Structure of dehydroquinate synthase reveals an active site capable of multistep catalysis.

Journal article

Dehydroquinate synthase (DHQS) has long been regarded as a catalytic marvel because of its ability to perform several consecutive chemical reactions in one active site. There has been considerable debate as to whether DHQS is actively involved in all these steps, or whether several steps occur spontaneously, making DHQS a spectator in its own mechanism. DHQS performs the second step in the shikimate pathway, which is required for the synthesis of aromatic compounds in bacteria, microbial euka...

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Authors: Carpenter, E; Hawkins, A; Frost, J; Brown, K

• Publication status: Published
• Journal: Nature
• Volume: 394
• Issue: 6690
• Pages: 299-302
• Publication date: 1998-07-01
• DOI: 10.1038/28431
• EISSN: 1476-4687
• ISSN: 0028-0836
• Language: English
• Keywords: Lyases; Crystallography, X-Ray; Transferases; Binding Sites; Protein Conformation; Catalysis; Aspergillus nidulans; Hydro-Lyases; Phosphotransferases (Alcohol Group Acceptor); Alcohol Oxidoreductases; Multienzyme Complexes; Phosphorus-Oxygen Lyases; Oxidation-Reduction; Models, Molecular