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Interaction Between Two Residues in the Inter-Domain Interface of Escherichia coli Peptidase N Modulates Catalytic Activity

Kumar, Anujith and Reddy, Surendranath and Srinivasan, N and Nandi, Dipankar (2009) Interaction Between Two Residues in the Inter-Domain Interface of Escherichia coli Peptidase N Modulates Catalytic Activity. In: Protein and Peptide Letters, 16 (4). pp. 415-422.

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Abstract

The role of interaction between Asn259 (catalytic domain) with Gln821 (C-terminal domain) in PeptidaseN was investigated. The k(cat) of PeptidaseN containing Asn259Asp or Gln821Glu is enhanced whereas it is suppressed in Asn259AspGln821Glu. Structural analysis shows this interaction to change the relative disposition of active site residues, which modulates catalytic activity.

Item Type: Journal Article
Additional Information: Copyright of this article belongs to Bentham Science Publishers.
Keywords: Aminopeptidase;catalytic activity;M1 family;protein structure;site-specific mutation.
Department/Centre: Division of Biological Sciences > Molecular Biophysics Unit
Depositing User: Id for Latest eprints
Date Deposited: 25 Aug 2009 12:04
Last Modified: 25 Aug 2009 12:04
URI: http://eprints.iisc.ac.in/id/eprint/20423

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