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Literature summary 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

Protein Variants

EC Number Protein Variants Comment Organism
3.1.3.1 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

EC Number Inhibitors Comment Organism Structure
3.1.3.1 phosphate competitive inhibitor Pinctada fucata
3.1.3.1 tungstate competitive inhibitor Pinctada fucata

Organism

EC Number Organism UniProt Comment Textmining
3.1.3.1 Pinctada fucata Q17TZ1
-
-

Purification (Commentary)

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

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.3.1 2-glycerol phosphate + H2O
-
 Pinctada fucata glycerol + phosphate
-
 ?
3.1.3.1 4-nitrophenyl phosphate + H2O
-
 Pinctada fucata 4-nitrophenol + phosphate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.1.3.1 alkaline phosphatase
-
 Pinctada fucata
3.1.3.1 ALP
-
 Pinctada fucata

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.1.3.1 25
-
 assay at Pinctada fucata

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.1.3.1 10
-
 assay at Pinctada fucata