Beta-aspartyl-peptidase
Beta-aspartyl-peptidase (EC 3.4.19.5, beta-aspartyl dipeptidase, beta-aspartyl peptidase, beta-aspartyldipeptidase) is an enzyme.[1] This enzyme catalyses the following chemical reaction
- Cleavage of a beta-linked Asp residue from the N-terminus of a polypeptide
| Beta-aspartyl-peptidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 3.4.19.5 | ||||||||
| CAS number | 37288-74-7 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Other isopeptide bonds, e.g. gamma-glutamyl and beta-alanyl, are not hydrolysed.
References
- Haley EE (1970). "β-Aspartyl peptidase from rat liver". Methods Enzymol. 19: 737–741. doi:10.1016/0076-6879(70)19061-6.
External links
- Beta-aspartyl-peptidase at the US National Library of Medicine Medical Subject Headings (MeSH)
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