Effect of genetic circular permutation near the active site on the activity and stability of an enzyme inhibitor.

Journal Article (Journal Article)

We report here the effect of circular permutation on the structure and function of a model protein tendamistat, a 74 amino acid competitive inhibitor of porcine pancreatic alpha-amylase. The activity and stability of wild type and two permuted tendamistat variants were characterized by measurement of alpha-amylase kinetic and thermodynamic binding parameters and their thermodynamics of unfolding. Our results show that large variations in structure and function can occur upon circularly permuting tendamistat near its active site that are not obvious, a priori, from the structure of the native protein and we propose a structural thermodynamic explanation of the experimental observations.

Full Text

Duke Authors

Cited Authors

  • Piervincenzi, RT; Chilkoti, A

Published Date

  • January 2004

Published In

Volume / Issue

  • 21 / 1

Start / End Page

  • 33 - 42

PubMed ID

  • 14715318

International Standard Serial Number (ISSN)

  • 1389-0344

Digital Object Identifier (DOI)

  • 10.1016/s1389-0344(03)00080-7


  • eng