Display Settings:

Format

Send to:

Choose Destination
See comment in PubMed Commons below
J Phys Chem B. 2010 Nov 25;114(46):15113-8. doi: 10.1021/jp102820e. Epub 2010 Nov 3.

Rate enhancement of an interfacial biochemical reaction through localization of substrate and enzyme by an adaptor domain.

Author information

  • 1Department of Chemistry and Howard Hughes Medical Institute, The University of Chicago, Chicago, Illinois 60637, USA.

Abstract

This paper describes a model system to characterize the rate enhancement that stems from localization of an enzyme with its substrate. The approach is based on a self-assembled monolayer that presents a substrate for the serine esterase cutinase along with a peptide ligand for an SH2 adaptor domain. The monolayer is treated with a fusion protein of cutinase and the SH2 domain, and the rate for the interfacial reaction is monitored using cyclic voltammetry. The rate is approximately 30-fold greater for monolayers that present the ligand for the SH2 domain than for those that omit the ligand. The rate enhancement is due to the interaction of the adaptor domain with the immobilized ligand. Further, the rate enhancement increases with the densities of both the ligand and the substrate. This example provides a well-defined model system for quantitatively assessing the magnitude of rate enhancement that is possible with colocalization of an enzyme with its substrate and may be particularly significant for understanding the signaling events that rely on enzyme localization at the cell membrane.

PMID:
21047083
[PubMed - indexed for MEDLINE]
PMCID:
PMC2987271
Free PMC Article

Images from this publication.See all images (4)Free text

Figure 1
Figure 2
Figure 3
Figure 4
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for American Chemical Society Icon for PubMed Central
    Loading ...
    Write to the Help Desk