Format

Send to:

Choose Destination
See comment in PubMed Commons below
J Biol Chem. 2003 Mar 7;278(10):7891-6. Epub 2003 Jan 2.

Activity-stability relationships in extremophilic enzymes.

Author information

  • 1Laboratory of Biochemistry, University of Liège, Institute of Chemistry B6, B-4000 Liège-Sart Tilman, Belgium.

Abstract

Psychrophilic, mesophilic, and thermophilic alpha-amylases have been studied as regards their conformational stability, heat inactivation, irreversible unfolding, activation parameters of the reaction, properties of the enzyme in complex with a transition state analog, and structural permeability. These data allowed us to propose an energy landscape for a family of extremophilic enzymes based on the folding funnel model, integrating the main differences in conformational energy, cooperativity of protein unfolding, and temperature dependence of the activity. In particular, the shape of the funnel bottom, which depicts the stability of the native state ensemble, also accounts for the thermodynamic parameters of activation that characterize these extremophilic enzymes, therefore providing a rational basis for stability-activity relationships in protein adaptation to extreme temperatures.

PMID:
12511577
[PubMed - indexed for MEDLINE]
Free full text
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for HighWire
    Loading ...
    Write to the Help Desk