EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
3.4.11.15 | 1,10-phenanthroline | - |
Saccharomyces cerevisiae | |
3.4.11.15 | amastatin | - |
Saccharomyces cerevisiae | |
3.4.11.15 | bestatin | - |
Saccharomyces cerevisiae | |
3.4.11.15 | 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 | |
3.4.11.15 | DTT | - |
Saccharomyces cerevisiae | |
3.4.11.15 | EDTA | - |
Saccharomyces cerevisiae |
EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|---|
3.4.11.15 | vacuole | - |
Saccharomyces cerevisiae | 5773 | - |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
3.4.11.15 | 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 | |
3.4.11.15 | Zinc | contains about one atom of zinc per molecule | Saccharomyces cerevisiae |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
3.4.11.15 | 70000 | - |
- |
Saccharomyces cerevisiae |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.4.11.15 | Saccharomyces cerevisiae | - |
- |
- |
EC Number | Posttranslational Modification | Comment | Organism |
---|---|---|---|
3.4.11.15 | glycoprotein | high-mannose-type sugar chains | Saccharomyces cerevisiae |
3.4.11.15 | 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 |
EC Number | Purification (Comment) | Organism |
---|---|---|
3.4.11.15 | - |
Saccharomyces cerevisiae |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.4.11.15 | Ala-7-amido-4-methylcoumarin + H2O | - |
Saccharomyces cerevisiae | Ala + 7-amino-4-methylcoumarin | - |
? | |
3.4.11.15 | 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 | - |
? | |
3.4.11.15 | Leu-7-amido-4-methylcoumarin + H2O | - |
Saccharomyces cerevisiae | Leu + 7-amino-4-methylcoumarin | - |
? | |
3.4.11.15 | Lys-7-amido-4-methylcoumarin + H2O | - |
Saccharomyces cerevisiae | Lys + 7-amino-4-methylcoumarin | - |
? | |
3.4.11.15 | Met-7-amido-4-methylcoumarin + H2O | - |
Saccharomyces cerevisiae | Met + 7-amino-4-methylcoumarin | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
3.4.11.15 | monomer | 1 * 70000 | Saccharomyces cerevisiae |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
3.4.11.15 | 7.5 | - |
in presence of cobalt | Saccharomyces cerevisiae |
EC Number | Organism | Comment | pI Value Maximum | pI Value |
---|---|---|---|---|
3.4.11.15 | Saccharomyces cerevisiae | - |
- |
5.2 |
EC Number | IC50 Value | IC50 Value Maximum | Comment | Organism | Inhibitor | Structure |
---|---|---|---|---|---|---|
3.4.11.15 | 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+ |