Jun 1, 1975

Substrate specificity of carboxypeptidase from Watermelon

Journal of Biochemistry
T Matoba, E Doi

Abstract

The substrate specificity of carboxypeptidase (F-II) purified from watermelon for various synthetic peptides and esters was examined kinetically. The enzyme showed a broad substrate specificity against various carbobenzoxy- and benzyl-dipeptides. Peptides containing glycine or proline were hydrolyzed slowly by the enzyme. Peptides containing hydrophobic amino acids were hydrolyzed rapidly. The presence of hydrophobic amino acid residues, not only at the C-terminal position but also at the second position and probably the third position from the C-terminal resulted in an increase in the rate of hydrolysis. Inhibition studies with diisopropyl flurophosphate and diastereomers of carbobenzoxy-Phe-Ala demonstrated that the peptidase and esterase activities of the enzyme are both catalyzed by the same site of the enzyme molecule, but the binding sites for peptides and esters seem not to be the same. The enzyme also had amidase activity, which was optimal at pH 7.0.

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Mentioned in this Paper

Carboxy-Terminal Amino Acid
Diuron
Structure-Activity Relationship
Amino Acids, I.V. solution additive
Peptide Hydrolases
Proline
Proteolytic Enzyme
Glycine
Glycine (Plant)
Esterases

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