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Tuberculosis
Researchers from Texas A&M University report recent findings in tuberculosis
January 27th, 2009
According to a study from the United States, "S-adenosylhomocysteine hydrolase (SAHH) is a ubiquitous enzyme that plays a central role in methylation-based processes by maintaining the intracellular balance between S-adenosylhomocysteine (SAH) and S-adenosylmethionine. We report the first prokaryotic crystal structure of SAHH, from Mycobacterium tuberculosis (Mtb), in complex with adenosine ( ADO) and nicotinamide adenine dinucleotide." "Structures of complexes with three inhibitors are also reported: 3'-keto aristeromycin (ARI), 2-fluoroadenosine, and 3-deazaadenosine. The ARI complex is the first reported structure of SAHH complexed with this inhibitor, and confirms...
Source: TB & Outbreaks Week (2009-01-27)
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