New structure, new paper!
KlGlk1 glucokinase characterized thanks to support of SBCF!

November 15, 2019

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Structural Biology Core Facility users from Helmholtz Zentrum Munich in Neuherberg and the Małopolska Centre of Biotechnology characterized a novel protein involved in glucose signaling.

As most of you know glucose phosphorylating enzymes are crucial in the regulation of basic cellular processes, including metabolism and gene expression. Glucokinases provide a pool of phosphorylated glucose to control cell metabolism. The glucose processing enzymes from Kluyveromyces lactis are poorly characterized despite the growing interest of industrial and research laboratories in the use of this specific yeast strain.

SBCF users from Helmholtz Zentrum Munich in Neuherberg and the Małopolska Centre of Biotechnology characterized a novel protein involved in glucose signaling. The team of researchers used X-ray crystallography as a main research tool along with a combination of biochemical methods to characterize enzyme kinetics, its substrate specificity, thermal stability and oligomerization state in solution. Structure of this particular enzyme is of high importance due to the use of K. lactis in biotechnology processes.

The research in Krakow was financed from National Science Centre grant no. UMO-2015/19/D/NZ1/02009 and the Homing and Team Tech Core Facility programs from the Foundation for Polish Science (FNP) with the support of the Structural Biology Core Facility.

Link to the full article here. 

Written by Krzysztof Żak