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Literature summary extracted from

  • Roston, D.; Cui, Q.
    Substrate and transition state binding in alkaline phosphatase analyzed by computation of oxygen isotope effects (2016), J. Am. Chem. Soc., 138, 11946-11957 .
    View publication on PubMedView publication on EuropePMC

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.1.3.1 Zn2+ contains zinc Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
3.1.3.1 Escherichia coli P00634
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.3.1 3-nitrophenyl phosphate + H2O
-
Escherichia coli 3-nitrophenol + phosphate
-
?
3.1.3.1 4-aminophenyl phosphate + H2O
-
Escherichia coli 4-aminophenol + phosphate
-
?
3.1.3.1 4-nitrophenyl phosphate + H2O
-
Escherichia coli 4-nitrophenol + phosphate
-
?
3.1.3.1 ethyl phosphate + H2O
-
Escherichia coli ethanol + phosphate
-
?
3.1.3.1 methyl 3-nitrophenyl phosphate + H2O
-
Escherichia coli methyl phosphate + 3-nitrophenol
-
?
3.1.3.1 methyl 4-nitrophenyl phosphate + H2O
-
Escherichia coli methyl phosphate + 4-nitrophenol
-
?
3.1.3.1 methylphenyl phosphate + H2O
-
Escherichia coli methyl phosphate + phenol
-
?
3.1.3.1 phenyl phosphate + H2O
-
Escherichia coli phenol + phosphate
-
?
3.1.3.1 propargyl phosphate + H2O
-
Escherichia coli prop-1-yne + phosphate
-
?