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  Structure and mechanistic implications of a tryptophan synthase quinonoid intermediate

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.

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ChemBioChem_9_2008_1024.pdf (Any fulltext), 671KB
 
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 Creators:
Barends, Thomas1, Author           
Domratcheva, Tatiana1, Author           
Kulik, Victor1, Author           
Blumenstein, Lars1, Author           
Niks, Dimitri, Author
Dunn, Michael F., Author
Schlichting, Ilme1, Author           
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1Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              

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Free keywords: allosterism, enzyme catalysis, protein structures, reactive intermediates, structure-activity relationships
 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.

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Language(s): eng - English
 Dates: 2007-11-182008-03-202008-03-202008-05-05
 Publication Status: Issued
 Pages: 5
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
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Title: ChemBioChem : A European Journal of Chemical Biology
  Other : ChemBioChem
Source Genre: Journal
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Publ. Info: Weinheim, Germany : Wiley-VCH
Pages: - Volume / Issue: 9 (7) Sequence Number: - Start / End Page: 1024 - 1028 Identifier: ISSN: 1439-4227
CoNE: https://pure.mpg.de/cone/journals/resource/110978984568897_1