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

Abstract:

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

journal_name

Protein Pept Lett

authors

Kumar A,Reddy S,Srinivasan N,Nandi D

doi

10.2174/092986609787848081

subject

Has Abstract

pub_date

2009-01-01 00:00:00

pages

415-22

issue

4

eissn

0929-8665

issn

1875-5305

journal_volume

16

pub_type

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