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Literature summary for 3.4.11.22 extracted from

  • Schu, P.
    Aminopeptidase I enzymatic activity (2008), Methods Enzymol., 451, 67-78.
    View publication on PubMed

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