Application | Comment | Organism |
---|---|---|
degradation | most likely major intracellular oligopeptidase responsible for the degradation of peptides resulting from nonvacuolar proteolysis | Saccharomyces cerevisiae |
Cloned (Comment) | Organism |
---|---|
- |
Saccharomyces cerevisiae |
Protein Variants | Comment | Organism |
---|---|---|
additional information | prd1-6 mutants with thermolabile saccharolysin activity, prd1::URA3 mutants devoid of the cytoplasmic and mitochondrial activities | Saccharomyces cerevisiae |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
4-hydroxymercuribenzoate | 100% inhibition with 0.1 mM | Saccharomyces cerevisiae | |
Cpp-Ala-Ala-Phe-p-aminobenzoic acid | strongly inhibits | Saccharomyces cerevisiae | |
EDTA | inhibits 50% at 1 mM and 90% at 10 mM, can be efficiently reactivated by the addition of Zn2+, Co2+ and Mn2+ | Saccharomyces cerevisiae | |
HgCl2 | 100% inhibition with 0.01 mM | Saccharomyces cerevisiae | |
additional information | not inhibited by DTT, N-ethylmaleimide, iodoacetic acid or iodoacetamide | Saccharomyces cerevisiae |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.006 | - |
Pz-Pro-Leu-Gly-Pro-D-Arg | - |
Saccharomyces cerevisiae | |
0.029 | - |
Dnp-Pro-Leu-Gly-Pro-Trp-D-Lys | - |
Saccharomyces cerevisiae | |
0.035 | - |
MeOSuc-Ala-Ala-Pro-Met-NHPhNO2 | - |
Saccharomyces cerevisiae | |
0.06 | - |
Bz-Pro-Phe-Arg-NHPhNO2 | - |
Saccharomyces cerevisiae | |
0.085 | - |
Ac-Ala-Ala-Pro-Phe-NHPhNO2 | - |
Saccharomyces cerevisiae | |
0.19 | - |
Ac-Ala-Ala-Pro-Met-NHPhNO2 | - |
Saccharomyces cerevisiae |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
cytosol | - |
Saccharomyces cerevisiae | 5829 | - |
mitochondrion | intermembrane space | Saccharomyces cerevisiae | 5739 | - |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
81800 | - |
- |
Saccharomyces cerevisiae |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Saccharomyces cerevisiae | - |
- |
- |
Purification (Comment) | Organism |
---|---|
250fold by chromatographies | Saccharomyces cerevisiae |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
Ac-Ala-Ala-Pro-Met-NHPhNO2 + H2O | - |
Saccharomyces cerevisiae | ? | - |
? | |
Ac-Ala-Ala-Pro-Phe-NHPhNO2 + H2O | - |
Saccharomyces cerevisiae | ? | - |
? | |
bradykinin + H2O | cleaved at the Phe-Ser bond | Saccharomyces cerevisiae | ? | - |
? | |
Bz-Pro-Phe-Arg-NHPhNO2 + H2O | - |
Saccharomyces cerevisiae | ? | - |
? | |
Dnp-Pro-Leu-Gly-Pro-Trp-D-Lys + H2O | - |
Saccharomyces cerevisiae | ? | - |
? | |
Mcc-Pro-Leu-Gly-Pro-D-Lys(Dnp) + H2O | - |
Saccharomyces cerevisiae | Mcc-Pro-Leu + Gly-Pro-D-Lys(Dnp) | - |
? | |
MeOSuc-Ala-Ala-Pro-Met-NHPhNO2 + H2O | - |
Saccharomyces cerevisiae | ? | - |
? | |
additional information | no cleavage of peptides with a free N-terminus, azocasein and (3H)methylcasein | Saccharomyces cerevisiae | ? | - |
? | |
Pz-Pro-Leu-Gly-Pro-D-Arg + H2O | - |
Saccharomyces cerevisiae | Pz-Pro-Leu + Gly-Pro-D-Arg | - |
? | |
Pz-Pro-Leu-Gly-Pro-D-Arg + H2O | - |
Saccharomyces cerevisiae | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
monomer | - |
Saccharomyces cerevisiae |
Synonyms | Comment | Organism |
---|---|---|
EC 3.4.22.22 | formerly | Saccharomyces cerevisiae |
Prd1 | - |
Saccharomyces cerevisiae |
yscD | - |
Saccharomyces cerevisiae |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
5.5 | - |
with MeOSuc-Ala-Ala-Pro-Met-NHPhNO2 | Saccharomyces cerevisiae |
5.9 | - |
with Ac-Ala-Ala-Pro-Met-NHPhNO2 | Saccharomyces cerevisiae |
7.9 | - |
with Bz-Pro-Phe-Arg-NHPhNO2 | Saccharomyces cerevisiae |