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Protein & Peptide Letters


ISSN (Print): 0929-8665
ISSN (Online): 1875-5305

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

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

Volume 16 , Issue 4 , 2009

Page: [415 - 422] Pages: 8

DOI: 10.2174/092986609787848081

Price: $65


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.

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

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