Display Settings:

Items per page

Results: 9

1.
FIGURE 1.

FIGURE 1. From: 1-Deoxy-d-xylulose 5-Phosphate Synthase Catalyzes a Novel Random Sequential Mechanism.

The methylerythritol phosphate (MEP) pathway. DMAPP, dimethylallyl pyrophosphate; IPP, isopentenyl pyrophosphate; CDP, cytidine diphosphate.

Leighanne A. Brammer, et al. J Biol Chem. 2011 October 21;286(42):36522-36531.
2.
FIGURE 9.

FIGURE 9. From: 1-Deoxy-d-xylulose 5-Phosphate Synthase Catalyzes a Novel Random Sequential Mechanism.

Pyruvate (A) and d-GAP (B) docked to the active site of D. radiodurans DXP synthase. Each substrate binds to the active site without blocking access of the other (C).

Leighanne A. Brammer, et al. J Biol Chem. 2011 October 21;286(42):36522-36531.
3.
FIGURE 3.

FIGURE 3. From: 1-Deoxy-d-xylulose 5-Phosphate Synthase Catalyzes a Novel Random Sequential Mechanism.

Tryptophan fluorescence emission spectra of Trp-76 DXP synthase with corresponding binding curves for the natural substrates pyruvate (A) and d-GAP (B).

Leighanne A. Brammer, et al. J Biol Chem. 2011 October 21;286(42):36522-36531.
4.
FIGURE 8.

FIGURE 8. From: 1-Deoxy-d-xylulose 5-Phosphate Synthase Catalyzes a Novel Random Sequential Mechanism.

Inhibition of DXP synthase by d-glyceraldehyde. A, the concentration of pyruvate was varied at a fixed concentration of d-GAP (120 μm), with increasing concentrations of glyceraldehyde: 0 (○), 2.5 (●), 5 (□), 10 (■), and 15 (Δ) mm glyceraldehyde. B, the concentration of d-GAP was varied at a fixed concentration of pyruvate (240 μm), with increasing concentrations of glyceraldehyde: 0 (○), 2.5 (●), 10 (□), and 15 (■) mm glyceraldehyde.

Leighanne A. Brammer, et al. J Biol Chem. 2011 October 21;286(42):36522-36531.
5.
FIGURE 7.

FIGURE 7. From: 1-Deoxy-d-xylulose 5-Phosphate Synthase Catalyzes a Novel Random Sequential Mechanism.

Inhibition of DXP synthase by MAP. A, the concentration of pyruvate was varied at a fixed concentration of d-GAP (120 μm), with increasing concentrations of MAP: 0 (○), 2 (●), 5 (□), and 10 (■) μm MAP. B, the concentration of d-GAP was varied at a fixed concentration of pyruvate (240 μm), with increasing concentrations of MAP: 0 (○), 2 (●), 5 (□), 10 (■), and 12 (Δ) μm MAP.

Leighanne A. Brammer, et al. J Biol Chem. 2011 October 21;286(42):36522-36531.
6.
FIGURE 4.

FIGURE 4. From: 1-Deoxy-d-xylulose 5-Phosphate Synthase Catalyzes a Novel Random Sequential Mechanism.

β-Fluoropyruvate and MAP shown as pyruvate mimics in a mechanism requiring ternary complex formation. A, following decarboxylation of β-fluoropyruvate, DXP synthase adopts a “post-decarboxylation” state. B, following formation of the phosphono-2-lactyl-ThDP (PLThDP) intermediate, the enzyme adopts a pre-decarboxylation state. E, ThDP-bound enzyme; Pyr, pyruvate; Pyr*, 2-hydroxyethyl-ThDP; G, d-GAP; E-Pyr-G, catalytically competent ternary complex.

Leighanne A. Brammer, et al. J Biol Chem. 2011 October 21;286(42):36522-36531.
7.
FIGURE 2.

FIGURE 2. From: 1-Deoxy-d-xylulose 5-Phosphate Synthase Catalyzes a Novel Random Sequential Mechanism.

Proposed mechanistic models for DXP synthase. E, ThDP-bound enzyme; Pyr, pyruvate; Pyr*, 2-hydroxyethyl-ThDP; G, d-GAP; E-Pyr-G, catalytically competent ternary complex. A, ordered mechanism where pyruvate binds tightly and essentially irreversibly to DXP synthase (). B, ping-pong mechanism where CO2 liberation occurs prior to d-GAP binding ().

Leighanne A. Brammer, et al. J Biol Chem. 2011 October 21;286(42):36522-36531.
8.
FIGURE 5.

FIGURE 5. From: 1-Deoxy-d-xylulose 5-Phosphate Synthase Catalyzes a Novel Random Sequential Mechanism.

Double reciprocal analysis of initial velocities under conditions where either d-GAP or pyruvate is varied at different fixed concentrations of the co-substrate. Kinetic analyses were performed by varying subsaturating concentrations of d-GAP: 18 (○), 24 (●), 36 (□), 48 (■), 60 (Δ), 72 (▴) μm at varying sub-saturating pyruvate concentrations: 12.3 (○), 24.5 (●), 36.8 (□), 49 (■), 73.5 (Δ), and 98 (▴) μm.

Leighanne A. Brammer, et al. J Biol Chem. 2011 October 21;286(42):36522-36531.
9.
FIGURE 6.

FIGURE 6. From: 1-Deoxy-d-xylulose 5-Phosphate Synthase Catalyzes a Novel Random Sequential Mechanism.

Global non-linear regression analysis of control data for a random sequential mechanism. A–C, random sequential mechanism. B and E, varying d-GAP at fixed pyruvate concentrations: 18.0 (black circles), 24.0 (orange squares), 36.0 (purple triangles), 48.0 (inverted yellow triangles), 60.0 (green diamonds), 72.0 (red sideways triangles), 82.3 (blue sideways triangles), 94.0 (pink circles) μm pyruvate. C and F, varying pyruvate at fixed d-GAP concentrations: 12.3 (black circles), 24.5 (orange squares), 36.8 (purple triangles), 49.0 (yellow inverted triangles), 73.5 (green diamonds), 98.0 (red sideways triangles), 122.5 (blue sideways triangles), and 146.0 (pink circles) μm d-GAP. D–F, random sequential mechanism considering substrate inhibition by d-GAP (nonproductive reaction) and pyruvate (formation of acetolactate).

Leighanne A. Brammer, et al. J Biol Chem. 2011 October 21;286(42):36522-36531.

Display Settings:

Items per page

Supplemental Content

Recent activity

Your browsing activity is empty.

Activity recording is turned off.

Turn recording back on

See more...
Write to the Help Desk