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Revealing substrate promiscuity of 1-deoxy-D-xylulose 5-phosphate synthase.

Org Lett. 2009 Oct 15;11(20):4748-51. doi:10.1021/ol901961q
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摘要


A study of DXP synthase has revealed flexibility in the acceptor substrate binding pocket for nonpolar substrates and has uncovered new details of the catalytic mechanism to show that pyruvate can act as both donor and acceptor substrate.

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原始数据


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