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Zak, K.M. ; Kalińska, M.* ; Wątor, E.* ; Kuśka, K.* ; Krutyhołowa, R.* ; Dubin, G.* ; Popowicz, G.M. ; Grudnik, P.*

Crystal structure of kluyveromyces lactis glucokinase (KlGlk1).

Int. J. Mol. Sci. 20:4821 (2019)
Verlagsversion Forschungsdaten DOI
Open Access Gold
Creative Commons Lizenzvertrag
Glucose phosphorylating enzymes are crucial in the regulation of basic cellular processes, including metabolism and gene expression. Glucokinases and hexokinases provide a pool of phosphorylated glucose in an adenosine diphosphate (ADP)- and ATP-dependent manner to shape the cell metabolism. The glucose processing enzymes from Kluyveromyces lactis are poorly characterized despite the emerging contribution of this yeast strain to industrial and laboratory scale biotechnology. The first reports on K. lactis glucokinase (KlGlk1) positioned the enzyme as an essential component required for glucose signaling. Nevertheless, no biochemical and structural information was available until now. Here, we present the first crystal structure of KlGlk1 together with biochemical characterization, including substrate specificity and enzyme kinetics. Additionally, comparative analysis of the presented structure and the prior structures of lactis hexokinase (KlHxk1) demonstrates the potential transitions between open and closed enzyme conformations upon ligand binding.
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Publikationstyp Artikel: Journalartikel
Dokumenttyp Wissenschaftlicher Artikel
Schlagwörter Kluyveromyces Lactis ; Glucokinase ; Sugar Metabolism; Adp-dependent Glucokinase; Hexokinase Pii; Glucose; Protein; Yeast; Complex; Enzyme; Optimization; Repression; Resolution
ISSN (print) / ISBN 1422-0067
e-ISSN 1661-6596
Quellenangaben Band: 20, Heft: 19, Seiten: , Artikelnummer: 4821 Supplement: ,
Verlag MDPI
Verlagsort Basel
Begutachtungsstatus Peer reviewed