USP9X hydrolyzes Ub:PEX5S yielding PEX5S and Ubiquitin

Stable Identifier
Reaction [transition]
Homo sapiens
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The deubiquitinating enzyme USP9X hydrolyzes the thioester bond between the carboxyl terminus of ubiquitin and cysteine-11 of PEX5S (inferred from the large isoform of PEX5L in Grou et al. 2012). The thioester bond is unstable and appears also to be spontaneously disrupted by nucleophilic attack of small metabolites such as reduced glutathione (Grou et al. 2009).

Literature References
PubMed ID Title Journal Year
19208625 Properties of the ubiquitin-pex5p thiol ester conjugate

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

J. Biol. Chem. 2009
22371489 Identification of ubiquitin-specific protease 9X (USP9X) as a deubiquitinase acting on ubiquitin-peroxin 5 (PEX5) thioester conjugate

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

J. Biol. Chem. 2012
Catalyst Activity

cysteine-type deubiquitinase activity of USP9X:Ub:PEX5S [cytosol]

Inferred From
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