Insights into the Distribution and Functional Properties of <scp>l</scp>-Asparaginase in the Archaeal Domain and Characterization of <i>Picrophilus torridus</i> Asparaginase Belonging to the Novel Family Asp2like1
Archana Sharma, Vineeta Kaushik, Manisha Goel
Abstract
asparaginase (PtAsp2like1) was characterized in detail to find its suitability in therapeutics. PtAsp2like1 was a glutaminase-free asparaginase that showed the optimum activity at 80 °C and pH 10.0. The Km of PtAsp2like1 toward substrate l-asparagine was 11.69 mM. This study demonstrates the improved mapping of asparaginases in the archaeal domain, facilitating future focused research on archaeal asparaginases for therapeutic applications.
Topics & Concepts
AsparaginaseAsparagineArchaeaProtein familyBiologyComputational biologyBiochemistryChemistryEnzymeGeneticsGeneLymphoblastic LeukemiaLeukemiaAcute Lymphoblastic Leukemia researchBiochemical and Molecular ResearchFolate and B Vitamins Research