Literature summary for 3.5.2.16 extracted from

Huang, C.Y.; Yang, Y.S.
The role of metal on imide hydrolysis: metal content and pH profiles of metal ion-replaced mammalian imidase (2002), Biochem. Biophys. Res. Commun., 297, 1027-1032.

Search for more literature for 3.5.2.16

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Cd2+	apoenzyme reconstituted with Co2+ has 15.8fold lower activity than the native Zn-containing enzyme	Sus scrofa
Co2+	apoenzyme reconstituted with Co2+ has about 2fold higher activity than the native Zn-containing enzyme	Sus scrofa
Mn2+	apoenzyme reconstituted with Co2+ has 4.4fold lower activity than the native Zn-containing enzyme	Sus scrofa
additional information	enzyme reconstituted with Cu2+ and Ni2+ has no enzymatic activity	Sus scrofa
Zinc	native enzyme contains 1 Zn2+ per subunit	Sus scrofa

Organism

Organism	UniProt	Comment	Textmining
Sus scrofa	-	-	-

Source Tissue

Source Tissue	Comment	Organism	Textmining
liver	-	Sus scrofa	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
phthalimide + H2O	-	Sus scrofa	2-(aminocarbonyl)benzoic acid	-	?

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Release 2023.1 (January 2023)