The purification and characterization of 3-dehydroquinase from Streptomyces coelicolor

White, P.J., Young, J., Hunter, I.S., Nimmo, H.G. and Coggins, J.R. (1990) The purification and characterization of 3-dehydroquinase from Streptomyces coelicolor. Biochemical Journal, 265(3), pp. 735-738. (doi: 10.1042/bj2650735) (PMID:2306211) (PMCID:PMC1133695)

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Abstract

The enzyme 3-dehydroquinase was purified over 4000-fold to homogeneity from Streptomyces coelicolor. The subunit Mr estimated from polyacrylamide-gel electrophoresis in the presence of SDS was 16,000. The native Mr estimated by gel filtration on a Superose 6 column was 209,000, indicating that the enzyme is a large oligomer. The enzyme was found to be extremely thermostable. This stability, along with the structural and kinetic properties of the enzyme, suggest that it is very similar to the quinate-inducible 3-dehydroquinase found in Neurospora crassa and Aspergillus nidulans. This similarity was confirmed by direct N-terminal sequencing.

Item Type:Articles
Status:Published
Refereed:Yes
Glasgow Author(s) Enlighten ID:Nimmo, Professor Hugh and Coggins, Professor John
Authors: White, P.J., Young, J., Hunter, I.S., Nimmo, H.G., and Coggins, J.R.
College/School:College of Medical Veterinary and Life Sciences > Institute of Molecular Cell and Systems Biology
College of Medical Veterinary and Life Sciences > School of Life Sciences
Journal Name:Biochemical Journal
Publisher:Portland Press
ISSN:0264-6021
ISSN (Online):1470-8728

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