Interaction between two residues in the inter-domain interface of escherichia coli peptidase N modulates catalytic activity

Anujith Kumar, Surendranath Reddy, N. Srinivasan, Dipankar Nandi

Research output: Contribution to journalArticle

3 Citations (Scopus)

Abstract

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

Original languageEnglish
Pages (from-to)415-422
Number of pages8
JournalProtein and Peptide Letters
Volume16
Issue number4
DOIs
Publication statusPublished - 01-04-2009

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Structural analysis
Escherichia coli
Catalyst activity
Catalytic Domain
Peptide Hydrolases
peptidase N

All Science Journal Classification (ASJC) codes

  • Structural Biology
  • Biochemistry

Cite this

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Interaction between two residues in the inter-domain interface of escherichia coli peptidase N modulates catalytic activity. / Kumar, Anujith; Reddy, Surendranath; Srinivasan, N.; Nandi, Dipankar.

In: Protein and Peptide Letters, Vol. 16, No. 4, 01.04.2009, p. 415-422.

Research output: Contribution to journalArticle

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