Literature summary for 3.1.3.1 extracted from

Zalatan, J.G.; Catrina, I.; Mitchell, R.; Grzyska, P.K.; Obrien, P.J.; Herschlag, D.; Hengge, A.C.
Kinetic isotope effects for alkaline phosphatase reactions: implications for the role of active-site metal ions in catalysis (2007), J. Am. Chem. Soc., 129, 9789-9798.

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Metals/Ions

Metals/Ions	Comment	Organism	Structure
Zn2+	strong support for a model in which electrostatic interactions between the bimetallo Zn2+ site and a nonbridging phosphate ester oxygen atom make a significant contribution to the large rate enhancement observed for alkaline phosphatase-catalyzed phosphate monoester hydrolysis	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Escherichia coli

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
4-nitrophenyl phosphate + H2O	strong support for a model in which electrostatic interactions between the bimetallo Zn2+ site and a nonbridging phosphate ester oxygen atom make a significant contribution to the large rate enhancement observed for alkaline phosphatase-catalyzed phosphate monoester hydrolysis	Escherichia coli	4-nitrophenol + phosphate	-	?

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Release 2023.1 (January 2023)