Literature summary for 3.4.19.12 extracted from

Navarro, M.F.; Carmody, L.; Romo-Fewell, O.; Lokensgard, M.E.; Love, J.J.
Characterizing substrate selectivity of ubiquitin C-terminal hydrolase-L3 using engineered alpha-linked ubiquitin substrates (2014), Biochemistry, 53, 8031-8042.

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Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P15374	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	UCH-L3 hydrolysis rates for the different engineered substrates are very closely correlated to the thermal stabilities of each attached test protein substrate. The thermal stabilities of the engineered substrates are not altered by fusion to ubiquitin. No substrate: alpha-linked, linear di-ubiquitin	Homo sapiens	?	-	?
ubiquitin-B domain of staphylococcal protein-A + H2O	and variants thereof, substrate is expressed as alpha-linked C-terminal fusion to ubiquitin	Homo sapiens	ubiquitin + B domain of staphylococcal protein-A	-	?
ubiquitin-beta1 domain of streptococcal protein G + H2O	and variants thereof, substrate is expressed as alpha-linked C-terminal fusion to ubiquitin	Homo sapiens	ubiquitin + beta1 domain of streptococcal protein G	-	?

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Release 2023.1 (January 2023)