The characterisation of a galactokinase from Streptomyces coelicolor.

Autor: Keenan T; Department of Chemistry, University of York, Heslington, York, YO10 5DD, UK. Electronic address: tessa.keenan@york.ac.uk., Mills R; Department of Chemistry, University of York, Heslington, York, YO10 5DD, UK., Pocock E; Department of Chemistry, University of York, Heslington, York, YO10 5DD, UK., Budhadev D; Department of Chemistry, University of York, Heslington, York, YO10 5DD, UK., Parmeggiani F; Manchester Institute of Biotechnology, School of Chemistry, The University of Manchester, 131 Princess Street, Manchester, M1 7DN, UK., Flitsch S; Manchester Institute of Biotechnology, School of Chemistry, The University of Manchester, 131 Princess Street, Manchester, M1 7DN, UK., Fascione M; Department of Chemistry, University of York, Heslington, York, YO10 5DD, UK.
Jazyk: angličtina
Zdroj: Carbohydrate research [Carbohydr Res] 2019 Jan 15; Vol. 472, pp. 132-137. Date of Electronic Publication: 2018 Dec 14.
DOI: 10.1016/j.carres.2018.12.005
Abstrakt: Promiscuous galactokinases (GalKs), which catalyse the ATP dependent phosphorylation of galactose in nature, have been widely exploited in biotechnology for the rapid synthesis of diverse sugar-1-phosphates. This work focuses on the characterisation of a bacterial GalK from Streptomyces coelicolor (ScGalK), which was overproduced in Escherichia coli and shown to phosphorylate galactose. ScGalK displayed a broad substrate tolerance, with activity towards Gal, GalN, Gal3D, GalNAc, Man and L-Ara. Most interestingly, ScGalK demonstrated a high activity over a broad pH and temperature range, suggesting that the enzyme could be highly amenable to multi-enzyme systems.
(Copyright © 2018. Published by Elsevier Ltd.)
Databáze: MEDLINE
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