EC 3.4.19.12 - Ubiquitinyl hydrolase 1

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IntEnz Enzyme Nomenclature
EC 3.4.19.12

Names

Accepted name:
ubiquitinyl hydrolase 1
Other names:
ubiquitin C-terminal hydrolase
yeast ubiquitin hydrolase
Systematic name:
-

Reaction

Comments:

Links to polypeptides smaller than 60 residues are hydrolysed more readily than those to larger polypeptides. Isoforms exist with quantitatively different specificities, amongst the best known being UCH-L1 and UCH-L3, which are major proteins of the brain of mammals [1]. Inhibited by ubiquitin aldehyde (in which Gly76 is replaced by aminoacetaldehyde). Ubiquitinyl hydrolase 1 is the type example of peptidase family C12, with a similar protein fold to papain and catalytic amino acids Cys, His and Asp. There is a separate family (C19) of enzymes that also hydrolyse ubiquitinyl bonds, and it is thought that all the ubiquitinyl hydrolases are also ubiquitin thioesterases (EC 3.1.2.15).

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , MEROPS , UniPathway
Protein domains and families: PROSITE:PDOC00127
Structural data: CSA , EC2PDB
Gene Ontology: GO:0036459
CAS Registry Numbers: 189642-63-5 86480-67-3
UniProtKB/Swiss-Prot: (562) [show] [UniProt]

References

  1. Johnston, S.C., Larsen, C.N., Cook, W.J., Wilkinson, K.D. and Hill, C.P.
    Crystal structure of a deubiquitinating enzyme (human UCH-L3) at 1.8Å resolution.
    EMBO J. 16: 3787-3796 (1997). [PMID: 9233788]
  2. Wilkinson, K.D.
    Ubiquitin C-terminal hydrolase.
    In: Barrett, A.J., Rawlings, N.D. and Woessner, J.F. (Eds.) Handbook of Proteolytic Enzymes, Academic Press, London, 1998, 470-472

[EC 3.4.19.12 created 2000]