Interaction between two residues in the inter-domain interface of Escherichia coli peptidase N modulates catalytic activity.
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.
Department of Biochemistry, Indian Institute of Science, Bangalore, India 560012.
Anujith
A
Kumar
Surendranath
S
Reddy
N
N
Srinivasan
Dipankar
D
Nandi
D000595:Amino Acid Sequence; D000626:Aminopeptidases / Q000737:chemistry* / Q000378:metabolism; D020134:Catalytic Domain; D004926:Escherichia coli / Q000201:enzymology*; D008958:Models, Molecular; D016297:Mutagenesis, Site-Directed; D013379:Substrate Specificity
D000626:Aminopeptidases; C034113:peptidase N