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Division of Biochemistry and Molecular Biology, University of Glasgow, Glasgow G12 8QQ, UK
Department of Bioscience and Biotechnology, University of Strathclyde, Glasgow G1 1QW, UK
Department of Molecular and Cell Biology, University of Aberdeen, Aberdeen AB9 1AS, UK
4Author for correspondence: John R. Coggins. Tel: +44 141 330 5267. Fax: +44 141 330 4620. e-mail: J.Coggins@bio.gla.ac.uk
ABSTRACT
The tryptophan-sensitive 3-deoxy-D-arabino-heptulosonate-7-phosphate (DAHP) synthases from Streptomyces coelicolor A3(2), Streptomyces rimosus and Neurospora crassa have been purified to homogeneity. All three enzymes have a subunit Mr of 54000. The S. coelicolor DAHP synthase was physically and kinetically characterized and the N-terminal amino acid sequence was obtained. The N-terminal amino acid sequence could not be obtained for the enzymes from S. rimosus and N. crassa, their N-termini apparently being blocked. However, following proteolytic digestion, internal amino acid sequences were obtained from both enzymes. A comparison with the known DAHP synthase sequences indicated that these DAHP synthases are unrelated to other microbial DAHP synthase sequences but are similar to plant DAHP synthases. Up until now, two distinct classes of DAHP synthase have been described, one comprising exclusively enzymes from plants, the other restricted to enzymes from micro-organisms. These studies indicate that the class containing the plant DAHP synthases also contains enzymes from a microbial eukaryote and from several bacteria.
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