The characterisation of a galactokinase from Streptomyces coelicolor

Tessa Keenan; Rhys Mills; Emily Pocock; Darshita Budhadev; Fabio Parmeggiani; Sabine Flitsch; Martin Fascione

doi:10.1016/j.carres.2018.12.005

The characterisation of a galactokinase from Streptomyces coelicolor

Tessa Keenan, Rhys Mills, Emily Pocock, Darshita Budhadev, Fabio Parmeggiani, Sabine Flitsch, Martin Fascione

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Abstract

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.

Original language	English
Pages (from-to)	132-137
Number of pages	5
Journal	Carbohydrate Research
Volume	472
Early online date	14 Dec 2018
DOIs	https://doi.org/10.1016/j.carres.2018.12.005
Publication status	Published - 15 Jan 2019

Keywords

Galactokinase
Sugar-1-phosphates
Streptomyces coelicolor
Substrate specificity

Research Beacons, Institutes and Platforms

Manchester Institute of Biotechnology

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10.1016/j.carres.2018.12.005

ScGalK manuscript 5Dec18_REFAccepted author manuscript, 792 KB

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title = "The characterisation of a galactokinase from Streptomyces coelicolor",

abstract = "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.",

keywords = "Galactokinase, Sugar-1-phosphates, Streptomyces coelicolor, Substrate specificity",

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doi = "10.1016/j.carres.2018.12.005",

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journal = "Carbohydrate Research",

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T1 - The characterisation of a galactokinase from Streptomyces coelicolor

AU - Keenan, Tessa

AU - Mills, Rhys

AU - Pocock, Emily

AU - Budhadev, Darshita

AU - Parmeggiani, Fabio

AU - Flitsch, Sabine

AU - Fascione, Martin

PY - 2019/1/15

Y1 - 2019/1/15

N2 - 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.

AB - 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.

KW - Galactokinase

KW - Sugar-1-phosphates

KW - Streptomyces coelicolor

KW - Substrate specificity

U2 - 10.1016/j.carres.2018.12.005

DO - 10.1016/j.carres.2018.12.005

M3 - Article

SN - 0008-6215

VL - 472

SP - 132

EP - 137

JO - Carbohydrate Research

JF - Carbohydrate Research

ER -

The characterisation of a galactokinase from Streptomyces coelicolor

Abstract

Keywords

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