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Literature summary extracted from

  • Suarez-Rendueles, P.; Bordallo, J.; Cueva, R.
    Aminopeptidase I (2004), Handbook of Proteolytic Enzymes (Barrett, J. ; Rawlings, N. D. ; Woessner, J. F. , eds), 1, 940-941.
No PubMed abstract available

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.4.11.22 gene APE1, DNA and amino acid sequence determination and analysis, transcription is regulated by growth phase and by carbon source Saccharomyces cerevisiae

Protein Variants

EC Number Protein Variants Comment Organism
3.4.11.22 additional information a mutant enzyme is defective in autophagocytosis and vacuole biogenesis Saccharomyces cerevisiae

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.4.11.22 cytosol the zymogen remains in the cytoplasm and does not enter the secretory pathway Saccharomyces cerevisiae 5829
-
3.4.11.22 vacuole the precursor enzyme is transported into the vacuole via the non-classic Cvt pathway by cytoplasmic double-membrane vesicles, which fuse with the vacuole releasing a single-membrane autophagic body into the vacuolar lumen where it is proteolytically maturated, overview Saccharomyces cerevisiae 5773
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.4.11.22 Cl- specific, strong activation Saccharomyces cerevisiae
3.4.11.22 Zn2+ specific, strong activation, 2 mol per mol of enzyme Saccharomyces cerevisiae

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.4.11.22 53000
-
 12 * 53000, active enzyme Saccharomyces cerevisiae
3.4.11.22 640000
-
-
 Saccharomyces cerevisiae

Organism

EC Number Organism UniProt Comment Textmining
3.4.11.22 Saccharomyces cerevisiae
-
 gene APE1
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.4.11.22 additional information the zymogen is unglycosylated Saccharomyces cerevisiae
3.4.11.22 proteolytic modification the inactive zymogen is activated by cleavage through cerevisin in a PEP4-dependent manner Saccharomyces cerevisiae

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.11.22 L-Leu-4-nitroanilide + H2O
-
 Saccharomyces cerevisiae L-Leu + 4-nitroaniline
-
 ?
3.4.11.22 additional information the enzyme prefers substrates with N-terminal leucine or another hydrophobic amino acid residue, and is less active with Gly or charged amino acids at the P1 position Saccharomyces cerevisiae ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.4.11.22 dodecamer 12 * 53000, active enzyme Saccharomyces cerevisiae
3.4.11.22 More dimeric and hexameric enzyme forms are inactive Saccharomyces cerevisiae

Synonyms

EC Number Synonyms Comment Organism
3.4.11.22 aminopeptidase I
-
 Saccharomyces cerevisiae
3.4.11.22 Aminopeptidase III
-
 Saccharomyces cerevisiae
3.4.11.22 aminopeptidase IV
-
 Saccharomyces cerevisiae
3.4.11.22 Aminopeptidase yscI
-
 Saccharomyces cerevisiae
3.4.11.22 LAP IV
-
 Saccharomyces cerevisiae
3.4.11.22 More the enzyme belongs to the peptidase family M18 Saccharomyces cerevisiae

pI Value

EC Number Organism Comment pI Value Maximum pI Value
3.4.11.22 Saccharomyces cerevisiae
-
-
 4.7