ML-323

Description	in vitro: ML323 probably exerts its inhibitory effect through an allosteric mechanism. The measured inhibition constants of ML323 for the free enzyme (Ki) and the enzyme-substrate complex (K′i) were 68 nM and 183 nM, respectively, which is in accordance with the IC50 determination. ML323 showed little to no inhibition against the USPs tested, including USP2, USP5, USP7, USP8, USP10, USP11, USP14 and USP21. Notably, ML323 did not inhibit the USP46-UAF1 complex that contains the same UAF1 subunit as the USP1-UAF1 complex and demonstrated little inhibition against USP1 alone (IC50 > 200 μM) in a Ub-Rho assay in which USP1-UAF1 and USP1 demonstrated similar Km values. Furthermore, ML323 displayed little to no inhibition against DUBs in the ubiquitin C-terminal hydrolase (UCH), ovarian tumor protease (OTU) and Machado-Joseph domain (MJD) families and did not inhibit a deSUMOylase, SENP1, and a deneddylase, NEDP1. ML323 inhibits USP1-UAF1 through a mixed inhibition mechanism. inhibition of c
Pathways	Cell Cycle/DNA Damage
Targets	DUB

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