Directed Mutagenesis of Catalytic Residues in L-Asparaginase II from Salmonella paratyphi: Structural, Functional and Stability Analysis Using In-Vitro, Docking and Simulation Studies.
Jul 2026· Applied Biochemistry and Biotechnology· 0 citations· 14 references
Medicine
TL;DR
Findings demonstrate that rational site-directed mutagenesis can effectively enhance both the catalytic efficiency and thermal stability of recSalA and indicate that the introduced mutations preserve the overall protein architecture.
The rational engineering of an α-L-rhamnosidase (DthRha) to address limitations and enhance its performance for flavonoid production highlights the R783A mutant as a robust and thermally stable biocatalyst with great potential for the sustainable production of bioactive flavonoids.
Haoyu Jia, Luran Wang, Tong Yan et al.· International Journal of Bio...· 1 citation
Aspartase from Escherichia coli (AspA) catalyzes the direct conversion of acrylic acid to β-alanine; however, its substrate specificity and low catalytic efficiency limit its broader application. We engineered an AspA mutant capable of efficiently catalyzing the amination of acrylic acid for β-alanine synthesis, using...
Long-Xian Li, Bao-Di Ma, Yi Xu· Catalysts· 0 citations
NMR data, in combination with enzymatic assays using active variants confirmed differences in the active, apo states of these enzymes, and provided additional atomic detail regarding the importance of the P94 residue in saSrtA substrate recognition.
Erich G. Walkenhauer, Noah Cox-Tigre, M. Chaubey et al.· bioRxiv· 0 citations
The C-terminal domain was crucial for folding and dimerization, while H541A/Y542A led to monomeric 1NH with ∼52% activity, providing insights into role of domains and the catalytic mechanism of 1NH.
Tushar Dhamale, S. S. Dhakar, P. Phale· Archives of Biochemistry and...· 0 citations
Hydxymycotrienin A is identified as a promising, bioavailable ‘privileged scaffold’ that offers a non-covalent therapeutic strategy for NSCLC, characterizing Hydroxymycotrienin A as a promising, bioavailable ‘privileged scaffold’ that offers a non-covalent therapeutic strategy.
Adeline Celina Rufus, Sidharth Kumar N, M. Ramasamy et al.· Frontiers in Bioinformatics· 0 citations
An in silico framework to accelerate the rational design of propeptide-based inhibitors and the development of novel therapeutic approaches targeting RgpB is established and a significant increase in the relative binding affinity for the selected variants compared to the wild type is confirmed.
S. Tapia, O. Yáñez, Olimpo García-Beltrán et al.· RSC Advances· 0 citations
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