Display Settings:

Format

Send to:

Choose Destination
See comment in PubMed Commons below
FEBS Lett. 1999 Nov 26;462(1-2):7-11.

The mechanism of the alkaline phosphatase reaction: insights from NMR, crystallography and site-specific mutagenesis.

Author information

  • 1Department of Chemistry, Merkert Chemistry Center, Boston College, Chestnut Hill, MA 02467, USA.

Abstract

The proposed double in-line displacement mechanism of Escherichia coli alkaline phosphatase (AP) involving two-metal ion catalysis is based on NMR spectroscopic and X-ray crystallographic studies. This mechanism is further supported by the X-ray crystal structures of the covalent phospho-enzyme intermediate of the H331Q mutant AP and of the transition state complex between the wild-type enzyme and vanadate, a transition state analog. Kinetic and structural studies on several genetically engineered versions of AP illustrate the overall importance of the active site's metal geometry, hydrogen bonding network and electrostatic potential in the catalytic mechanism.

PMID:
10580082
[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 Elsevier Science
    Loading ...
    Write to the Help Desk