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Literature summary extracted from

  • Ohba, Y.; Mizuno, Y.; Takasawa, T.; Shiokawa, H.
    Two isozymes of chicken muscle acylphosphatase: purification and properties (1985), J. Biochem., 98, 909-919.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.6.1.7 Ch1 Gallus gallus

General Stability

EC Number General Stability Organism
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 Oryctolagus cuniculus
3.6.1.7 enzyme is very stable Equus caballus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.6.1.7 additional information
-
additional information kinetic data Gallus gallus
3.6.1.7 additional information
-
additional information kinetic data Sus scrofa
3.6.1.7 additional information
-
additional information kinetic data Oryctolagus cuniculus
3.6.1.7 additional information
-
additional information kinetic data Equus caballus
3.6.1.7 0.17
-
benzoyl phosphate Ch2 Gallus gallus
3.6.1.7 0.39
-
benzoyl phosphate Ch1 monomer Gallus gallus
3.6.1.7 0.48
-
benzoyl phosphate Ch1 dimer Gallus gallus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.6.1.7 9400
-
Ch1, 1 * 9400, SDS-PAGE Gallus gallus
3.6.1.7 9400
-
Ch1, 2 * 9400, SDS-PAGE Gallus gallus
3.6.1.7 11060
-
calculated from amino acid sequence Equus caballus
3.6.1.7 11400
-
Ch2, 1 * 11400, SDS-PAGE Gallus gallus
3.6.1.7 11900
-
Ch1, sedimentation equilibrium Gallus gallus
3.6.1.7 12000
-
Ch2, sedimentation equilibrium Gallus gallus

Organism

EC Number Organism UniProt Comment Textmining
3.6.1.7 Equus caballus
-
-
-
3.6.1.7 Gallus gallus
-
Ch1 and Ch2 are genetically specified isozymes
-
3.6.1.7 Gallus gallus
-
two different isozymes: Ch1 and Ch2
-
3.6.1.7 Oryctolagus cuniculus
-
-
-
3.6.1.7 Sus scrofa
-
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.6.1.7 no modification
-
Sus scrofa
3.6.1.7 no modification Ch1 and Ch2: no sugar, no hexose, no hexosamine Gallus gallus

Purification (Commentary)

EC Number Purification (Comment) Organism
3.6.1.7
-
Sus scrofa
3.6.1.7
-
Oryctolagus cuniculus
3.6.1.7
-
Equus caballus
3.6.1.7 two isozymes: Ch1 and Ch2 Gallus gallus

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.6.1.7 muscle skeletal muscle Gallus gallus
-
3.6.1.7 muscle skeletal muscle Sus scrofa
-
3.6.1.7 muscle skeletal muscle Oryctolagus cuniculus
-
3.6.1.7 muscle skeletal muscle Equus caballus
-
3.6.1.7 muscle muscle-type and common-type enzyme Gallus gallus
-

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 5960
-
Ch1 Gallus gallus
3.6.1.7 8500
-
Ch2 Gallus gallus

Storage Stability

EC Number Storage Stability Organism
3.6.1.7 4°C, Ch1 crystalline enzyme suspension, long-time stable Gallus gallus
3.6.1.7 4°C, Ch2, 70% ammonium sulfate, long-time stable Gallus gallus

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
-
Sus scrofa 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 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 Sus scrofa 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 benzoyl phosphate + H2O
-
Gallus gallus benzoate + phosphate
-
?
3.6.1.7 benzoyl phosphate + H2O
-
Sus scrofa benzoate + phosphate
-
?
3.6.1.7 benzoyl phosphate + H2O
-
Oryctolagus cuniculus benzoate + phosphate
-
?
3.6.1.7 benzoyl phosphate + H2O
-
Equus caballus benzoate + phosphate
-
?

Subunits

EC Number Subunits Comment Organism
3.6.1.7 dimer
-
Sus scrofa
3.6.1.7 dimer
-
Equus caballus
3.6.1.7 dimer Ch1, 2 * 9400, SDS-PAGE Gallus gallus
3.6.1.7 monomer
-
Sus scrofa
3.6.1.7 monomer
-
Oryctolagus cuniculus
3.6.1.7 monomer
-
Equus caballus
3.6.1.7 monomer Ch2, 1 * 11400, SDS-PAGE Gallus gallus
3.6.1.7 monomer Ch1, 1 * 9400, SDS-PAGE Gallus gallus

Synonyms

EC Number Synonyms Comment Organism
3.6.1.7 Ch1 Ch1 and Ch2 are different genetically specified isozymes Gallus gallus
3.6.1.7 Ch1 multiple forms of chicken acylphosphatase, 2 isozymes: Ch1 and Ch2 differ in molecular weight, amino acid composition and kinetic parameters Gallus gallus
3.6.1.7 Ch2 Ch1 and Ch2 are different genetically specified isozymes Gallus gallus
3.6.1.7 Ch2 multiple forms of chicken acylphosphatase, 2 isozymes: Ch1 and Ch2 differ in molecular weight, amino acid composition and kinetic parameters Gallus gallus

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 Sus scrofa
3.6.1.7 25
-
assay at Oryctolagus cuniculus
3.6.1.7 25
-
assay at Equus caballus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.6.1.7 5
-
-
Sus scrofa
3.6.1.7 5
-
dimer of Ch1, and Ch2 Gallus gallus
3.6.1.7 5.3
-
assay at Gallus gallus
3.6.1.7 5.3
-
assay at Sus scrofa
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
-
monomer of Ch1 Gallus gallus