Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Minowa, O.; Ohba, Y.; Mizuno, Y.; Shiokawa, H.
    The primary structure of chicken muscle acylphosphatase isozyme Ch1 (1987), J. Biochem., 102, 1213-1220.
    View publication on PubMed

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.6.1.7 11320
-
 Ch1, calculated from amino acid sequence Gallus gallus

Organism

EC Number Organism UniProt Comment Textmining
3.6.1.7 Gallus gallus
-
 two different isozymes: Ch1 and Ch2
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.6.1.7 from breast and leg muscles Gallus gallus
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
-

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 6000
-
 Ch1, substrate benzoyl phosphate, 25°C Gallus gallus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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 benzoyl phosphate + H2O
-
 Gallus gallus benzoate + phosphate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
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 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