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3.4.19.12: ubiquitinyl hydrolase 1

This is an abbreviated version!
For detailed information about ubiquitinyl hydrolase 1, go to the full flat file.

Word Map on EC 3.4.19.12

Reaction

Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal) =

Synonyms

A20, AD-019, AMSH, associated molecule with the SH3-domain of STAM, AT-3, ataxin-3, BAP1, BPLF1, BRCA1-associated protein-1, C-terminal hydrolases UCHL3, C-terminal ubiquitin hydrolase, Cezanne, CGI-70, CYLD, de-ubiquitinating enzyme, deubiquinating isopeptidase T, deubiquitinating enzyme, Doa4, Doa4 ubiquitin hydrolase, Doa4p ubiquitin isopeptidase, DUB, dUCH, EC 3.1.2.15, esterase, ubiquitin thiol-, hydrolase, ubiquitin carboxyl-terminal, hydrolase, ubiquitin carboxyl-terminal (Aplysia californica gene Ap-uch), Iso-T, isopeptidase, isopeptidase T, More, Neuron cytoplasmic protein 9.5, neuronal-specific protein gene product 9.5, OsUCH1, OsUCH2, OsUCH3, OsUCH4, OsUCH5, OTU-1, OTUB1, OTUB2, Otubain-1, Otubain-2, ovarian tumour 1, PA-700 associated isopeptidase, papain-like protease, PGP 9.5, PGP 9.5/UCHL1, PGP9.5, PGP9.5.1, PLP2, PLpro, Ub isopeptidase, ubiquitin C terminal hydrolase 1, ubiquitin C-terminal hydrolase, ubiquitin C-terminal hydrolase (Aplysia californica gene Ap-uch), ubiquitin C-terminal hydrolase 1, ubiquitin C-terminal hydrolase 37, ubiquitin C-terminal hydrolase 8, ubiquitin C-terminal hydrolase isoform L3, ubiquitin C-terminal hydrolase L-1, ubiquitin C-terminal hydrolase L1, ubiquitin C-terminal hydrolase L3, Ubiquitin C-terminal hydrolase UCH37, ubiquitin C-terminal hydrolase-1, ubiquitin C-terminal hydrolase-L1, ubiquitin C-terminal hydrolase-L3, ubiquitin C-terminal hydrolase-L5, ubiquitin C-terminal hydrorase-L1, ubiquitin carboxy terminal hydrolase-L1, ubiquitin carboxy terminal hydrolase-L3, ubiquitin carboxy-terminal hydrolase, ubiquitin carboxy-terminal hydrolase 1, ubiquitin carboxy-terminal hydrolase L1, ubiquitin carboxy-terminal hydrolase-L1, ubiquitin carboxy-terminal hydrolase-L3, ubiquitin carboxyhydrolase L3, ubiquitin carboxyl terminal esterase L1, ubiquitin carboxyl terminal hydrolase 1, ubiquitin carboxyl terminal hydrolase L1, ubiquitin carboxyl terminal hydrolase-L1, ubiquitin carboxyl-terminal hydrolase, ubiquitin carboxyl-terminal hydrolase 1, ubiquitin carboxyl-terminal hydrolase 44, ubiquitin carboxyl-terminal hydrolase isozyme L1, ubiquitin carboxyl-terminal hydrolase L-1, ubiquitin carboxyl-terminal hydrolase L1, ubiquitin carboxyl-terminal hydrolase l3, ubiquitin carboxyl-terminal hydrolase L5, ubiquitin carboxyl-terminal hydrolase-L1, ubiquitin carboxyl-terminal hydrolase-L5, ubiquitin carboxyterminal hydrolase L1, ubiquitin carboxyterminal hydrolase L3, ubiquitin carboxyterminal hydrolase-L1, ubiquitin hydrolase, ubiquitin hydrolase Uch-L1, ubiquitin hydrolase UCH-L3, ubiquitin isopeptidase, Ubiquitin thiolesterase, Ubiquitin thiolesterase L1, Ubiquitin thiolesterase L3, Ubiquitin thiolesterase L4, Ubiquitin thiolesterase L5, ubiquitin-C-terminal hydrolase L1, ubiquitin-carboxyl-terminal hydrolase PGP-9.5, ubiquitin-specific protease 44, UBPY, UCH, UCH L-1, UCH L1, UCH-1, UCH-8, UCH-L1, UCH-L2, UCH-L3, UCH-L4, UCH-L5, UCH37, UCH54, UCHL-1, UCHL-3, UCHL1, UCHL1/PGP 9.5, UCHL2, Uchl3, UCHL5, UCHL5N240, USP19, USP22, USP44, yeast ubiquitin hydrolase, YUH, YUH1

ECTree

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.19 Omega peptidases
                3.4.19.12 ubiquitinyl hydrolase 1

Crystallization

Crystallization on EC 3.4.19.12 - ubiquitinyl hydrolase 1

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
at 2.4 A resolution, x-ray crystallography. Overall fold resembles that of other ubiquitin hydrolases, including UCHL3. Geometry of the catalytic residues in the active site of UCH-L1 is distorted in such a way that the hydrolytic activity appears to be impossible without substrate induced conformational rearrangements
hanging drop vapour diffusion method, 1.45 A resolution crystal structure of human UCH-L3 in complex with the inhibitor ubiquitin vinylmethyl ester
purified recombinant UCH37 catalytic domain, i.e. UCH37N, selenomethionine-substituted UCH37N, and of mutant C88A, sitting-drop vapor diffusion method, 14 mg/ml protein in 25 mM Tris-HCl, pH 7.5, 1 mM DTT, 20°C, versus a reservoir solution containing 22% PEG 4000, 0.2 M MgCl2, 0.1 M Tris-HCl, pH 8.5, and 3.5% xylitol, microseeding, X-ray diffraction structure determination and analysis at 2.2 A resolution
purified recombinant wild-type and mutant GST-tagged enzymes, 35 mg/ml protein in 50 mM Tris-HCl, pH 7.4, 150 mM NaCl, 10 mM DTT, crystallization at room temperature, X-ray diffraction structure determination and analysis at 2.6 A resolution, molecular modeling, structure-function relationship
purified recombinant wild-type UCH-L1 and the Parkinson disease-associated variant of the enzyme, mutant S18Y, bound to a ubiquitin-based suicide substrate, ubiquitin vinyl methyl ester, hanging drop vapour diffusion method, 25 mg/ml enzyme-UbVMe complex in 50 mM Tris-HCl, pH 7.4, 150 mM NaCl, and 10 mM DTT, are mixed with 2.4 M ammonium sulfate and 0.1 M bicine, pH 9.0, 2 months, X-ray diffraction structure determination and analysis at 2.4-2.85 A resolution, molecular replacement
UCH-L3, crystal structure at 1.8 A resolution
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X-ray structure of UCHL1 co-crystallized with a peptide-based fluoromethylketone inhibitor, benzyloxycarbonyl-Val-Ala-Glu(gamma-methoxy) fluoromethylketone (Z-VAE(OMe)-FMK (VAEFMK)), at 2.35 A resolution is reported
hanging drop vapour diffusion method, 3.1 A resolution crystal structure of the PLP2 domain originating from PEDV polyprotein 1a bound to ubiquitin