An analysis of substrate binding interactions in the heme peroxidase enzymes

DOI: 10.1016/j.abb.2010.02.015
PMID: 20206594

Authors: Andrea Gumiero (University of Leicester) , Emma J. Murphy (University of Leicester) , Clive L. Metcalfe (University of Leicester) , Peter C. E. Moody (University of Leicester) , Emma L. Raven (University of Leicester)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Archives Of Biochemistry And Biophysics , VOL 500 (1) , PAGES 13-20

State: Published (Approved)
Published: March 2010
Diamond Proposal Number(s): 310

Abstract: The interactions of heme peroxidase enzymes with their substrates have been studied for many years, but only in the last decade or so has structural information begun to appear. This review looks at crystal structures for a number of heme peroxidases in complex with a number of (mainly organic) substrates. It examines the nature and location of the binding interaction, and explores functional similarities and differences across the family.

Journal Keywords: Enzyme Mechanism

Diamond Keywords: Enzymes

Subject Areas: Biology and Bio-materials, Chemistry, Physics


Instruments: I03-Macromolecular Crystallography , I04-Macromolecular Crystallography

Added On: 15/04/2010 11:18

Discipline Tags:

Structural biology Life Sciences & Biotech

Technical Tags: