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Literature summary for 3.4.11.15 extracted from

  • Nakai, T.; Yasuhara, T.
    Aminopeptidase Y (2004), Handbook of proteolytic enzymes (Barrett, A. J. , Rawlings, N. D. , Woessner, J. F. , eds. ) Academic Press, 1, 956-957.
No PubMed abstract available
Search for more literature for 3.4.11.15

Inhibitors

Inhibitors Comment Organism Structure
1,10-phenanthroline
-
 Saccharomyces cerevisiae
amastatin
-
 Saccharomyces cerevisiae
bestatin
-
 Saccharomyces cerevisiae
Co2+ 25fold enhancement of hydrolysis of Arg-7-amido-4-methylcoumarin and Lys-7-amido-4-methylcoumarin. Hydrolysis of substrates longer than tripeptide or dipeptide-7-amido-4-methylcoumarin is inhibited, IC50: 0.1 mM Saccharomyces cerevisiae
DTT
-
 Saccharomyces cerevisiae
EDTA
-
 Saccharomyces cerevisiae

Localization

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

Metals/Ions

Metals/Ions Comment Organism Structure
Co2+ 25fold enhancement of hydrolysis of Arg-7-amido-4-methylcoumarin and Lys-7-amido-4-methylcoumarin. Hydrolysis of substrates longer than tripeptide or dipeptide-7-amido-4-methylcoumarin is inhibited Saccharomyces cerevisiae
Zinc contains about one atom of zinc per molecule Saccharomyces cerevisiae

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
70000
-
-
 Saccharomyces cerevisiae

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein high-mannose-type sugar chains Saccharomyces cerevisiae
proteolytic modification the aminopeptidase Y gene encodes a 56 residue prepro sequence. the first 21 residues form a hydrophobic stretch that may function as a signal sequence for the endoplasmic reticulum, and the remaining 35 residue segment accounts for the 4000 Da difference between the proform and mature aminopeptidase Y Saccharomyces cerevisiae

Purification (Commentary)

Purification (Comment) Organism
-
 Saccharomyces cerevisiae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Ala-7-amido-4-methylcoumarin + H2O
-
 Saccharomyces cerevisiae Ala + 7-amino-4-methylcoumarin
-
 ?
Arg-7-amido-4-methylcoumarin + H2O Arg-7-amido-4-methylcoumarin and Lys-7-amido-4-methylcoumarin are the most sensitive substrates. Leu-7-amido-4-methylcoumarin, Met-7-amido-4-methylcoumarin and Ala-7-amido-4-methylcoumarin are next in susceptibility to hydrolysis, followed by Ser-7-amido-4-methylcoumarin, Phe-7-amido-4-methylcoumarin, Tyr-7-amido-4-methylcoumarin and Pro-7-amido-4-methylcoumarin Saccharomyces cerevisiae Arg + 7-amino-4-methylcoumarin
-
 ?
Leu-7-amido-4-methylcoumarin + H2O
-
 Saccharomyces cerevisiae Leu + 7-amino-4-methylcoumarin
-
 ?
Lys-7-amido-4-methylcoumarin + H2O
-
 Saccharomyces cerevisiae Lys + 7-amino-4-methylcoumarin
-
 ?
Met-7-amido-4-methylcoumarin + H2O
-
 Saccharomyces cerevisiae Met + 7-amino-4-methylcoumarin
-
 ?

Subunits

Subunits Comment Organism
monomer 1 * 70000 Saccharomyces cerevisiae

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
 in presence of cobalt Saccharomyces cerevisiae

pI Value

Organism Comment pI Value Maximum pI Value
Saccharomyces cerevisiae
-
-
 5.2

IC50 Value

IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
0.1
-
 25fold enhancement of hydrolysis of Arg-7-amido-4-methylcoumarin and Lys-7-amido-4-methylcoumarin. Hydrolysis of substrates longer than tripeptide or dipeptide-7-amido-4-methylcoumarin is inhibited, IC50: 0.1 mM Saccharomyces cerevisiae Co2+