Enzyme Cascade with Horseradish Peroxidase Readout for High-Throughput Screening and Engineering of Human Arginase-1.
Sign Up to like & getrecommendations! Published in 2023 at "Analytical chemistry"
DOI: 10.1021/acs.analchem.2c05429
Abstract: We report an enzyme cascade with horseradish peroxidase-based readout for screening human arginase-1 (hArg1) activity. We combined the four enzymes hArg1, ornithine decarboxylase, putrescine oxidase, and horseradish peroxidase in a reaction cascade that generated colorimetric… read more here.
Keywords: enzyme cascade; human arginase; horseradish peroxidase; arginase ... See more keywords
Discovery and Optimization of Rationally Designed Bicyclic Inhibitors of Human Arginase to Enhance Cancer Immunotherapy.
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DOI: 10.1021/acsmedchemlett.0c00058
Abstract: The action of arginase, a metalloenzyme responsible for the hydrolysis of arginine to urea and ornithine, is hypothesized to suppress immune-cell activity within the tumor microenvironment, and thus its inhibition may constitute a means by… read more here.
Keywords: optimization rationally; discovery optimization; inhibitors human; human arginase ... See more keywords
Structural insights into human Arginase-1 pH dependence and its inhibition by the small molecule inhibitor CB-1158
Sign Up to like & getrecommendations! Published in 2019 at "Journal of Structural Biology"
DOI: 10.2210/pdb6q9p/pdb
Abstract: Abstract Arginase-1 is a manganese-dependent metalloenzyme that catalyzes the hydrolysis of L-arginine into L-ornithine and urea. Arginase-1 is abundantly expressed by tumor-infiltrating myeloid cells that promote tumor immunosuppression, which is relieved by inhibition of Arginase-1.… read more here.
Keywords: arginase; dependence; human arginase; abh ... See more keywords