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From the following article

The catalytic cycle of a thiamin diphosphate enzyme examined by cryocrystallography

Georg Wille, Danilo Meyer, Andrea Steinmetz, Erik Hinze, Ralph Golbik & Kai Tittmann

Nature Chemical Biology 2, 324 - 328 (2006) Published online: 7 May 2006 Corrected online: 30 May 2006

doi:10.1038/nchembio788

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Figure 1 - Unfortunately we are unable to provide accessible alternative text for this. If you require assistance to access this image, or to obtain a text description, please contact npg@nature.com

Figure 1

Detection and quantification of covalent ThDP intermediates in POX catalysis by 1H NMR spectroscopy after acid-quench isolation according to5, 12.

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Figure 2

Stereo view of the active site of pyruvate oxidase F479W with the two neighboring cofactors ThDP and FAD and the amino acid residues in close proximity to the reactive C2 carbon atom of ThDP.

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Figure 3

The four reaction intermediates of the cofactor ThDP in pyruvate oxidase.

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Figure 4

Exo-site binding cavity of the substrate pyruvate in the structure of the LThDP-containing enzyme.

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Scheme 1 - Unfortunately we are unable to provide accessible alternative text for this. If you require assistance to access this image, or to obtain a text description, please contact npg@nature.com

Scheme 1

Proposed mechanism of POX catalysis with major intermediates involved in the oxidative decarboxylation of pyruvate.

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