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Literature summary for 3.4.19.12 extracted from

  • Johnston, S.C.; Larsen, C.N.; Cook, W.J.; Wilkinson, K.D.; Hill, C.P.
    Crystal structure of a deubiquitinating enzyme (human UCH-L3) at 1.8 A resolution (1997), EMBO J., 16, 3787-3796.
    View publication on PubMedView publication on EuropePMC
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Crystallization (Commentary)

Crystallization (Comment) Organism
UCH-L3, crystal structure at 1.8 A resolution Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ubiquitin-peptide + H2O Homo sapiens UCH enzymes may function to regenerate active ubiquitin from adducts with small nuceleophiles ?
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 ?

Organism

Organism UniProt Comment Textmining
Homo sapiens
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-
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Source Tissue

Source Tissue Comment Organism Textmining
brain UCH-L1 Homo sapiens
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hematopoietic cell UCH-L3 Homo sapiens
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ubiquitin-peptide + H2O UCH enzymes may function to regenerate active ubiquitin from adducts with small nuceleophiles Homo sapiens ?
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 ?
ubiquitinyl-peptide + H2O UCH-L3 cleaves peptide extensions of up to 20 residues with high efficiency and low sequence preference Homo sapiens ubiquitin + peptide
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 ?