The Zn-peptidase superfamily: Functional convergence after evolutionary divergence

Kira S. Makarova, Nick V. Grishin

Research output: Contribution to journalArticle

84 Scopus citations

Abstract

Zn-dependent carboxypeptidases (ZnCP) cleave off the C-terminal amino acid residues from proteins and peptides. Here we describe a superfamily that unites classical ZnCP with other enzymes, most of which are known (or likely) to participate in metal-dependent peptide bond cleavage, but not necessarily in polypeytide substrates. It is demonstrated that aspartoacylase (ASP gene) and succinylglutamate desuccinylase (ASTE gene) are members of the ZnCP family. The Zn-binding site along with the structural core of the protein is shown to be conserved between ZnCP and another large family of hydrolases that includes mostly aminopeptidases (ZnAP). Both families (ZnCP and ZnAP) include not only proteases but also enzymes that perform N-deacylation, and enzymes that catalyze N-desuccinylation of amino acids. This is a result of functional convergence that apparently occurred after the divergence of the two families.

Original languageEnglish (US)
Pages (from-to)11-17
Number of pages7
JournalJournal of Molecular Biology
Volume292
Issue number1
DOIs
StatePublished - Sep 10 1999

Keywords

  • Aminopeptidase
  • Aspartoacylase
  • Carboxypeptidase
  • Protease
  • Succinylglutamate desuccinylase

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

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