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Literature summary for 3.4.11.22 extracted from

  • Caprioglio, D.R.
    Yeast aminopeptidases Ape2, Aap1' and Yin7 (2004), Handbook of Proteolytic Enzymes (Barrett, J. ; Rawlings, N. D. ; Woessner, J. F. , eds), 1, 316-318.
No PubMed abstract available
Search for more literature for 3.4.11.22

Cloned(Commentary)

Cloned (Comment) Organism
gene APE2, DNA and amino acid sequence determination and analysis, genetic structure Saccharomyces cerevisiae

Inhibitors

Inhibitors Comment Organism Structure
bestatin strong inhibition Saccharomyces cerevisiae
EDTA
-
 Saccharomyces cerevisiae
Fe2+
-
 Saccharomyces cerevisiae
HgCl2
-
 Saccharomyces cerevisiae
Mg2+
-
 Saccharomyces cerevisiae
additional information no inhibition by nitriloacetic acid Saccharomyces cerevisiae
Zn2+
-
 Saccharomyces cerevisiae

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane glycosylated enzyme form Saccharomyces cerevisiae 16020
-
additional information Ape2 activity is found in allphases of growth Saccharomyces cerevisiae
-
-
periplasmic space glycosylated enzyme form Saccharomyces cerevisiae 42597
-

Metals/Ions

Metals/Ions Comment Organism Structure
Co2+ activates Saccharomyces cerevisiae

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
85000 90000 unglycosylated active enzyme form, gel filtration Saccharomyces cerevisiae
97634
-
 1 * 97634, amino acid sequence calculation Saccharomyces cerevisiae
140000
-
 glycosylated active enzyme form, gel filtration Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Saccharomyces cerevisiae the glycosylated Ape2 aminopeptidase might be responsible for uptake of hydrophobic peptides, especially of leucine N-terminal peptides ?
-
 ?

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein the enzyme exists in a glycosylated and an unglycosylated form, which are both catalytically active Saccharomyces cerevisiae
no glycoprotein the enzyme exists in a glycosylated and an unglycosylated form, which are both catalytically active Saccharomyces cerevisiae

Purification (Commentary)

Purification (Comment) Organism
native enzyme either 331fold by ammonium sulfate fractionation, heat precipitation, gel filtration, ion exchange and adsorption chromatography, or by a single step anion exchange chromatography process Saccharomyces cerevisiae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-Leu-2-naphthylamide + H2O preferred substrate Saccharomyces cerevisiae L-Leu + 2-naphthylamine
-
 ?
L-Leu-4-nitroanilide + H2O preferred substrate Saccharomyces cerevisiae L-Leu + 4-nitroaniline
-
 ?
L-Lys-2-naphthylamide + H2O low activity Saccharomyces cerevisiae L-Lys + 2-naphthylamine
-
 ?
L-Lys-4-nitroanilide + H2O low activity Saccharomyces cerevisiae L-Lys + 4-nitroaniline
-
 ?
additional information the glycosylated Ape2 aminopeptidase might be responsible for uptake of hydrophobic peptides, especially of leucine N-terminal peptides Saccharomyces cerevisiae ?
-
 ?
additional information the enzyme cleaves internal peptide binds in di- and tripeptides with preference for hydrophobic N-terminal amino acids Saccharomyces cerevisiae ?
-
 ?

Subunits

Subunits Comment Organism
monomer 1 * 97634, amino acid sequence calculation Saccharomyces cerevisiae

Synonyms

Synonyms Comment Organism
Ape2 aminopeptidase
-
 Saccharomyces cerevisiae
More the enzyme belongs to the peptidase family M1 Saccharomyces cerevisiae

pI Value

Organism Comment pI Value Maximum pI Value
Saccharomyces cerevisiae sequence calculation
-
 5.7