The potency, selectivity, and kinetics of asPTP inhibition can be significantly improved by exploring the inhibitory action of a range of biarsenical compounds that differ in interarsenical distance, steric bulk, and electronic structure Q259G - isoform PTPalpha, mutation turns alpha isoform to PTP1B-like enzyme in substrate recognition Q314A substrate-trapping mutant of the HePTP catalytic domain (HePTP residues 44-339), shows 13fold reduced activity compared to the wild type enzyme R112A site-directed mutagenesis, affects inhibition by abietic acid, 3-(3,5-dibromo-4-hydroxybenzoyl)-2-ethylbenzofuran-6-sulfonic acid-[4-(thiazol-2-ylsulfamyl)phenyl]-amide, and 2-[(carboxycarbonyl)amino]-4,5,6,7-tetrahydro-thieno[2,3-c]-pyridine-3-carboxylic acid R221G naturally occurring mutation, identified in primary mediastinal B cell lymphoma (PMBCL) patients, the mutation is located in the P-loop of enzyme PTP1B, catalytically inactive mutant
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[Available from: Jothimani D, Kailasam E, Danielraj S, Nallathambi B, Ramachandran H, Sekar P, et al
