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Literature summary for 3.4.19.12 extracted from

  • Nishio, K.; Kim, S.W.; Kawai, K.; Mizushima, T.; Yamane, T.; Hamazaki, J.; Murata, S.; Tanaka, K.; Morimoto, Y.
    Crystal structure of the de-ubiquitinating enzyme UCH37 (human UCH-L5) catalytic domain (2009), Biochem. Biophys. Res. Commun., 390, 855-860.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
recombinant UCH37 catalytic domain as N-terminally GST-tagged protein is expressed in Escherichia coli BL21(RIPL) Homo sapiens

Crystallization (Commentary)

Crystallization (Comment) Organism
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 Homo sapiens

Protein Variants

Protein Variants Comment Organism
C88A mutant structure determination and comparison to the wild-type enzyme Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens Q9Y5K5
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant N-terminally GST-tagged UCH37 catalytic domain from Escherichia coli BL21(RIPL) by glutathione affinity chromatography, proteolytic removal of the GST-tag, and gel filtration Homo sapiens

Subunits

Subunits Comment Organism
More the catalytic domain, the UCH-domain, i.e. UCH37N, of UCH37 comprises residues 1-228 residues. UCH37N is composed of a central six-stranded anti-parallel beta-sheet, with seven alpha-helices on either side of the sheet causing it to form a bilobal structure, loop and active site structures, overview Homo sapiens

Synonyms

Synonyms Comment Organism
UCH-L5
-
Homo sapiens
UCH37
-
Homo sapiens