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Literature summary for 3.1.3.1 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

Inhibitors Comment Organism Structure
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

Organism UniProt Comment Textmining
Haliotis diversicolor
-
-
-

Purification (Commentary)

Purification (Comment) Organism
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)

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

Synonyms

Synonyms Comment Organism
alkaline phosphatase
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Haliotis diversicolor
ALPase
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Haliotis diversicolor

Temperature Optimum [°C]

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

pH Optimum

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