Interaction Between Two Residues in the Inter-Domain Interface of Escherichia coli Peptidase N Modulates Catalytic Activity
Authors: Kumar, Anujith; Reddy, Surendranath; Srinivasan, N.; Nandi, Dipankar
Source: Protein and Peptide Letters, Volume 16, Number 4, April 2009 , pp. 415-422(8)
Publisher: Bentham Science Publishers
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.
Document Type: Research Article
Publication date: April 1, 2009
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