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Characterisation of an oxidoreductase from the Arylamine N-acetyltransferase operon in Mycobacterium smegmatis

DOI: 10.1111/j.1742-4658.2011.08382.x DOI Help
PMID: 21972977 PMID Help

Authors: Jim Evangelopoulos (Birkbeck University of London) , Nora Cronin (Institute of Cancer Research) , Tina Daviter (Birkbeck University of London) , Edith Sim (University of Oxford) , Nicholas Keep (Department of Crystallography, Birkbeck College) , Sanjib Bhakta (Birkbeck University of London)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Febs Journal

State: Published (Approved)
Published: October 2011

Abstract: Mycobacterium tuberculosis, the most successful bacterial pathogen, causes tuberculosis, a disease that still causes more than 2 million deaths per year. Arylamine N-acetyltransferase is an enzyme that is conserved in most Mycobacterium spp. The nat gene belongs to an operon that is important for the intracellular survival of M. tuberculosis within macrophages. The nat operon in Mycobacterium smegmatis and other fast-growing mycobacterial species has a unique organization containing genes with uncharacterized function. Here, we describe the biochemical, biophysical and structural characterization of the MSMEG_0308 gene product (MS0308) of the M. smegmatis nat operon. While characterizing the function of MS0308, we validated the oxidoreductase property; however, we found that the enzyme was not utilizing dihydrofolate as its substrate, hence we first report that MS0308 is not a dihydrofolate reductase, as annotated in the genome. The structure of this oxidoreductase was solved at 2.0 Å in complex with the cofactor NADPH and has revealed the hydrophobic pocket where the endogenous substrate binds.

Journal Keywords: Crystallography; X-Ray; Humans; Models; Molecular; Mycobacterium; NADP; Operon; Oxidoreductases; Recombinant; Tetrahydrofolate Dehydrogenase

Subject Areas: Biology and Bio-materials

Instruments: I03-Macromolecular Crystallography

Added On: 10/10/2011 11:29

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