Display Settings:

Format

Send to:

Choose Destination
Proc Natl Acad Sci U S A. 2006 Jun 6;103(23):8697-702. Epub 2006 May 30.

Understanding bistability in complex enzyme-driven reaction networks.

Author information

  • 1Mathematical Biosciences Institute, 231 West 18th Avenue, Ohio State University, Columbus, OH 43210, USA.

Abstract

Much attention has been paid recently to bistability and switch-like behavior that might be resident in important biochemical reaction networks. There is, in fact, a great deal of subtlety in the relationship between the structure of a reaction network and its capacity to engender bistability. In common physicochemical settings, large classes of extremely complex networks, taken with mass action kinetics, cannot give rise to bistability no matter what values the rate constants take. On the other hand, bistable behavior can be induced in those same settings by certain very simple and classical mass action mechanisms for enzyme catalysis of a single overall reaction. We present a theorem that distinguishes between those mass action networks that might support bistable behavior and those that cannot. Moreover, we indicate how switch-like behavior results from a well-studied mechanism for the action of human dihydrofolate reductase, an important anti-cancer target.

PMID:
16735474
[PubMed - indexed for MEDLINE]
PMCID:
PMC1592242
Free PMC Article

Images from this publication.See all images (7)Free text

Fig. 1.
Fig. 2.
Fig. 3.
Fig. 4.
Fig. 5.
Fig. 6.
Fig. 7.
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

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