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

Abstract:

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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Publication status:
Published

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Publisher copy:
10.1110/ps.04705404

Authors


Nichols, C More by this author
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Journal:
Protein science : a publication of the Protein Society
Volume:
13
Issue:
8
Pages:
2108-2119
Publication date:
2004-08-05
DOI:
EISSN:
1469-896X
ISSN:
0961-8368
URN:
uuid:1973dd2c-549c-46d9-838c-03d28e454395
Source identifiers:
72620
Local pid:
pubs:72620

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