Home > Publications database > Probing the Active Site of Class 3 L-Asparaginase by Mutagenesis: Mutations of the Ser-Lys Tandems of ReAV > print

001     632962
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100 1 _ |a Pokrywka, Kinga
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245 _ _ |a Probing the Active Site of Class 3 L-Asparaginase by Mutagenesis: Mutations of the Ser-Lys Tandems of ReAV
260 _ _ |a Basel
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520 _ _ |a 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 (Ser48-Lys51, Ser80-Lys263) are located in the close proximity of the metal binding site, with Ser48 hypothesized to be the catalytic nucleophile. To further investigate the catalytic process of ReAV, site-directed mutagenesis was employed to introduce alanine substitutions at residues from the Ser-Lys tandems and at Arg47, located near the Ser48-Lys51 tandem. These mutational studies, along with enzymatic assays and X-ray structure determinations, demonstrated that substitution of each of these highly conserved residues abolished the catalytic activity, confirming their essential role in enzyme mechanism.
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700 1 _ |a Grzechowiak, Marta
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700 1 _ |a Sliwiak, Joanna
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700 1 _ |a Worsztynowicz, Paulina
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700 1 _ |a Loch, Joanna I.
|0 0000-0002-7345-4527
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700 1 _ |a Ruszkowski, Milosz
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700 1 _ |a Gilski, Miroslaw
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700 1 _ |a Jaskolski, Mariusz
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773 _ _ |a 10.3390/biom15070944
|g Vol. 15, no. 7, p. 944 -
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856 4 _ |u https://www.mdpi.com/2218-273X/15/7/944
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