Fig. 3: BT_1526 produces myo-inositol-phosphate in vitro.
From: Characterization of inositol lipid metabolism in gut-associated Bacteroidetes
a, Proposed mechanism for the MIPS-catalysed NAD-dependent/redox-neutral conversion of G6P to MIP. b, Molybdenum blue assay for detection of MIP. Kinetic analysis of recombinant BT_1526 MIPS using G6P as substrate. c, The crystal structure of BT_1526 MIPS: (i) The monomer subunit, (ii) the tetramer, with cartoon representations to illustrate relative rotations of subunits and (iii) the structure of the MIPS:NAD complex in the cofactor binding site. Letters with numbers indicate the amino acid in the given position in the protein using the one-letter amino acid code. d, Production of inositol lipids during growth in inositol-supplemented minimal medium (‘Glc’, exclusively glucose in medium; ‘Inos:Glc’, 1:1 molar abundance of inositol:glucose). Intensity values for the lipid peak at m/z 781.48, PI-DAG 30:0, measured in lipid extracts from WT and ΔBT_1526 strains grown either in minimal medium with glucose as the carbon source, or a 1:1 mix of myo-inositol:glucose, with n = 2 biological replicates. The inset shows higher y-axis resolution for lipid peaks from the ΔBT_1526 strain.
