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Literature summary for 3.1.3.1 extracted from

  • Xie, L.P.; Xu, G.R.; Cao, W.Z.; Zhang, J.; Zhang, R.Q.
    An essential tryptophan residue in alkaline phosphatase from pearl oyster (Pinctada fucata) (2008), Biochemistry (Moscow), 73, 87-91.
    View publication on PubMed
Search for more literature for 3.1.3.1

Protein Variants

Protein Variants Comment Organism
additional information ALP is completely inactivated in the presence of 0.2 mM N-bromosuccinimide. Inactivation of purified alkaline phosphatase by N-bromosuccinimide is dependent on modification of only one of five tryptophan residues in the enzyme. Substrate protection experiments show that the tryptophan residue is not located at the substratebinding site but is involved in the catalytic activity Pinctada fucata

Inhibitors

Inhibitors Comment Organism Structure
phosphate competitive inhibitor Pinctada fucata
tungstate competitive inhibitor Pinctada fucata

Organism

Organism UniProt Comment Textmining
Pinctada fucata Q17TZ1
-
-

Purification (Commentary)

Purification (Comment) Organism
using L-histidyldia-zobenzylphosphonic acid agarose affinity chromatography Pinctada fucata

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-glycerol phosphate + H2O
-
 Pinctada fucata glycerol + phosphate
-
 ?
4-nitrophenyl phosphate + H2O
-
 Pinctada fucata 4-nitrophenol + phosphate
-
 ?

Synonyms

Synonyms Comment Organism
alkaline phosphatase
-
 Pinctada fucata
ALP
-
 Pinctada fucata

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
 assay at Pinctada fucata

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
10
-
 assay at Pinctada fucata