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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 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.

Beta-Ala-His+dipeptidase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)

Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)