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Crystal structure of Chaetomium thermophilum Glycerol Kinase in complex with substrate in P1 space groupCrystal structure of Chaetomium thermophilum Glycerol Kinase in complex with substrate in P1 space group
Structural highlights
FunctionPublication Abstract from PubMedGlycerol 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. Structural Characterization of Glycerol Kinase from the Thermophilic Fungus Chaetomium thermophilum.,Wilk P, Kuska K, Wator E, Malecki PH, Wos K, Tokarz P, Dubin G, Grudnik P Int J Mol Sci. 2020 Dec 16;21(24). pii: ijms21249570. doi: 10.3390/ijms21249570. PMID:33339113[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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