Structural characterization of glycerol kinase from the thermophilic fungus chaetomium thermophilum
| Autor: | Elżbieta Wątor, Piotr Wilk, Klaudia Woś, Piotr H. Malecki, Grzegorz Dubin, Piotr Tokarz, Przemyslaw Grudnik, Katarzyna Kuśka |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2020 |
| Předmět: |
0301 basic medicine
Glycerol kinase crystal structure glycerol Chaetomium Molecular Dynamics Simulation Article Catalysis lcsh:Chemistry Fungal Proteins Inorganic Chemistry 03 medical and health sciences chemistry.chemical_compound 0302 clinical medicine Chaetomium thermophilum Catalytic Domain Enzyme Stability Glycerol Physical and Theoretical Chemistry glycerol kinase lcsh:QH301-705.5 Molecular Biology Spectroscopy chemistry.chemical_classification glycerol-3-phosphate biology Thermophile Organic Chemistry General Medicine ADPGK biology.organism_classification glycerol metabolism ADP-dependent glucokinase Computer Science Applications 030104 developmental biology Enzyme lcsh:Biology (General) lcsh:QD1-999 chemistry Biochemistry ddc:540 Glycerol 3-phosphate 030217 neurology & neurosurgery Bacteria Archaea |
| Zdroj: | International Journal of Molecular Sciences, 21 (24) International journal of molecular sciences 21(24), 9570-(2020). doi:10.3390/ijms21249570 International Journal of Molecular Sciences Volume 21 Issue 24 International Journal of Molecular Sciences, Vol 21, Iss 9570, p 9570 (2020) |
| ISSN: | 1422-0067 |
| Popis: | Glycerol is an organic compound that can be utilized as an alternative source of carbon by various organisms. One of the ways to assimilate glycerol by the cell is the phosphorylative catabolic pathway in which its activation is catalyzed by glycerol kinase (GK) and glycerol-3-phosphate (G3P) is formed. To date, several GK crystal structures from bacteria, archaea, and unicellular eukaryotic parasites have been solved. Herein, we present a series of crystal structures of GK from Chaetomium thermophilum (CtGK) in apo and glycerol-bound forms. In addition, we show the feasibility of an ADP-dependent glucokinase (ADPGK)-coupled enzymatic assay to measure the CtGK activity. New structures described in our work provide structural insights into the GK catalyzed reaction in the filamentous fungus and set the foundation for understanding the glycerol metabolism in eukaryotes. © 2020 by the authors. Licensee MDPI, Basel, Switzerland. International Journal of Molecular Sciences, 21 (24) ISSN:1422-0067 |
| Databáze: | OpenAIRE |
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