Literature summary for 3.1.3.1 extracted from

Harada, T.; Koyama, I.; Matsunaga, T.; Kikuno, A.; Kasahara, T.; Hassimoto, M.; Alpers, D.H.; Komoda, T.
Characterization of structural and catalytic differences in rat intestinal alkaline phosphatase isozymes (2005), FEBS J., 272, 2477-2486.

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Metals/Ions

Metals/Ions	Comment	Organism	Structure
additional information	the SWISS-MODEL program is used to construct a model of isoenzyme rIAP-I. Analysis of the active site of the enzyme and the effect of various combinations of metals at the active site. The model shows the possibility of a Zn triad at the metal-binding position of the active site in rIAP-I	Rattus norvegicus
additional information	the SWISS-MODEL program is used to construct a model of isoenzyme rIAP-II. Analysis of the active site of the enzyme and the effect of various combinations of metals at the active site	Rattus norvegicus

Organism

Organism	UniProt	Comment	Textmining
Rattus norvegicus	-	-	-

Source Tissue

Source Tissue	Comment	Organism	Textmining
intestine	-	Rattus norvegicus	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
4-nitrophenyl phosphate + H2O	-	Rattus norvegicus	4-nitrophenol + phosphate	-	?

Synonyms

Synonyms	Comment	Organism
rIAP-I	-	Rattus norvegicus
rIAP-II	-	Rattus norvegicus

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Release 2023.1 (January 2023)