Cloned (Comment) | Organism |
---|---|
gene APE2, DNA and amino acid sequence determination and analysis, genetic structure | Saccharomyces cerevisiae |
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 | 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 | Comment | Organism | Structure |
---|---|---|---|
Co2+ | activates | Saccharomyces cerevisiae |
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 | 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 | UniProt | Comment | Textmining |
---|---|---|---|
Saccharomyces cerevisiae | - |
- |
- |
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 (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 | 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 | Comment | Organism |
---|---|---|
monomer | 1 * 97634, amino acid sequence calculation | Saccharomyces cerevisiae |
Synonyms | Comment | Organism |
---|---|---|
Ape2 aminopeptidase | - |
Saccharomyces cerevisiae |
More | the enzyme belongs to the peptidase family M1 | Saccharomyces cerevisiae |
Organism | Comment | pI Value Maximum | pI Value |
---|---|---|---|
Saccharomyces cerevisiae | sequence calculation | - |
5.7 |