Beta-Ala-His dipeptidase
| Beta-Ala-His dipeptidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 3.4.13.20 | ||||||||
| CAS number | 525589-43-9 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Beta-Ala-His dipeptidase (EC 3.4.13.20, serum carnosinase) is an enzyme.[1][2] This enzyme catalyses the following chemical reaction
- Preferential hydrolysis of the beta-Ala!His dipeptide (carnosine), and also anserine, Xaa!His dipeptides and other dipeptides including homocarnosine
This enzyme is present in the serum of humans and higher primates.
References
- ↑ Lenney, J.F.; George, R.P.; Weiss, A.M.; Kucera, C.M.; Chan, P.W.H.; Rinzler, G.S. (1982). "Human serum carnosinase: characterization, distinction from cellular carnosinase, and activation by cadmium". Clin. Chim. Acta. 123: 221–231. PMID 7116644. doi:10.1016/0009-8981(82)90166-8.
- ↑ Jackson, M.C.; Kucera, C.M.; Lenney, J.F. (1991). "Purification and properties of human serum carnosinase". Clin. Chim. Acta. 196 (2-3): 193–206. PMID 1903095. doi:10.1016/0009-8981(91)90073-L.
External links
- Beta-Ala-His dipeptidase at the US National Library of Medicine Medical Subject Headings (MeSH)
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