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Crystallization and preliminary X-ray characterization of the 2,4′-dihydroxyacetophenone dioxygenase from

DOI: 10.1107/S2053230X14009649 DOI Help
PMID: 24915102 PMID Help

Authors: G. Beaven (School of Biological Sciences, University of Southampton) , A. Bowyer (University of Southampton) , P. Erskine (Royal Free and University College Medical School) , S. P. Wood (University College London) , A. Mccoy (University of Cambridge) , L. Coates (Oak Ridge National Laboratory) , R. Keegan (Research Complex at Harwell) , A. Lebedev (Science and Technology Facilities Council (STFC)) , D. J. Hopper (Institute of Biological, Environmental and Rural Sciences, Aberystwyth University) , M. A. Kaderbhai (Institute of Biological, Environmental and Rural Sciences, Aberystwyth University) , J. B. Cooper (University College London)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Acta Crystallographica Section F Structural Biology Communications , VOL 70 , PAGES 823 - 826

State: Published (Approved)
Published: June 2014
Diamond Proposal Number(s): 1425 , 7131

Abstract: The enzyme 2,4'-dihydroxyacetophenone dioxygenase (or DAD) catalyses the conversion of 2,4'-dihydroxyacetophenone to 4-hydroxybenzoic acid and formic acid with the incorporation of molecular oxygen. Whilst the vast majority of dioxygenases cleave within the aromatic ring of the substrate, DAD is very unusual in that it is involved in C-C bond cleavage in a substituent of the aromatic ring. There is evidence that the enzyme is a homotetramer of 20.3 kDa subunits each containing nonhaem iron and its sequence suggests that it belongs to the cupin family of dioxygenases. By the use of limited chymotrypsinolysis, the DAD enzyme from Alcaligenes sp. 4HAP has been crystallized in a form that diffracts synchrotron radiation to a resolution of 2.2 Å.

Subject Areas: Biology and Bio-materials


Instruments: I02-Macromolecular Crystallography

Other Facilities: ESRF

Added On: 25/09/2014 15:56

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