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In this complex structure, the phenyl side chain of F812 is shifted 3.7 A away from the active site pocket D811E/C842S site-directed mutagenesis, analysis of binding structure of substrate Eps15846-854 compared to wild-type enzyme and enzyme PTP1B D92A - site-directed mutagenesis, the D92A mutation causes a 250 to 700fold reduction in phospholipid phosphatase activity of PTEN, the mutation perturbs the structure and function of the active site imposing significantly different impacts on the two activities of PTEN E187C site-directed mutagenesis, altered kinetics compared to the wild-type enzyme E187C/S188C site-directed mutagenesis, altered kinetics compared to the wild-type enzyme F135Y 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 F182H isoform PTP1B, exchange of residue 182 with that of isoform PTPH1, modulation of functionality of catalytic center F182Y site-directed mutagenesis, affects inhibition by abietic acid and 2-[(carboxycarbonyl)amino]-4,5,6,7-tetrahydro-thieno[2,3-c]-pyridine-3-carboxylic acid F183C site-directed mutagenesis, altered kinetics compared to the wild-type enzyme F196Y site-directed mutagenesis, affects inhibition by abietic acid and 2-[(carboxycarbonyl)amino]-4,5,6,7-tetrahydro-thieno[2,3-c]-pyridine-3-carboxylic acid F280Y site-directed mutagenesis, does not affect abietane-type diterpenoids as inhibitors F28A - decreased activity G117E - mutant of PTP-1B, 45% increase in Km-value, decrease in kcat-value G129E - naturally occuring mutation, the Cowden syndrome-associated G129E mutation abrogates the phospholipid phosphatase activity but not the phosphoprotein phosphatase activity of PTEN, the mutation perturbs the structure and function of the active site imposing significantly different impacts on the two activities of PTEN, complete loss of phospholipid phosphatase activity of the G129E PTEN mutant G184C site-directed mutagenesis, altered kinetics compared to the wild-type enzyme G259Q - isoform PTP1B, mutation turns 1B isoform to PTPalpha-like enzyme in substrate recognition G259S site-directed mutagenesis, affects inhibition by 2-[(carboxycarbonyl)amino]-4,5,6,7-tetrahydro-thieno[2,3-c]-pyridine-3-carboxylic acid G259V naturally occurring mutation, identified in primary mediastinal B cell lymphoma (PMBCL) patients, the mutation is located in the Q-loop of enzyme PTP1B, catalytically inactive mutant
