Literature summary for 3.4.19.12 extracted from

Lee, S.P.; Park, C.M.; Kim, K.S.; Kim, E.; Jeong, M.; Shin, J.Y.; Yun, C.H.; Kim, K.; Chock, P.B.; Chae, H.Z.
Structural and biochemical analyses reveal ubiquitin C-terminal hydrolase-L1 as a specific client of the peroxiredoxin II chaperone (2018), Arch. Biochem. Biophys., 640, 61-74 .

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General Stability

General Stability	Organism
peroxiredoxin II specifically binds to the near-native intermediates (early-unfolding intermediates) of ubiquitin C-terminal hydrolase-L1 to maintain its native state and activity against various stresses rather than preventing deleterious protein aggregation through quaternary structural changes	Rattus norvegicus

Organism

Organism	UniProt	Comment	Textmining
Rattus norvegicus	Q00981	-	-

Synonyms

Synonyms	Comment	Organism
ubiquitin C-terminal hydrolase-L1	-	Rattus norvegicus
UCH-L1	-	Rattus norvegicus

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Release 2023.1 (January 2023)