Beta-Ala-His dipeptidase
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
| 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 | ||||||||
| |||||||||
This enzyme is present in the serum of humans and higher primates.
References
- Lenney JF, George RP, Weiss AM, Kucera CM, Chan PW, Rinzler GS (August 1982). "Human serum carnosinase: characterization, distinction from cellular carnosinase, and activation by cadmium". Clinica Chimica Acta; International Journal of Clinical Chemistry. 123 (3): 221–31. doi:10.1016/0009-8981(82)90166-8. PMID 7116644.
- Jackson MC, Kucera CM, Lenney JF (February 1991). "Purification and properties of human serum carnosinase". Clinica Chimica Acta; International Journal of Clinical Chemistry. 196 (2–3): 193–205. doi:10.1016/0009-8981(91)90073-L. PMID 1903095.
External links
- Beta-Ala-His+dipeptidase at the US National Library of Medicine Medical Subject Headings (MeSH)
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