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

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

The ReAV enzyme from <i>Rhizobium etli</i>, 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 sub...

Full description

Saved in:
Bibliographic Details
Main Authors: Kinga Pokrywka, Marta Grzechowiak, Joanna Sliwiak, Paulina Worsztynowicz, Joanna I. Loch, Milosz Ruszkowski, Miroslaw Gilski, Mariusz Jaskolski
Format: Article
Language:English
Published: MDPI AG 2025-06-01
Series:Biomolecules
Subjects:
hydrolase
amidohydrolase
L-asparaginase
leukemia
metalloprotein
site-directed mutagenesis
Online Access:https://www.mdpi.com/2218-273X/15/7/944
Tags: Add Tag
No Tags, Be the first to tag this record!

Similar Items

Similar Items