Biophysical and kinetic analysis of wild-type and site-directed mutants of the isolated and native dehydroquinate synthase domain of the AROM protein.

Journal article

Dehydroquinate synthase (DHQS) is the N-terminal domain of the pentafunctional AROM protein that catalyses steps 2 to 7 in the shikimate pathway in microbial eukaryotes. DHQS converts 3-deoxy-D-arabino-heptulosonate-7-phosphate (DAHP) to dehydroquinate in a reaction that includes alcohol oxidation, phosphate beta-elimination, carbonyl reduction, ring opening, and intramolecular aldol condensation. Kinetic analysis of the isolated DHQS domains with the AROM protein showed that for the substrat...

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Authors: Park, A; Lamb, H; Nichols, C; Moore, J; Brown, K

• Publication status: Published
• Journal: Protein science : a publication of the Protein Society
• Volume: 13
• Issue: 8
• Pages: 2108-2119
• Publication date: 2004-08-01
• DOI: 10.1110/ps.04705404
• EISSN: 1469-896X
• ISSN: 0961-8368
• Language: English
• Keywords: Transferases; Amino Acid Substitution; Mutagenesis, Site-Directed; Phosphotransferases (Alcohol Group Acceptor); Multienzyme Complexes; Quinic Acid; Protein Structure, Tertiary; Lyases; Hydro-Lyases; Biophysical Phenomena; Sugar Phosphates; Binding Sites; Kinetics; Calorimetry, Differential Scanning; Substrate Specificity; Phosphorus-Oxygen Lyases; Humans; Biophysics; Animals; Alcohol Oxidoreductases