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

BRENDA support

Literature summary extracted from

  • Liao, J.H.; Chen, Q.X.; Zhang, Q.; Yang, Y.; Shi, Y.
    Unfolding and inactivation of Abalone (Haliotis diversicolor) alkaline phosphatase during denaturation by guanidine hydrochloride (2008), Appl. Biochem. Biotechnol., 158, 323-333.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.1.3.1 guanidine hydrochloride inactivation of the enzyme by GuHCl (guanidine hydrochloride) is a slow, reversible reaction with fractional remaining activity. The microscopic rate constants are determined. The enzyme is protected by the substrate to a certain extent during guanidine denaturation. The changes of conformation of the enzyme in different concentrations of GuHCl are studied. The inactivation occurs before the noticeable conformational changes of the enzyme molecule as a whole can be detected, which suggests that the active site of the enzyme has more flexibility than the whole enzyme molecule Haliotis diversicolor

Organism

EC Number Organism UniProt Comment Textmining
3.1.3.1 Haliotis diversicolor
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.1.3.1 crude extract is purified using ion exchange gel DEAE-32, then by filtration chromatograph through Sephadex G-200, and ion exchange gel DEAE-32 Haliotis diversicolor

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.3.1 4-nitrophenyl phosphate + H2O
-
Haliotis diversicolor 4-nitrophenol + phosphate
-
?

Synonyms

EC Number Synonyms Comment Organism
3.1.3.1 alkaline phosphatase
-
Haliotis diversicolor
3.1.3.1 ALPase
-
Haliotis diversicolor

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.1.3.1 37
-
assay at Haliotis diversicolor

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.1.3.1 10.1
-
assay at Haliotis diversicolor