Protein Variants | Comment | Organism |
---|---|---|
N87I | mutant enzyme with reduced transport rate and reduced enzymatic activity, 30% | Saccharomyces cerevisiae |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
Ag+ | - |
Saccharomyces cerevisiae | |
benzyloxycarbonyl-L-phenylalanine chloromethyl ketone | - |
Saccharomyces cerevisiae | |
Cu+ | - |
Saccharomyces cerevisiae | |
diisopropyl fluorophosphate | - |
Saccharomyces cerevisiae | |
Hg2+ | - |
Saccharomyces cerevisiae | |
PMSF | - |
Saccharomyces cerevisiae |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
vacuole | the enzyme is synthesized on ribosomes and sorted into vacuoles. The vacuolar localization signal Gln24-Arg-Pro-Leu27 is loacetd near the NH2-terminus of the propeptide | Saccharomyces cerevisiae | 5773 | - |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | Saccharomyces cerevisiae | the enzyme is involved in the C-terminal processing of peptides and proteins | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Saccharomyces cerevisiae | - |
- |
- |
Posttranslational Modification | Comment | Organism |
---|---|---|
glycoprotein | the enzyme is synthesized as a prepro-form that travels through the endoplasmic reticulum and Golgi to its final destination in vacuoles. Various post-translational events have been identified, e.g. carbohydrate modification and cleavage of the presegments. Core glycosylation occurs to a 67000 Da form called p1-CPY. Oligosaccharide modification is completed to give p2-CPY, 69000 Da, in which 2 N-acetyl-glucosamines and 8-14 mannoses, including a 1 mannosyl-phosphate group are attached | Saccharomyces cerevisiae |
proteolytic modification | the gene for carboxypeptidase Y, PRC1, encodes an inactive pre-pro-enzyme with a 20 residue signal peptide, a 91 residue propeptide and a 421 residue mature region. When the newly synthesized carboxypeptidase Y is translocated to the endoplasmic reticulum membrane, the signal peptide is removed by a signal peptidase. In the lumen of the endoplasmic reticulum, the processed protein undergoes folding. Maturation proceeds in the vacuoles where the pro segment of pro-CPY is cleaved by several vacuolar hydrolases, including proteinase A and proteinase B and aminopeptidase. Proteinase A is considered to be the first step in the activation cascade of proCPY in which the protein is cleaved leaving the C-terminal 35 amino acid residue portion of the pro-segment attached to the mature CPY. Subsequently proteinase B is involved in further processing to leave 5 residues attached to the mature CPY. The reamaining 5 residues are finally removed by aminopeptidase | Saccharomyces cerevisiae |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | the enzyme is involved in the C-terminal processing of peptides and proteins | Saccharomyces cerevisiae | ? | - |
? |