USP9X hydrolyzes Ub:PEX5L yielding PEX5L and Ubiquitin

Stable Identifier
R-HSA-9033491
Type
Reaction [transition]
Species
Homo sapiens
Compartment
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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).

Literature References
PubMed ID Title Journal Year
22371489 Identification of ubiquitin-specific protease 9X (USP9X) as a deubiquitinase acting on ubiquitin-peroxin 5 (PEX5) thioester conjugate

Grou, CP, Francisco, T, Rodrigues, TA, Freitas, MO, Pinto, MP, Carvalho, AF, Domingues, P, Wood, SA, Rodríguez-Borges, JE, Sá-Miranda, C, Fransen, M, Azevedo, JE

J. Biol. Chem. 2012
19208625 Properties of the ubiquitin-pex5p thiol ester conjugate

Grou, CP, Carvalho, AF, Pinto, MP, Huybrechts, SJ, Sá-Miranda, C, Fransen, M, Azevedo, JE

J. Biol. Chem. 2009
Participants
Participates
Catalyst Activity

thiol-dependent ubiquitin-specific protease activity of USP9X:Ub:PEX5L [cytosol]

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