EC Number | Cloned (Comment) | Organism |
---|---|---|
3.4.11.21 | gene YHR113W, located on chromosome VIII, DNA and amino acid sequence determination and analysis | Saccharomyces cerevisiae |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
3.4.11.21 | 1,10-phenanthroline | 33.5% inhibition at 5 mM | Saccharomyces cerevisiae | |
3.4.11.21 | EDTA | 76.1% inhibition at 20 mM | Saccharomyces cerevisiae | |
3.4.11.21 | additional information | poor inhibition by bestatin at 0.2 mM | Saccharomyces cerevisiae |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
3.4.11.21 | 0.064 | - |
angiotensin I | - |
Saccharomyces cerevisiae |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
3.4.11.21 | 56000 | - |
monomer, determined by SDS-PAGE | Saccharomyces cerevisiae |
3.4.11.21 | 680000 | - |
gel filtration | Saccharomyces cerevisiae |
3.4.11.21 | 680000 | - |
native enzyme, dodecamer, determined using a Superose 6 column | Saccharomyces cerevisiae |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.4.11.21 | Saccharomyces cerevisiae | - |
- |
- |
3.4.11.21 | Saccharomyces cerevisiae B-8032 | - |
- |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
3.4.11.21 | aspartyl aminopeptidase is purified from yeast cells, using ultracentrifugation, ammonium sulfate fractionating, and chromatography on a Bio-Gel column, on a Mono Q column, and a Superose 6 column | Saccharomyces cerevisiae |
3.4.11.21 | native enzyme to homogeneity by ultracentrifugation, ammonium sulfate fractionation, anion exchange chromatography, and gel filtration | Saccharomyces cerevisiae |
EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|---|
3.4.11.21 | additional information | - |
angiotensin I: 100%, angiotensin II: 144%, angiotensinogen 1-14: 35%, angiotensin II antipeptide: 116%, N-acetyl-angiotensinogen 1-14: 0%, Tyr-bradykinin: 0%, Ile-Ser-bradykinin: 0%, [sar1,ala8] angiotensin II: 0% | Saccharomyces cerevisiae |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.4.11.21 | angiotensin I + H2O | - |
Saccharomyces cerevisiae | ? | - |
? | |
3.4.11.21 | angiotensin I + H2O | - |
Saccharomyces cerevisiae B-8032 | ? | - |
? | |
3.4.11.21 | angiotensin I + H2O | i.e. Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu | Saccharomyces cerevisiae | Asp + Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu | - |
? | |
3.4.11.21 | angiotensin I + H2O | i.e. Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu | Saccharomyces cerevisiae B-8032 | Asp + Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu | - |
? | |
3.4.11.21 | angiotensin II + H2O | - |
Saccharomyces cerevisiae | ? | - |
? | |
3.4.11.21 | angiotensin II + H2O | - |
Saccharomyces cerevisiae B-8032 | ? | - |
? | |
3.4.11.21 | angiotensin II + H2O | i.e. Asp-Tyr-Arg-Val-Tyr-Ile-His-Pro-Phe, best substrate | Saccharomyces cerevisiae | Asp + angiotensin III | i.e. Tyr-Arg-Val-Tyr-Ile-His-Pro-Phe | ? | |
3.4.11.21 | angiotensin II + H2O | i.e. Asp-Tyr-Arg-Val-Tyr-Ile-His-Pro-Phe, best substrate | Saccharomyces cerevisiae B-8032 | Asp + angiotensin III | i.e. Tyr-Arg-Val-Tyr-Ile-His-Pro-Phe | ? | |
3.4.11.21 | angiotensin II antipeptide + H2O | i.e. Glu-Gly-Val-Thr-Val-His-Pro-Val | Saccharomyces cerevisiae | Glu + Gly-Val-Thr-Val-His-Pro-Val | - |
? | |
3.4.11.21 | angiotensin II antipeptide + H2O | - |
Saccharomyces cerevisiae | ? | - |
? | |
3.4.11.21 | angiotensinogen 1-14 + H2O | i.e. Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu-Leu-Val-Tyr-Ser, low activity | Saccharomyces cerevisiae | Asp + Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu-Leu-Val-Tyr-Ser | - |
? | |
3.4.11.21 | angiotensinogen 1-14 + H2O | - |
Saccharomyces cerevisiae | ? | - |
? | |
3.4.11.21 | additional information | the enzyme is specific for unblocked N-terminal acidic amino acid residues, no activity with N-acetyl-angiotensinogen 1-14, Tyr-bradykinin, Ile-Ser-bradykinin, and [Sar1, Ala8]-angiotensin II, overview | Saccharomyces cerevisiae | ? | - |
? | |
3.4.11.21 | additional information | the enzyme is specific for unblocked N-terminal acidic amino acid residues, no activity with N-acetyl-angiotensinogen 1-14, Tyr-bradykinin, Ile-Ser-bradykinin, and [Sar1, Ala8]-angiotensin II, overview | Saccharomyces cerevisiae B-8032 | ? | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
3.4.11.21 | dodecamer | 12 * 56000, SDS-PAGE | Saccharomyces cerevisiae |
3.4.11.21 | dodecamer | dodecamer comprising 12 identical units | Saccharomyces cerevisiae |
3.4.11.21 | More | peptide mass fingerprinting by MALDI-TOF MS analysis | Saccharomyces cerevisiae |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
3.4.11.21 | Aminopeptidase | - |
Saccharomyces cerevisiae |
3.4.11.21 | aspartyl aminopeptidase | - |
Saccharomyces cerevisiae |
3.4.11.21 | Yhr113w | - |
Saccharomyces cerevisiae |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
3.4.11.21 | 37 | - |
assay at | Saccharomyces cerevisiae |
3.4.11.21 | 37 | - |
activity assay | Saccharomyces cerevisiae |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
3.4.11.21 | additional information | - |
neutral pH-optimum | Saccharomyces cerevisiae |