Carboxypeptidase Y

Carboxypeptidase Y is a glycoprotein exopeptidase of the "acid" and "serine" class. Carboxypeptidase Y has a broad amino acid specificity, including proline and amidated amino acid residues. It is active in urea and sodium dodecyl sulfate solutions and can thus act under denaturing conditions in the sequencing of polypeptides.

Carboxypeptidase Y catalyzes the following reaction:

Characteristics of Carboxypeptidase Y from Yeast:

Enzymatic Reaction (image will open in a new window)

Molecular weight: 61,000 (Hayashi, R., et al., 1973 and Kuhn, R., et al., 1973).

Composition: A glycoprotein containing 13 - 15% neutral hexose and 2.6 - 5.2% amino sugar. Unlike carboxypeptidases A and B, contains no metal ion (Johansen, J., Breddam, K. and Ottesen, M., 1976).

Extinction coefficient: = 15.0(Hayashi, R., et al., 1973 and Kuhn, R., et al., 1973).

Stability: Stable in urea. Retains activity in up to 6 M urea. Stable 2 hrs. at 25°C (pH 5.0 - 8.0) and 2 hrs. at 37°C (pH 5.0 - 7.0).

Storage: Store at 2 - 8°C. Do not re-freeze or prolong exposure at room temperature.