Conformational transitions in the active site of mycobacterial 2-oxoglutarate dehydrogenase upon binding phosphonate analogues of 2-oxoglutarate: from a Michaelis-like complex to ThDP adducts.
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DOI: 10.1016/j.jsb.2019.08.012
Abstract: Mycobacterial KGD, the thiamine diphosphate (ThDP)-dependent E1o component of the 2-oxoglutarate dehydrogenase complex (OGDHC), is known to undergo significant conformational changes during catalysis with two distinct conformational states, previously named as the early and late… read more here.
Keywords: thdp; oxoglutarate dehydrogenase; analogues oxoglutarate; phosphonate analogues ... See more keywords