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Probing the Active Site of Class 3 L-Asparaginase by Mutagenesis: Mutations of the Ser-Lys Tandems of ReAV.

Biomolecules - 29 Jun 2025

Pokrywka Kinga, Grzechowiak Marta, Sliwiak Joanna, Worsztynowicz Paulina, Loch Joanna I, Ruszkowski Milosz, Gilski Miroslaw, Jaskolski Mariusz

Abstract excerpt

The ReAV enzyme from Rhizobium etli, a representative of Class 3 L-asparaginases, is sequentially and structurally different from other known L-asparaginases. This distinctiveness makes ReAV a candidate for novel antileukemic therapies. ReAV is a homodimeric protein, with each subunit containing a highly specific zinc-binding site created by two cysteines, a lysine, and a water molecule. Two Ser-Lys tandems...

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PMID: 40723816
DOI: 10.3390/biom15070944
PMCID: PMC12292245

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