X線結晶構造解析によるL―乳酸脱水素酵素のアロステリック特性の解明

概要

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The three-dimensional structure of allosteric L-lactate dehydrogenase from <I>Bildobacterium longum</I>, the first example of a T-state structure of L-lactate dehydrogenase, has been determined to 2.0Å. A comparative study of this structure with the previously reported R-state structure from <I>Bacillus stearothermophilus</I> has revealed the allosteric activation mechanism of the bacterial L-lactate dehydrogenase. The fructose 1, 6-bisphosphate-induced conformational change at the effector site and the substrate affinity change at the active site are clearly shown at a molecular level. Coupling of these changes can be simply explained by a set of concerted rotations between subunits in the tetramer of the enzyme.
日本結晶学会の論文