Ubiquitinyl hydrolase 1 (EC 3.4.19.12, ubiquitin C-terminal hydrolase, yeast ubiquitin hydrolase) is an enzyme.[1][2] This enzyme catalyses the following chemical reaction
| Ubiquitinyl hydrolase 1 | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.4.19.12 | ||||||||
| CAS no. | 189642-63-5&title= 86480-67-3, 189642-63-5 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
- Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin
This enzyme hydrolyses links to polypeptides smaller than 60 residues faster than those to larger polypeptides.
References
edit- ^ Johnston SC, Larsen CN, Cook WJ, Wilkinson KD, Hill CP (July 1997). "Crystal structure of a deubiquitinating enzyme (human UCH-L3) at 1.8 A resolution". The EMBO Journal. 16 (13): 3787–96. doi:10.1093/emboj/16.13.3787. PMC 1170002. PMID 9233788.
- ^ Wilkinson, K.D.; Rawlings, N.D.; Woessner, J.F. (1998). "Ubiquitin C-terminal hydrolase". In Barrett, A.J. (ed.). Handbook of Proteolytic Enzymes. London: Academic Press. pp. 470–472.
External links
edit- Ubiquitinyl+hydrolase+1 at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
