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Literature summary 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

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.4.11.2 gene AAP1', DNA and amino acid sequence determination and analysis, genetic structure, overview Saccharomyces cerevisiae
3.4.11.22 gene APE2, DNA and amino acid sequence determination and analysis, genetic structure Saccharomyces cerevisiae

Protein Variants

EC Number Protein Variants Comment Organism
3.4.11.2 additional information enzyme overexpression leads to increased enzyme activity, glycogen accumulation, and upregulation of the HSP70 gene SSA3, gene disruption reduces the glycogen accumulation ability Saccharomyces cerevisiae

Inhibitors

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

Localization

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

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.4.11.2 Zn2+ required for activity, best at 0.05 mM Saccharomyces cerevisiae
3.4.11.22 Co2+ activates Saccharomyces cerevisiae

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.4.11.2 97634
-
 x * 97634, sequence calculation Saccharomyces cerevisiae
3.4.11.22 85000 90000 unglycosylated active enzyme form, gel filtration Saccharomyces cerevisiae
3.4.11.22 97634
-
 1 * 97634, amino acid sequence calculation Saccharomyces cerevisiae
3.4.11.22 140000
-
 glycosylated active enzyme form, gel filtration Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

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

Organism

EC Number Organism UniProt Comment Textmining
3.4.11.2 Saccharomyces cerevisiae
-
 gene AAP1'
-
3.4.11.22 Saccharomyces cerevisiae
-
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.4.11.2 glycoprotein the enzyme possesses 4 potential N-glycosylation sites Saccharomyces cerevisiae
3.4.11.22 glycoprotein the enzyme exists in a glycosylated and an unglycosylated form, which are both catalytically active Saccharomyces cerevisiae
3.4.11.22 no glycoprotein the enzyme exists in a glycosylated and an unglycosylated form, which are both catalytically active Saccharomyces cerevisiae

Purification (Commentary)

EC Number Purification (Comment) Organism
3.4.11.22 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)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.11.2 L-Ala-2-naphthylamide + H2O preferred substrate Saccharomyces cerevisiae L-Ala + 2-naphthylamine
-
 ?
3.4.11.2 L-Arg-2-naphthylamide + H2O
-
 Saccharomyces cerevisiae L-Arg + 2-naphthylamine
-
 ?
3.4.11.2 additional information no activity with N-terminal Leu-substrates Saccharomyces cerevisiae ?
-
 ?
3.4.11.22 L-Leu-2-naphthylamide + H2O preferred substrate Saccharomyces cerevisiae L-Leu + 2-naphthylamine
-
 ?
3.4.11.22 L-Leu-4-nitroanilide + H2O preferred substrate Saccharomyces cerevisiae L-Leu + 4-nitroaniline
-
 ?
3.4.11.22 L-Lys-2-naphthylamide + H2O low activity Saccharomyces cerevisiae L-Lys + 2-naphthylamine
-
 ?
3.4.11.22 L-Lys-4-nitroanilide + H2O low activity Saccharomyces cerevisiae L-Lys + 4-nitroaniline
-
 ?
3.4.11.22 additional information the glycosylated Ape2 aminopeptidase might be responsible for uptake of hydrophobic peptides, especially of leucine N-terminal peptides Saccharomyces cerevisiae ?
-
 ?
3.4.11.22 additional information the enzyme cleaves internal peptide binds in di- and tripeptides with preference for hydrophobic N-terminal amino acids Saccharomyces cerevisiae ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.4.11.2 ? x * 97634, sequence calculation Saccharomyces cerevisiae
3.4.11.22 monomer 1 * 97634, amino acid sequence calculation Saccharomyces cerevisiae

Synonyms

EC Number Synonyms Comment Organism
3.4.11.2 Aap 1' aminopeptidase
-
 Saccharomyces cerevisiae
3.4.11.2 Aap1 aminopeptidase
-
 Saccharomyces cerevisiae
3.4.11.2 Aap1'
-
 Saccharomyces cerevisiae
3.4.11.2 alanine/arginine aminopeptidase
-
 Saccharomyces cerevisiae
3.4.11.2 More the enzyme belongs to the M1 peptidase family Saccharomyces cerevisiae
3.4.11.22 Ape2 aminopeptidase
-
 Saccharomyces cerevisiae
3.4.11.22 More the enzyme belongs to the peptidase family M1 Saccharomyces cerevisiae

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.4.11.2 7.5
-
 assay at Saccharomyces cerevisiae

pI Value

EC Number Organism Comment pI Value Maximum pI Value
3.4.11.2 Saccharomyces cerevisiae sequence calculation
-
 5.1
3.4.11.22 Saccharomyces cerevisiae sequence calculation
-
 5.7