ubiquitinyl hydrolase 1;
ubiquitin C-terminal hydrolase;
yeast ubiquitin hydrolase

Hydrolases;
Acting on peptide bonds (peptidases);
Omega peptidases

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)

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 thiolesterases (EC 3.1.2.15)

1  [PMID:9233788]

Johnston SC, Larsen CN, Cook WJ, Wilkinson KD, Hill CP.

Crystal structure of a deubiquitinating enzyme (human UCH-L3) at 1.8 A resolution.

EMBO. J. 16 (1997) 3787-96.

Homo sapiens [GN:hsa]

HSA: 7345 7347

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, p. 470-472.