Porcine carboxypepticase B: Multiple substrates binding modes

Nava Zisapel*, Mordechai Sokolovsky

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review


The kinetics of porcine carboxypeptidase B catalyzed hydrolysis of hippurylarginine, hippurylargininic acid, Z·Ala3 and hippurylphenyllactic acid have been examined in order to elucidate the substrate specificity of the enzyme. Activity toward both basic and non-basic (i.e., hydrophobic type) substrates has been confirmed. However, it would appear that these substrates are not all bound in the same manner to the same site. The pH dependencies of the kinetic parameters revealed characteristic differences among the two types of substrates. Furthermore, inhibition studies with L-argininic acid, e{open}-aminocaproic acid, Z-D-Ala-L-Arg and β-phenylpropionic acid support this postulate. These studies provide insite regarding possible pathways for the evolution of the carboxypeptidases.

Original languageEnglish
Pages (from-to)357-363
Number of pages7
JournalBiochemical and Biophysical Research Communications
Issue number2
StatePublished - 31 Jan 1972


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