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

doi:10.2174/092986609787848081

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^*

^*Corresponding author for this work

Manipal Institute of Regenerative Medicine, Bangalore

Research output: Contribution to journal › Article › peer-review

4 Citations (Scopus)

Abstract

The role of interaction between Asn259 (catalytic domain) with Gln821 (C-terminal domain) in PeptidaseN was investigated. The k_cat 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 language	English
Pages (from-to)	415-422
Number of pages	8
Journal	Protein and Peptide Letters
Volume	16
Issue number	4
DOIs	https://doi.org/10.2174/092986609787848081
Publication status	Published - 01-04-2009

All Science Journal Classification (ASJC) codes

Structural Biology
Biochemistry

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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.",

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AU - Nandi, Dipankar

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N2 - 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.

AB - 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.

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

Abstract

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