The deubiquitinating enzyme USP9X hydrolyzes the thioester bond between the carboxyl terminus of ubiquitin and cysteine-11 of PEX5L (Grou et al. 2012). The thioester bond is unstable and appears to be also spontaneously (non-enzymatically) disrupted by nucleophilic attack of small metabolites such as reduced glutathione (Grou et al. 2009).
Huybrechts, SJ, Sá-Miranda, C, Grou, CP, Carvalho, AF, Azevedo, JE, Pinto, MP, Fransen, M
Domingues, P, Sá-Miranda, C, Rodrigues, TA, Freitas, MO, Grou, CP, Carvalho, AF, Wood, SA, Azevedo, JE, Pinto, MP, Rodríguez-Borges, JE, Fransen, M, Francisco, T
cysteine-type deubiquitinase activity of USP9X:Ub:PEX5L [cytosol]
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