1998
DOI: 10.1021/bi972274d
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Substrate Specificity of Deubiquitinating Enzymes:  Ubiquitin C-Terminal Hydrolases

Abstract: Ubiquitin C-terminal hydrolases (UCH) are deubiquitinating enzymes which hydrolyze C-terminal esters and amides of ubiquitin. Here we report the processing of a number of ubiquitin derivatives by two human UCH isozymes (isozymes L1 and L3) and find that these enzymes show little discrimination based on the P1' amino acid, except that proline is cleaved slowly. Ubiquitinyllysine derivatives linked by the alpha- or epsilon-amino group are hydrolyzed at identical rates. Isozyme-specific hydrolytic preferences are… Show more

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Cited by 381 publications
(328 citation statements)
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“…However, the ability to hydrolyze Lys48 and Lys63 linked chains can be conferred upon UCHL3 through expansion of this loop by the insertion of 5 or 10 glycine residues (201). Two classes of physiological substrate have been proposed, based on in vitro enzymatic analysis (140). 1) The proubiquitin genes in most organisms contain head to tail repeats of the ubiquitin sequence with an additional amino acid or short peptide capping the COOH terminus, which is highly variable between species.…”
Section: B Uch Familymentioning
confidence: 99%
“…However, the ability to hydrolyze Lys48 and Lys63 linked chains can be conferred upon UCHL3 through expansion of this loop by the insertion of 5 or 10 glycine residues (201). Two classes of physiological substrate have been proposed, based on in vitro enzymatic analysis (140). 1) The proubiquitin genes in most organisms contain head to tail repeats of the ubiquitin sequence with an additional amino acid or short peptide capping the COOH terminus, which is highly variable between species.…”
Section: B Uch Familymentioning
confidence: 99%
“…The physiological targets of UCH-L1 are unknown. In vitro, UCH-L1 acts as a C-terminal hydrolase and catalyses the hydrolysis of C-terminal ubiquityl esters and amides (Larsen et al, 1998). In addition, recent evidence suggests that UCH-L1 may have the unique capacity to act both as a deubiquitinating enzyme and as a ubiquitin conjugase, depending on its level of expression and capacity to form enzymatically active homodimers (Liu et al, 2002).…”
Section: The Rescue Program: Lmp-2a and The Capture Of Cellular Ubiqumentioning
confidence: 99%
“…These multiubiquitin chains are suitable substrates for measuring the activity of UBP family of DUB enzymes (Wilkinson et al, 1995). Moreover, the oligomer (UB) 2 is also a good substrate for the UCH-L1 (Larsen et al, 1998), which is one of the most abundant enzyme in the brain, comprising up to 2% of total brain proteins (Leroy et al, 1998).…”
Section: Deubiquitinating Activities Decline During Apoptosismentioning
confidence: 99%