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

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

Volume: 16 Issue: 4

Author(s): Anujith Kumar, Surendranath Reddy, N. Srinivasan and Dipankar Nandi

Affiliation:

Keywords: Aminopeptidase, catalytic activity, M1 family, protein structure, site-specific mutation

Abstract: The role of interaction between Asn259 (catalytic domain) with Gln821 (C-terminal domain) in PeptidaseN was investigated. The kcat 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.

Cite this article as:

Kumar Anujith, Reddy Surendranath, Srinivasan N. and Nandi Dipankar, Interaction Between Two Residues in the Inter-Domain Interface of Escherichia coli Peptidase N Modulates Catalytic Activity, Protein & Peptide Letters 2009; 16 (4) . https://dx.doi.org/10.2174/092986609787848081