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Literature summary for 3.4.16.5 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
Search for more literature for 3.4.16.5

Protein Variants

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

Inhibitors

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

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/ Products (Substrates)

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

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Posttranslational Modification

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 and Products (Substrate)

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 ?
-
 ?