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Literature summary for 3.4.16.5 extracted from
- Recognition of C-terminal amide groups by (serine) carboxypeptidase Y investigated by site-directed mutagenesis (1994), J. Biol. Chem., 269, 15528-15532.
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 degradation of biologically active peptide amides | ? | - |
? |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Saccharomyces cerevisiae | - |
carboxypeptidase Y | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | Asn51 and Glu145 of carboxypeptidase Y each donate a hydrogen bond to the alpha-carboxylate of peptide substrates. The same groups are involved in the interaction with the C-terminal carboxamide group of peptide amides. Asn51 donates a hydrogen bond to the C=O group of the substrate, and Glu145 (in the charged form) accepts one from the NH2 group of the substrate | Saccharomyces cerevisiae | ? | - |
? | |
| additional information | the enzyme is involved in the degradation of biologically active peptide amides | Saccharomyces cerevisiae | ? | - |
? | |
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