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Literature summary extracted from

  • Jung, G.; Ueno, H.; Hayashi, R.
    Carboxypeptidase Y: structural basis for protein sorting and catalytic triad (1999), J. Biochem., 126, 1-6.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
3.4.16.5 N87I mutant enzyme with reduced transport rate and reduced enzymatic activity, 30% Saccharomyces cerevisiae

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.16.5 Ag+
-
 Saccharomyces cerevisiae
3.4.16.5 benzyloxycarbonyl-L-phenylalanine chloromethyl ketone
-
 Saccharomyces cerevisiae
3.4.16.5 Cu+
-
 Saccharomyces cerevisiae
3.4.16.5 diisopropyl fluorophosphate
-
 Saccharomyces cerevisiae
3.4.16.5 Hg2+
-
 Saccharomyces cerevisiae
3.4.16.5 PMSF
-
 Saccharomyces cerevisiae

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.4.16.5 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/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.4.16.5 additional information Saccharomyces cerevisiae the enzyme is involved in the C-terminal processing of peptides and proteins ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.4.16.5 Saccharomyces cerevisiae
-
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.4.16.5 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
3.4.16.5 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 and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.16.5 additional information the enzyme is involved in the C-terminal processing of peptides and proteins Saccharomyces cerevisiae ?
-
 ?