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

Publication ,  Journal Article
Piervincenzi, RT; Chilkoti, A
Published in: Biomolecular engineering
January 2004

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.

Duke Scholars

Published In

Biomolecular engineering

DOI

ISSN

1389-0344

Publication Date

January 2004

Volume

21

Issue

1

Start / End Page

33 / 42

Related Subject Headings

  • alpha-Amylases
  • Swine
  • Structure-Activity Relationship
  • Recombinant Proteins
  • Protein Folding
  • Protein Engineering
  • Protein Denaturation
  • Protein Conformation
  • Protein Binding
  • Peptides
 

Citation

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ICMJE
MLA
NLM
Piervincenzi, R. T., & Chilkoti, A. (2004). Effect of genetic circular permutation near the active site on the activity and stability of an enzyme inhibitor. Biomolecular Engineering, 21(1), 33–42. https://doi.org/10.1016/s1389-0344(03)00080-7
Piervincenzi, Ronald T., and Ashutosh Chilkoti. “Effect of genetic circular permutation near the active site on the activity and stability of an enzyme inhibitor.Biomolecular Engineering 21, no. 1 (January 2004): 33–42. https://doi.org/10.1016/s1389-0344(03)00080-7.
Piervincenzi RT, Chilkoti A. Effect of genetic circular permutation near the active site on the activity and stability of an enzyme inhibitor. Biomolecular engineering. 2004 Jan;21(1):33–42.
Piervincenzi, Ronald T., and Ashutosh Chilkoti. “Effect of genetic circular permutation near the active site on the activity and stability of an enzyme inhibitor.Biomolecular Engineering, vol. 21, no. 1, Jan. 2004, pp. 33–42. Epmc, doi:10.1016/s1389-0344(03)00080-7.
Piervincenzi RT, Chilkoti A. Effect of genetic circular permutation near the active site on the activity and stability of an enzyme inhibitor. Biomolecular engineering. 2004 Jan;21(1):33–42.
Journal cover image

Published In

Biomolecular engineering

DOI

ISSN

1389-0344

Publication Date

January 2004

Volume

21

Issue

1

Start / End Page

33 / 42

Related Subject Headings

  • alpha-Amylases
  • Swine
  • Structure-Activity Relationship
  • Recombinant Proteins
  • Protein Folding
  • Protein Engineering
  • Protein Denaturation
  • Protein Conformation
  • Protein Binding
  • Peptides