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Details on Person Members of this largest family of human deubiquitinases (DUB...
| Class:Id | Summation:5689567 |
|---|---|
| _displayName | Members of this largest family of human deubiquitinases (DUB... |
| _timestamp | 2015-04-23 15:26:54 |
| created | [InstanceEdit:5689562] Jupe, Steve, 2015-04-23 |
| literatureReference | [LiteratureReference:5689557] Deubiquitinases as a signaling target of oxidative stress [LiteratureReference:5689570] Reversible inactivation of deubiquitinases by reactive oxygen species in vitro and in cells [LiteratureReference:5689574] Chemistry-based functional proteomics reveals novel members of the deubiquitinating enzyme family [LiteratureReference:5689566] On terminal alkynes that can react with active-site cysteine nucleophiles in proteases |
| modified | [InstanceEdit:5689606] Jupe, Steve, 2015-04-23 |
| text | Members of this largest family of human deubiquitinases (DUBs) are thiol proteases that contain a Cys-His-Asp/Asn catalytic triad in which the Asp/Asn functions to polarize and orient the His, while the His serves as a general acid/base by both priming the catalytic Cys for nucleophilic attack on the (iso)peptide carbonyl carbon and by donating a proton to the lysine epsilon-amino leaving group. The nucleophilic attack of the catalytic Cys on the carbonyl carbon produces a negatively charged transition state that is stabilized by an oxyanion hole composed of hydrogen bond donors. A Cys-carbonyl acyl intermediate ensues and is then hydrolyzed by nucleophilic attack of a water molecule to liberate a protein C-terminal carboxylate and regenerate the enzyme. Thiol protease DUB crystal structures in complex with ubiquitin (Ub) have a highly conserved catalytic dyad/triad structure. Ub binding often causes structural rearrangements necessary for catalysis. Many DUBs are inactivated by oxidation of the catalytic cysteine to sulphenic acid (single bond SOH) (Cotto-Rios et al. 2012, Lee et al. 2013). This can be reversed by reduction with DTT or glutathione. The sulphenic acid can be reduced further irreversibly oxidized to sulphinic acid (single bond SO2H) or sulphonic acid (single bond SO3H). Thiol proteases are reversibly inhibited by Ub C-terminal aldehyde, forming a thio-hemiacetal between the aldehyde group and the active site thiol. They are irreversibly inactivated by alkylation or oxidation of the catalytic cysteine or reaction of the active site thiol on Ub derivatives containing electrophilic groups near the C-terminus of Ub (i.e., Ub-vinylsulfone, -vinylmethyl ester, -chloroethylamine, and -propargylamine) (Borodovsky et al. 2002, Ekkebus et al. 2013). |
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No pathways have been reviewed or authored by Members of this largest family of human deubiquitinases (DUB... (5689567)
