Organic letters

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

LA Brammer, CF Meyers

文献索引：Brammer, Leighanne A.; Meyers, Caren Freel Organic Letters, 2009 , vol. 11, # 20 p. 4748 - 4751

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被引用次数: 29

摘要

The first enzyme in the MEP pathway (Figure 1), 1-deoxy-d-xylulose 5-phosphate (DXP) synthase, represents a new class of thiamine-dependent enzymes that catalyzes the formation of DXP from pyruvate and d-glyceraldehyde 3-phosphate (d-GAP). This transformation is reminiscent of transketolases and decarboxylases, where a two-carbon intermediate bound to thiamine diphosphate (ThDP) is condensed with an acceptor substrate to generate a new carbon−carbon bond. ...