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000472478 1001_ $$0P:(DE-HGF)0$$aVenskutonytė, Raminta$$b0
000472478 245__ $$aStructural characterization of the microbial enzyme urocanate reductase mediating imidazole propionate production
000472478 260__ $$a[London]$$bNature Publishing Group UK$$c2021
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000472478 520__ $$aThe human microbiome can produce metabolites that modulate insulin signaling. Type 2 diabetes patients have increased circulating concentrations of the microbially produced histidine metabolite, imidazole propionate (ImP) and administration of ImP in mice resulted in impaired glucose tolerance. Interestingly, the fecal microbiota of the patients had increased capacity to produce ImP, which is mediated by the bacterial enzyme urocanate reductase (UrdA). Here, we describe the X-ray structures of the ligand-binding domains of UrdA in four different states, representing the structural transitions along the catalytic reaction pathway of this unexplored enzyme linked to disease in humans. The structures in combination with functional data provide key insights into the mechanism of action of UrdA that open new possibilities for drug development strategies targeting type 2 diabetes.
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000472478 7001_ $$aKoh, Ara$$b1
000472478 7001_ $$aStenström, Olof$$b2
000472478 7001_ $$aKhan, Muhammad Tanweer$$b3
000472478 7001_ $$aLundqvist, Annika$$b4
000472478 7001_ $$0P:(DE-HGF)0$$aAkke, Mikael$$b5
000472478 7001_ $$00000-0002-4871-8818$$aBäckhed, Fredrik$$b6
000472478 7001_ $$00000-0002-5209-3160$$aLindkvist-Petersson, Karin$$b7$$eCorresponding author
000472478 773__ $$0PERI:(DE-600)2553671-0$$a10.1038/s41467-021-21548-y$$gVol. 12, no. 1, p. 1347$$n1$$p1347$$tNature Communications$$v12$$x2041-1723$$y2021
000472478 8564_ $$uhttps://www.nature.com/articles/s41467-021-21548-y
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