INVESTIGATION OF THE ACTIVE-CENTER AND CATALYTIC MECHANISM OF PORCINE KIDNEY AMINOACYLASE - A MODEL OF THE ACTIVE-CENTER

  • 1 January 1980
    • journal article
    • research article
    • Vol. 15  (1) , 29-37
Abstract
Porcine kidney aminoacylase (E.C. 3.5.1.14) is inhibited neither by phenylmethylsulfonylfluoride nor by alkylating agents (iodoacetate or idoacetamide). Reaction mechanisms including the formation of acylenzyme through seryl or cysteinyl side chains are ruled out. The enzyme is a metalloprotein that can be inactivated by EDTA and in which Co2+ is an equivalent substitute for the Zn2+ ion. The 2 SH groups/subunit of aminoacylase exhibit different reactivities to p-hydroxymercuribenzoate. Modification of the less reactive SH group reversibly inactivates the enzyme. This cysteinyl side chain is situated in the active center or in its immediate vicinity. A close similarity between aminoacylase and carboxypeptidase A was proposed with respect to their active center and catalytic mechanism.

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