Literature summary extracted from

Palma, M.S.; Rodrigues, S.A.; Rossi, A.
Acid phosphatase from maize scutellum: succinylation and some kinetic properties of the active enzyme (1981), Phytochemistry, 20, 2481-2482.

No PubMed abstract available

General Stability

EC Number	General Stability	Organism
3.1.3.2	enzyme maintains its catalytic activity after succinylation of 52 free amino groups per molecule. Free amino groups may play an important role in the maintenance of enzyme stability at pH values greater than pH 5.4	Zea mays

KM Value [mM]

EC Number	KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
3.1.3.2	0.3	-	p-nitrophenyl phosphate	pH 5.4	Zea mays
3.1.3.2	0.5	-	p-nitrophenyl phosphate	succinylated enzyme, pH 5.4	Zea mays
3.1.3.2	1.6	-	p-nitrophenyl phosphate	pH 6.7	Zea mays
3.1.3.2	6.5	-	p-nitrophenyl phosphate	succinylated enzyme, pH 6.7	Zea mays

Organism

EC Number	Organism	UniProt	Comment	Textmining
3.1.3.2	Zea mays	-	-	-

Source Tissue

EC Number	Source Tissue	Comment	Organism	Textmining
3.1.3.2	scutellum	-	Zea mays	-

Substrates and Products (Substrate)

EC Number	Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
3.1.3.2	p-nitrophenyl phosphate + H2O	-	Zea mays	p-nitrophenol + phosphate	-	?

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Release 2023.1 (January 2023)