The Zn-peptidase superfamily: functional convergence after evolutionary divergence

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 necessari...

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Bibliographic Details
Published in:Journal of molecular biology 1999-09, Vol.292 (1), p.11-17
Main Authors: Makarova, K S, Grishin, N V
Format: Article
Language:English
Subjects:
Amidohydrolases - chemistry
Amidohydrolases - genetics
Amino Acid Sequence
Aminopeptidases - chemistry
Bacterial Proteins - chemistry
Binding Sites
Carboxypeptidases - chemistry
Evolution, Molecular
Fungal Proteins - chemistry
Humans
Metalloproteins - chemistry
Models, Molecular
Molecular Sequence Data
Sequence Homology, Amino Acid
Space life sciences
Zinc - chemistry
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Summary: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 polypeptide 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.
ISSN:0022-2836
DOI:10.1006/jmbi.1999.3059