PubMed · 7201478
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D V Phillips, D E Dougherty, A E Smith. Cyclitols in soybean.. https://doi.org/10.1021/jf00111a011
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Numerous studies have reported critical roles for the gut microbiota in obesity. However, the specific microbes that causally contribute to obesity and the underlying mechanisms remain undetermined. Here, we conducted shotgun metagenomic sequencing in a Chinese cohort of 631 obese subjects and 374 normal-weight controls and identified a Megamonas-dominated, enterotype-like cluster enriched in obese subjects. Among this cohort, the presence of Megamonas and polygenic risk exhibited an additive impact on obesity. Megamonas rupellensis possessed genes for myo-inositol degradation, as demonstrated in vitro and in vivo, and the addition of myo-inositol effectively inhibited fatty acid absorption in intestinal organoids. Furthermore, mice colonized with M. rupellensis or E. coli heterologously expressing the myo-inositol-degrading iolG gene exhibited enhanced intestinal lipid absorption, thereby leading to obesity. Altogether, our findings uncover roles for M. rupellensis as a myo-inositol degrader that enhances lipid absorption and obesity, suggesting potential strategies for future obesity management.
myo-Inositol oxygenase (MIOX) is a non-heme diiron oxygenase that cleaves cyclohexane-(1,2,3,5/4,6-hexa)-ol (myo-inositol, MI) to d-glucuronate. Here, we use 2H ENDOR spectroscopy to demonstrate that MI binds to the diiron(II/III) cofactor of MIOX via an alkoxide bridge, most likely involving O1. Analysis shows that MI adopts a symmetrical geometry in which the O-C-2H plane of the bridge is approximately orthogonal to the Fe-O-Fe plane.
[reaction: see text] Phosphatidylinositol-3-phosphate (PtdIns(3)P) is a spatial regulator of vesicular trafficking and other vital cellular processes. We describe the asymmetric total synthesis of a metabolically stabilized analogue, phosphatidylinositol-3-methylenephosphate (PtdIns(3)MP) from a differentially protected myo-inositol. NMR studies of PtdIns(3)MP bound to the (15)N-labeled FYVE domain showed significant (1)H and (15)N chemical shift changes relative to the unliganded protein.