?
3.6.1.7 1,3-diphosphoglycerate + H2O Bos taurus possible role in preventing the intracellular accumulation of 1,3-diphosphoglycerate by catalyzing the hydrolysis of this substrate to 3-phosphoglycerate 3-phosphoglycerate + phosphate
-
?
3.6.1.7 1,3-diphosphoglycerate + H2O Oryctolagus cuniculus possible role in preventing the intracellular accumulation of 1,3-diphosphoglycerate by catalyzing the hydrolysis of this substrate to 3-phosphoglycerate 3-phosphoglycerate + phosphate
-
?
3.6.1.7 1,3-diphosphoglycerate + H2O Equus caballus possible role in preventing the intracellular accumulation of 1,3-diphosphoglycerate by catalyzing the hydrolysis of this substrate to 3-phosphoglycerate 3-phosphoglycerate + phosphate
-
?
3.6.1.7 1,3-diphosphoglycerate + H2O Gallus gallus 1,3-diphosphoglycerate can acylate histones, particularly the lysine-rich ones, 1,3-diphosphoglycerate phosphatase can prevent this acylation 3-phosphoglycerate + phosphate
-
?
3.6.1.7 1,3-diphosphoglycerate + H2O Homo sapiens 1,3-diphosphoglycerate can acylate histones, particularly the lysine-rich ones, 1,3-diphosphoglycerate phosphatase can prevent this acylation 3-phosphoglycerate + phosphate
-
?
3.6.1.7 1,3-diphosphoglycerate + H2O Sus scrofa 1,3-diphosphoglycerate can acylate histones, particularly the lysine-rich ones, 1,3-diphosphoglycerate phosphatase can prevent this acylation 3-phosphoglycerate + phosphate
-
?
3.6.1.7 1,3-diphosphoglycerate + H2O Saccharomyces cerevisiae 1,3-diphosphoglycerate can acylate histones, particularly the lysine-rich ones, 1,3-diphosphoglycerate phosphatase can prevent this acylation 3-phosphoglycerate + phosphate
-
?
3.6.1.7 1,3-diphosphoglycerate + H2O Bos taurus 1,3-diphosphoglycerate can acylate histones, particularly the lysine-rich ones, 1,3-diphosphoglycerate phosphatase can prevent this acylation 3-phosphoglycerate + phosphate
-
?
3.6.1.7 1,3-diphosphoglycerate + H2O Oryctolagus cuniculus 1,3-diphosphoglycerate can acylate histones, particularly the lysine-rich ones, 1,3-diphosphoglycerate phosphatase can prevent this acylation 3-phosphoglycerate + phosphate
-
?
3.6.1.7 1,3-diphosphoglycerate + H2O Equus caballus 1,3-diphosphoglycerate can acylate histones, particularly the lysine-rich ones, 1,3-diphosphoglycerate phosphatase can prevent this acylation 3-phosphoglycerate + phosphate
-
?
3.6.1.7 additional information Gallus gallus possible role in preventing the intracellular accumulation of 1,3-diphosphoglycerate by catalyzing the hydrolysis of this substrate to 3-phosphoglycerate ?
-
?
3.6.1.7 additional information Homo sapiens possible role in preventing the intracellular accumulation of 1,3-diphosphoglycerate by catalyzing the hydrolysis of this substrate to 3-phosphoglycerate ?
-
?
3.6.1.7 additional information Sus scrofa possible role in preventing the intracellular accumulation of 1,3-diphosphoglycerate by catalyzing the hydrolysis of this substrate to 3-phosphoglycerate ?
-
?
3.6.1.7 additional information Saccharomyces cerevisiae possible role in preventing the intracellular accumulation of 1,3-diphosphoglycerate by catalyzing the hydrolysis of this substrate to 3-phosphoglycerate ?
-
?
3.6.1.7 additional information Bos taurus possible role in preventing the intracellular accumulation of 1,3-diphosphoglycerate by catalyzing the hydrolysis of this substrate to 3-phosphoglycerate ?
-
?
3.6.1.7 additional information Oryctolagus cuniculus possible role in preventing the intracellular accumulation of 1,3-diphosphoglycerate by catalyzing the hydrolysis of this substrate to 3-phosphoglycerate ?
-
?
3.6.1.7 additional information Equus caballus possible role in preventing the intracellular accumulation of 1,3-diphosphoglycerate by catalyzing the hydrolysis of this substrate to 3-phosphoglycerate ?
-
?
3.6.1.7 additional information Equus caballus enzyme could control acylation and carbamylation of proteins by regulation the levels of reactive acyl and carbamoyl phosphates ?
-
?
3.6.1.7 additional information Equus caballus possible physiological role for acylphosphatase activity may be regulation of metabolic pathways involving 1,3-diphosphoglycerate and carbamoyl phosphate, e.g. glycolytic pathway and pyrimidine biosynthesis, by its ability to hydrolyze these substrates ?
-
?

Organism

EC Number Organism UniProt Comment Textmining
3.6.1.7 Bos taurus
-
bovine
-
3.6.1.7 Equus caballus
-
-
-
3.6.1.7 Gallus gallus
-
-
-
3.6.1.7 Homo sapiens
-
human
-
3.6.1.7 Oryctolagus cuniculus
-
-
-
3.6.1.7 Saccharomyces cerevisiae
-
-
-
3.6.1.7 Sus scrofa
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.6.1.7
-
Oryctolagus cuniculus
3.6.1.7 brain Bos taurus
3.6.1.7 erythrocyte isoenzyme Homo sapiens
3.6.1.7 heart muscle Sus scrofa
3.6.1.7 heart muscle Bos taurus
3.6.1.7 muscle and liver Equus caballus
3.6.1.7 partial Saccharomyces cerevisiae
3.6.1.7 partially from breast muscle Gallus gallus

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.6.1.7 brain
-
Gallus gallus
-
3.6.1.7 brain
-
Homo sapiens
-
3.6.1.7 brain
-
Sus scrofa
-
3.6.1.7 brain
-
Bos taurus
-
3.6.1.7 brain
-
Equus caballus
-
3.6.1.7 erythrocyte
-
Gallus gallus
-
3.6.1.7 erythrocyte
-
Homo sapiens
-
3.6.1.7 erythrocyte
-
Bos taurus
-
3.6.1.7 heart
-
Gallus gallus
-
3.6.1.7 heart
-
Homo sapiens
-
3.6.1.7 heart
-
Sus scrofa
-
3.6.1.7 heart
-
Bos taurus
-
3.6.1.7 heart
-
Equus caballus
-
3.6.1.7 liver
-
Gallus gallus
-
3.6.1.7 liver
-
Homo sapiens
-
3.6.1.7 liver
-
Equus caballus
-
3.6.1.7 muscle
-
Gallus gallus
-
3.6.1.7 muscle
-
Homo sapiens
-
3.6.1.7 muscle
-
Sus scrofa
-
3.6.1.7 muscle
-
Oryctolagus cuniculus
-
3.6.1.7 muscle
-
Equus caballus
-
3.6.1.7 muscle heart muscle Bos taurus
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.6.1.7 12
-
erythrocyte Homo sapiens
3.6.1.7 600
-
heart Sus scrofa
3.6.1.7 1250
-
brain Bos taurus
3.6.1.7 2800
-
liver Equus caballus
3.6.1.7 3000
-
muscle Equus caballus

Storage Stability

EC Number Storage Stability Organism
3.6.1.7 -20°C stable for at least 1 year Bos taurus
3.6.1.7 -20°C, long-time stable Sus scrofa
3.6.1.7 brain enzyme, unusually stable to prolonged storage Bos taurus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.6.1.7 1,3-diphosphoglycerate + H2O
-
Gallus gallus 3-phosphoglycerate + phosphate
-
?
3.6.1.7 1,3-diphosphoglycerate + H2O
-
Homo sapiens 3-phosphoglycerate + phosphate
-
?
3.6.1.7 1,3-diphosphoglycerate + H2O
-
Sus scrofa 3-phosphoglycerate + phosphate
-
?
3.6.1.7 1,3-diphosphoglycerate + H2O
-
Saccharomyces cerevisiae 3-phosphoglycerate + phosphate
-
?
3.6.1.7 1,3-diphosphoglycerate + H2O
-
Bos taurus 3-phosphoglycerate + phosphate
-
?
3.6.1.7 1,3-diphosphoglycerate + H2O
-
Oryctolagus cuniculus 3-phosphoglycerate + phosphate
-
?
3.6.1.7 1,3-diphosphoglycerate + H2O
-
Equus caballus 3-phosphoglycerate + phosphate
-
?
3.6.1.7 1,3-diphosphoglycerate + H2O possible role in preventing the intracellular accumulation of 1,3-diphosphoglycerate by catalyzing the hydrolysis of this substrate to 3-phosphoglycerate Gallus gallus 3-phosphoglycerate + phosphate
-
?
3.6.1.7 1,3-diphosphoglycerate + H2O possible role in preventing the intracellular accumulation of 1,3-diphosphoglycerate by catalyzing the hydrolysis of this substrate to 3-phosphoglycerate Homo sapiens 3-phosphoglycerate + phosphate
-
?
3.6.1.7 1,3-diphosphoglycerate + H2O possible role in preventing the intracellular accumulation of 1,3-diphosphoglycerate by catalyzing the hydrolysis of this substrate to 3-phosphoglycerate Sus scrofa 3-phosphoglycerate + phosphate
-
?
3.6.1.7 1,3-diphosphoglycerate + H2O possible role in preventing the intracellular accumulation of 1,3-diphosphoglycerate by catalyzing the hydrolysis of this substrate to 3-phosphoglycerate Saccharomyces cerevisiae 3-phosphoglycerate + phosphate
-
?
3.6.1.7 1,3-diphosphoglycerate + H2O possible role in preventing the intracellular accumulation of 1,3-diphosphoglycerate by catalyzing the hydrolysis of this substrate to 3-phosphoglycerate Bos taurus 3-phosphoglycerate + phosphate
-
?
3.6.1.7 1,3-diphosphoglycerate + H2O possible role in preventing the intracellular accumulation of 1,3-diphosphoglycerate by catalyzing the hydrolysis of this substrate to 3-phosphoglycerate Oryctolagus cuniculus 3-phosphoglycerate + phosphate
-
?
3.6.1.7 1,3-diphosphoglycerate + H2O possible role in preventing the intracellular accumulation of 1,3-diphosphoglycerate by catalyzing the hydrolysis of this substrate to 3-phosphoglycerate Equus caballus 3-phosphoglycerate + phosphate
-
?
3.6.1.7 1,3-diphosphoglycerate + H2O 1,3-diphosphoglycerate can acylate histones, particularly the lysine-rich ones, 1,3-diphosphoglycerate phosphatase can prevent this acylation Gallus gallus 3-phosphoglycerate + phosphate
-
?
3.6.1.7 1,3-diphosphoglycerate + H2O 1,3-diphosphoglycerate can acylate histones, particularly the lysine-rich ones, 1,3-diphosphoglycerate phosphatase can prevent this acylation Homo sapiens 3-phosphoglycerate + phosphate
-
?
3.6.1.7 1,3-diphosphoglycerate + H2O 1,3-diphosphoglycerate can acylate histones, particularly the lysine-rich ones, 1,3-diphosphoglycerate phosphatase can prevent this acylation Sus scrofa 3-phosphoglycerate + phosphate
-
?
3.6.1.7 1,3-diphosphoglycerate + H2O 1,3-diphosphoglycerate can acylate histones, particularly the lysine-rich ones, 1,3-diphosphoglycerate phosphatase can prevent this acylation Saccharomyces cerevisiae 3-phosphoglycerate + phosphate
-
?
3.6.1.7 1,3-diphosphoglycerate + H2O 1,3-diphosphoglycerate can acylate histones, particularly the lysine-rich ones, 1,3-diphosphoglycerate phosphatase can prevent this acylation Bos taurus 3-phosphoglycerate + phosphate
-
?
3.6.1.7 1,3-diphosphoglycerate + H2O 1,3-diphosphoglycerate can acylate histones, particularly the lysine-rich ones, 1,3-diphosphoglycerate phosphatase can prevent this acylation Oryctolagus cuniculus 3-phosphoglycerate + phosphate
-
?
3.6.1.7 1,3-diphosphoglycerate + H2O 1,3-diphosphoglycerate can acylate histones, particularly the lysine-rich ones, 1,3-diphosphoglycerate phosphatase can prevent this acylation Equus caballus 3-phosphoglycerate + phosphate
-
?
3.6.1.7 acetyl phosphate + H2O
-
Gallus gallus acetate + phosphate
-
?
3.6.1.7 acetyl phosphate + H2O
-
Homo sapiens acetate + phosphate
-
?
3.6.1.7 acetyl phosphate + H2O
-
Sus scrofa acetate + phosphate
-
?
3.6.1.7 acetyl phosphate + H2O
-
Bos taurus acetate + phosphate
-
?
3.6.1.7 acetyl phosphate + H2O
-
Oryctolagus cuniculus acetate + phosphate
-
?
3.6.1.7 acetyl phosphate + H2O
-
Equus caballus acetate + phosphate
-
?
3.6.1.7 acylphosphate + H2O specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates Gallus gallus carboxylate + phosphate
-
?
3.6.1.7 acylphosphate + H2O specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates Homo sapiens carboxylate + phosphate
-
?
3.6.1.7 acylphosphate + H2O specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates Sus scrofa carboxylate + phosphate
-
?
3.6.1.7 acylphosphate + H2O specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates Saccharomyces cerevisiae carboxylate + phosphate
-
?
3.6.1.7 acylphosphate + H2O specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates Bos taurus carboxylate + phosphate
-
?
3.6.1.7 acylphosphate + H2O specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates Oryctolagus cuniculus carboxylate + phosphate
-
?
3.6.1.7 acylphosphate + H2O specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates Equus caballus carboxylate + phosphate
-
?
3.6.1.7 ATP + H2O muscle enzyme, very low activity Equus caballus ?
-
?
3.6.1.7 benzoyl phosphate + H2O
-
Gallus gallus benzoate + phosphate
-
?
3.6.1.7 benzoyl phosphate + H2O
-
Homo sapiens benzoate + phosphate
-
?
3.6.1.7 benzoyl phosphate + H2O
-
Sus scrofa benzoate + phosphate
-
?
3.6.1.7 benzoyl phosphate + H2O
-
Bos taurus benzoate + phosphate
-
?
3.6.1.7 benzoyl phosphate + H2O
-
Oryctolagus cuniculus benzoate + phosphate
-
?
3.6.1.7 benzoyl phosphate + H2O
-
Equus caballus benzoate + phosphate
-
?
3.6.1.7 carbamoyl phosphate + H2O
-
Sus scrofa carbamate + phosphate
-
?
3.6.1.7 carbamoyl phosphate + H2O
-
Bos taurus carbamate + phosphate
-
?
3.6.1.7 carbamoyl phosphate + H2O
-
Equus caballus carbamate + phosphate
-
?
3.6.1.7 carbamoyl phosphate + H2O erythrocyte enzyme: not a substrate Homo sapiens carbamate + phosphate
-
?
3.6.1.7 diphosphate + H2O muscle enzyme, very low activity Equus caballus 2 phosphate
-
?
3.6.1.7 diphosphate + H2O erythrocyte enzyme, inorganic diphosphate: not a substrate Homo sapiens 2 phosphate
-
?
3.6.1.7 additional information substrate specificity Gallus gallus ?
-
?
3.6.1.7 additional information substrate specificity Homo sapiens ?
-
?
3.6.1.7 additional information substrate specificity Sus scrofa ?
-
?
3.6.1.7 additional information substrate specificity Bos taurus ?
-
?
3.6.1.7 additional information substrate specificity Oryctolagus cuniculus ?
-
?
3.6.1.7 additional information substrate specificity Equus caballus ?
-
?
3.6.1.7 additional information specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates Gallus gallus ?
-
?
3.6.1.7 additional information specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates Homo sapiens ?
-
?
3.6.1.7 additional information specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates Sus scrofa ?
-
?
3.6.1.7 additional information specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates Saccharomyces cerevisiae ?
-
?
3.6.1.7 additional information specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates Bos taurus ?
-
?
3.6.1.7 additional information specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates Oryctolagus cuniculus ?
-
?
3.6.1.7 additional information specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates Equus caballus ?
-
?
3.6.1.7 additional information no activity with 3-phosphoglycerate, phosphocreatine, DL-3-glycerophosphate, fructose 1,6-diphosphate, glucose 6-phosphate, fructose 6-phosphate, phosphoenolpyruvate, ATP, ADP, AMP, cyclic-AMP, 6-phosphogluconate phosphoserine Homo sapiens ?
-
?
3.6.1.7 additional information acts specifically by splitting off the carboxyl phosphate bond Gallus gallus ?
-
?
3.6.1.7 additional information acts specifically by splitting off the carboxyl phosphate bond Homo sapiens ?
-
?
3.6.1.7 additional information acts specifically by splitting off the carboxyl phosphate bond Sus scrofa ?
-
?
3.6.1.7 additional information acts specifically by splitting off the carboxyl phosphate bond Saccharomyces cerevisiae ?
-
?
3.6.1.7 additional information acts specifically by splitting off the carboxyl phosphate bond Bos taurus ?
-
?
3.6.1.7 additional information acts specifically by splitting off the carboxyl phosphate bond Oryctolagus cuniculus ?
-
?
3.6.1.7 additional information acts specifically by splitting off the carboxyl phosphate bond Equus caballus ?
-
?
3.6.1.7 additional information no activity with phosphoenolpyruvate and phosvitin Equus caballus ?
-
?
3.6.1.7 additional information possible role in preventing the intracellular accumulation of 1,3-diphosphoglycerate by catalyzing the hydrolysis of this substrate to 3-phosphoglycerate Gallus gallus ?
-
?
3.6.1.7 additional information possible role in preventing the intracellular accumulation of 1,3-diphosphoglycerate by catalyzing the hydrolysis of this substrate to 3-phosphoglycerate Homo sapiens ?
-
?
3.6.1.7 additional information possible role in preventing the intracellular accumulation of 1,3-diphosphoglycerate by catalyzing the hydrolysis of this substrate to 3-phosphoglycerate Sus scrofa ?
-
?
3.6.1.7 additional information possible role in preventing the intracellular accumulation of 1,3-diphosphoglycerate by catalyzing the hydrolysis of this substrate to 3-phosphoglycerate Saccharomyces cerevisiae ?
-
?
3.6.1.7 additional information possible role in preventing the intracellular accumulation of 1,3-diphosphoglycerate by catalyzing the hydrolysis of this substrate to 3-phosphoglycerate Bos taurus ?
-
?
3.6.1.7 additional information possible role in preventing the intracellular accumulation of 1,3-diphosphoglycerate by catalyzing the hydrolysis of this substrate to 3-phosphoglycerate Oryctolagus cuniculus ?
-
?
3.6.1.7 additional information possible role in preventing the intracellular accumulation of 1,3-diphosphoglycerate by catalyzing the hydrolysis of this substrate to 3-phosphoglycerate Equus caballus ?
-
?
3.6.1.7 additional information enzyme could control acylation and carbamylation of proteins by regulation the levels of reactive acyl and carbamoyl phosphates Equus caballus ?
-
?
3.6.1.7 additional information possible physiological role for acylphosphatase activity may be regulation of metabolic pathways involving 1,3-diphosphoglycerate and carbamoyl phosphate, e.g. glycolytic pathway and pyrimidine biosynthesis, by its ability to hydrolyze these substrates Equus caballus ?
-
?
3.6.1.7 p-nitrobenzoyl phosphate + H2O
-
Homo sapiens p-nitrobenzoate + phosphate
-
?
3.6.1.7 p-nitrobenzoyl phosphate + H2O
-
Equus caballus p-nitrobenzoate + phosphate
-
?
3.6.1.7 p-nitrophenyl phosphate + H2O erythrocyte enzyme, not a substrate Homo sapiens p-nitrophenol + phosphate
-
?
3.6.1.7 p-nitrophenyl phosphate + H2O muscle enzyme, very low activity at pH 5.3, no activity at pH 10.4 Equus caballus p-nitrophenol + phosphate
-
?
3.6.1.7 phosphocreatine + H2O muscle enzyme, very low activity Equus caballus ?
-
?

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.6.1.7 25
-
assay at Gallus gallus
3.6.1.7 25
-
assay at Homo sapiens
3.6.1.7 25
-
assay at Sus scrofa
3.6.1.7 25
-
assay at Saccharomyces cerevisiae
3.6.1.7 25
-
assay at Bos taurus
3.6.1.7 25
-
assay at Oryctolagus cuniculus
3.6.1.7 25
-
assay at Equus caballus
3.6.1.7 27
-
assay at Sus scrofa
3.6.1.7 27
-
assay at Bos taurus
3.6.1.7 37
-
erythrocyte, assay at Homo sapiens

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.6.1.7 additional information
-
-
Gallus gallus
3.6.1.7 additional information
-
enzyme is thermostable Bos taurus
3.6.1.7 additional information
-
enzyme is thermostable Equus caballus
3.6.1.7 additional information
-
muscle and brain enzymes: stable at high temperatures Homo sapiens
3.6.1.7 70
-
erythrocyte enzyme, 5 min: 40% loss of activity Homo sapiens
3.6.1.7 85
-
heart enzyme, pH 2.0, 5 min, 95% activity retained Sus scrofa

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.6.1.7 additional information
-
-
Gallus gallus
3.6.1.7 additional information
-
muscle, pI: 11.4 Homo sapiens
3.6.1.7 additional information
-
muscle, pI: 11.4 Equus caballus
3.6.1.7 additional information
-
heart, pI: 7.25-7.3 Sus scrofa
3.6.1.7 additional information
-
erythrocyte enzyme is a basic protein Homo sapiens
3.6.1.7 5
-
-
Gallus gallus
3.6.1.7 5
-
-
Sus scrofa
3.6.1.7 5
-
erythrocyte enzyme, substrate: acetyl phosphate Homo sapiens
3.6.1.7 5.3
-
assay at Gallus gallus
3.6.1.7 5.3
-
assay at Homo sapiens
3.6.1.7 5.3
-
assay at Sus scrofa
3.6.1.7 5.3
-
assay at Saccharomyces cerevisiae
3.6.1.7 5.3
-
assay at Bos taurus
3.6.1.7 5.3
-
assay at Oryctolagus cuniculus
3.6.1.7 5.3
-
assay at Equus caballus
3.6.1.7 5.3
-
muscle and liver Equus caballus
3.6.1.7 5.4
-
-
Oryctolagus cuniculus
3.6.1.7 5.4
-
erythrocyte, assay at Homo sapiens
3.6.1.7 5.4 5.6 heart enzyme, substrate: acetyl phosphate Sus scrofa
3.6.1.7 6
-
assay at Sus scrofa
3.6.1.7 6
-
assay at Bos taurus
3.6.1.7 7.4 7.6 brain, substrate: acetyl phosphate Bos taurus

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
3.6.1.7 additional information
-
-
Gallus gallus
3.6.1.7 additional information
-
-
Homo sapiens
3.6.1.7 additional information
-
-
Oryctolagus cuniculus
3.6.1.7 additional information
-
brain enzyme is acid stable Bos taurus
3.6.1.7 additional information
-
liver enzyme is acid stable Equus caballus
3.6.1.7 1.5 2 heart enzyme, 100% activity retained Sus scrofa
3.6.1.7 9
-
-
Oryctolagus cuniculus
3.6.1.7 9
-
heart enzyme, 92% activity retained Sus scrofa

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
3.6.1.7 3.2
-
fructose 1,6-diphosphate noncompetitive inhibition Equus caballus
3.6.1.7 3.5
-
methyl phosphate moderate competitive inhibition Equus caballus
3.6.1.7 6.9
-
Carbamoyl phosphate erythrocyte enzyme, competitive inhibition Homo sapiens
3.6.1.7 11
-
benzyl phosphate moderate competitive inhibition Equus caballus