Literature summary for 3.1.3.1 extracted from

Nikolic-Hughes, I.; O'Brien, P.J.; Herschlag, D.
Alkaline phosphatase catalysis is ultrasensitive to charge sequestered between the active site zinc ions (2005), J. Am. Chem. Soc., 127, 9314-9315.

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Metals/Ions

Metals/Ions	Comment	Organism	Structure
Zn2+	the enzyme employs a binuclear metallocenter of two Zn2+ ions approximately 4 A apart to facilitate catalysis of phosphate monoester hydrolysis. Alkaline phosphatase catalysis is ultrasensitive to charge sequestered between the active site zinc ions	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
bis(p-nitrophenyl)phosphate + H2O	-	Escherichia coli	?	-	?
methyl p-nitrophenyl phosphate + H2O	-	Escherichia coli	methanol + p-nitrophenol + phosphate	-	?
methyl p-nitrophenyl phosphorothioate + H2O	-	Escherichia coli	methanol + p-nitrophenol + phosphorothioate	-	?
p-nitrophenyl phosphate + H2O	-	Escherichia coli	p-nitrophenol + phosphate	-	?
p-nitrophenyl sulfate + H2O	-	Escherichia coli	p-nitrophenol + sulfate	-	?

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Release 2023.1 (January 2023)