Next Article in Journal
Predictive Value of Serum Antibodies and Point Mutations of AQP4, AQP1 and MOG in A Cohort of Spanish Patients with Neuromyelitis Optica Spectrum Disorders
Next Article in Special Issue
Crystal Structure of a GH3 β-Glucosidase from the Thermophilic Fungus Chaetomium thermophilum
Previous Article in Journal
Radiochemical Approaches to Imaging Bacterial Infections: Intracellular versus Extracellular Targets
Previous Article in Special Issue
The C-Type Lysozyme from the upper Gastrointestinal Tract of Opisthocomus hoatzin, the Stinkbird
Article

Two Homologous Enzymes of the GalU Family in Rhodococcus opacus 1CP—RoGalU1 and RoGalU2

1
Environmental Microbiology, Institute of Biosciences, TU Bergakademie Freiberg, Leipziger Str. 29, 09599 Freiberg, Germany
2
EMBL Hamburg, Notkestr. 85, 22607 Hamburg, Germany
3
Microbial Biotechnology, Faculty of Biology & Biotechnology, Ruhr University Bochum, Universitätsstr. 150, 44780 Bochum, Germany
*
Authors to whom correspondence should be addressed.
Int. J. Mol. Sci. 2019, 20(22), 5809; https://0-doi-org.brum.beds.ac.uk/10.3390/ijms20225809
Received: 28 October 2019 / Revised: 15 November 2019 / Accepted: 16 November 2019 / Published: 19 November 2019
Uridine-5’-diphosphate (UDP)-glucose is reported as one of the most versatile building blocks within the metabolism of pro- and eukaryotes. The activated sugar moiety is formed by the enzyme UDP-glucose pyrophosphorylase (GalU). Two homologous enzymes (designated as RoGalU1 and RoGalU2) are encoded by most Rhodococcus strains, known for their capability to degrade numerous compounds, but also to synthesize natural products such as trehalose comprising biosurfactants. To evaluate their functionality respective genes of a trehalose biosurfactant producing model organism—Rhodococcus opacus 1CP—were cloned and expressed, proteins produced (yield up to 47 mg per L broth) and initially biochemically characterized. In the case of RoGalU2, the Vmax was determined to be 177 U mg−1 (uridine-5’-triphosphate (UTP)) and Km to be 0.51 mM (UTP), respectively. Like other GalUs this enzyme seems to be rather specific for the substrates UTP and glucose 1-phosphate, as it accepts only dTTP and galactose 1-phoshate in addition, but both with solely 2% residual activity. In comparison to other bacterial GalU enzymes the RoGalU2 was found to be somewhat higher in activity (factor 1.8) even at elevated temperatures. However, RoGalU1 was not obtained in an active form thus it remains enigmatic if this enzyme participates in metabolism. View Full-Text
Keywords: glycosylation; UDP-glucose pyrophosphorylase; UDP-glucose; nucleotide donors; Rhodococcus, Actinobacteria, gene redundancy; Leloir glycosyltransferases; activated sugar; UTP glycosylation; UDP-glucose pyrophosphorylase; UDP-glucose; nucleotide donors; Rhodococcus, Actinobacteria, gene redundancy; Leloir glycosyltransferases; activated sugar; UTP
Show Figures

Figure 1

MDPI and ACS Style

Kumpf, A.; Partzsch, A.; Pollender, A.; Bento, I.; Tischler, D. Two Homologous Enzymes of the GalU Family in Rhodococcus opacus 1CP—RoGalU1 and RoGalU2. Int. J. Mol. Sci. 2019, 20, 5809. https://0-doi-org.brum.beds.ac.uk/10.3390/ijms20225809

AMA Style

Kumpf A, Partzsch A, Pollender A, Bento I, Tischler D. Two Homologous Enzymes of the GalU Family in Rhodococcus opacus 1CP—RoGalU1 and RoGalU2. International Journal of Molecular Sciences. 2019; 20(22):5809. https://0-doi-org.brum.beds.ac.uk/10.3390/ijms20225809

Chicago/Turabian Style

Kumpf, Antje, Anett Partzsch, André Pollender, Isabel Bento, and Dirk Tischler. 2019. "Two Homologous Enzymes of the GalU Family in Rhodococcus opacus 1CP—RoGalU1 and RoGalU2" International Journal of Molecular Sciences 20, no. 22: 5809. https://0-doi-org.brum.beds.ac.uk/10.3390/ijms20225809

Find Other Styles
Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Article Access Map by Country/Region

1
Back to TopTop