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Literature summary for 3.6.1.7 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]

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

Organism

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

Purification (Commentary)

Purification (Comment) Organism
from breast and leg muscles Gallus gallus
two isozymes: Ch1 and Ch2 Gallus gallus

Source Tissue

Source Tissue Comment Organism Textmining
muscle skeletal muscle Gallus gallus
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
6000
-
Ch1, substrate benzoyl phosphate, 25°C Gallus gallus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acylphosphate + H2O specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates Gallus gallus carboxylate + phosphate
-
?
benzoyl phosphate + H2O
-
Gallus gallus benzoate + phosphate
-
?

Synonyms

Synonyms Comment Organism
Ch1 multiple forms of chicken acylphosphatase, 2 isozymes: Ch1 and Ch2 differ in molecular weight, amino acid composition and kinetic parameters Gallus gallus
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]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
assay at Gallus gallus