Literature summary for 3.4.11.22 extracted from

Schu, P.
Aminopeptidase I enzymatic activity (2008), Methods Enzymol., 451, 67-78.

Search for more literature for 3.4.11.22

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
vacuole	-	Saccharomyces cerevisiae	5773	-

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Zn2+	zinc metalloproteinase which is activated by 1 mM Zn2+, zinc is part of the active center polarizing the water molecule, which hydrolyzes the peptide bond	Saccharomyces cerevisiae

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
50000	-	12 * 50000, the active enzyme is a homododecameric complex of about 600 kDa, and dissociation into two hexamers leads to loss of enzymatic activity	Saccharomyces cerevisiae

Organism

Organism	UniProt	Comment	Textmining
Saccharomyces cerevisiae	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
Leu-4-nitroanilide + H2O	best substrate	Saccharomyces cerevisiae	Leu + 4-nitroaniline	-	?
Leu-beta-naphthylamide + H2O	-	Saccharomyces cerevisiae	Leu + beta-naphthylamine	-	?

Subunits

Subunits	Comment	Organism
homododecamer	12 * 50000, the active enzyme is a homododecameric complex of about 600 kDa, and dissociation into two hexamers leads to loss of enzymatic activity	Saccharomyces cerevisiae

Synonyms

Synonyms	Comment	Organism
aminopeptidase I	-	Saccharomyces cerevisiae
APE1	-	Saccharomyces cerevisiae
LAP4	-	Saccharomyces cerevisiae
leucine-aminopeptidase	-	Saccharomyces cerevisiae
YKL103C	-	Saccharomyces cerevisiae
yscI	-	Saccharomyces cerevisiae

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Release 2023.1 (January 2023)