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TitleHyperthermophilic L-Asparaginase from Thermococcus sibiricus and Its Double Mutant with Increased Activity: Insights into Substrate Specificity and Structure.
Journal, issue, pagesInt J Mol Sci, Vol. 26, Year 2025
Publish dateApr 10, 2025 (structure data deposition date)
AuthorsDumina, M.V. / Zhdanov, D.D. / Veselovsky, A.V. / Pokrovskaya, M.V. / Aleksandrova, S.S. / Minyaev, M.E. / Varfolomeeva, L.A. / Matyuta, I.O. / Boyko, K.M. / Zhgun, A.A.
External linksInt J Mol Sci / PubMed:40564901
MethodsX-ray diffraction
Resolution1.9 Å
Structure data

PDB-9ufq:
Crystal structure of L-asparaginase from Thermococcus Sibiricus
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

PDB-9ufr:
Crystal structure of L-asparaginase from Thermococcus Sibiricus double mutation D54G/T56Q
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

Chemicals

ChemComp-GLY:
GLYCINE

ChemComp-HOH:
WATER

ChemComp-PEG:
DI(HYDROXYETHYL)ETHER

ChemComp-GOL:
GLYCEROL

Source
  • thermococcus sibiricus (archaea)
KeywordsHYDROLASE / L-asparaginase / hyperthermophilic enzyme / thermo-L-asparaginase / TsAI / point mutant / double mutation

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