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Structure and mechanistic implications of a tryptophan synthase quinonoid intermediate

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Barends,  Thomas
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

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Domratcheva,  Tatiana
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

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Kulik,  Victor
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

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Blumenstein,  Lars
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

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Schlichting,  Ilme
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

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Citation

Barends, T., Domratcheva, T., Kulik, V., Blumenstein, L., Niks, D., Dunn, M. F., et al. (2008). Structure and mechanistic implications of a tryptophan synthase quinonoid intermediate. ChemBioChem: A European Journal of Chemical Biology, 9(7), 1024-1028. doi:10.1002/cbic.200700703.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0028-4975-F
Abstract
Way station. Quinonoid intermediates play a key role in the catalytic mechanism of pyridoxal 5′-phosphate (PLP)-dependent enzymes. Whereas structures of other PLP-bound reaction intermediates have been determined, a high-quality structure of a quinonoid species has not been reported. We present the crystal structure of the indoline quinonoid intermediate of tryptophan synthase (see figure) and discuss its implications for the enzymatic mechanism and allosteric regulation.