X-His dipeptidase
From Wikipedia the free encyclopedia
| Xaa-His dipeptidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 Aminoacylhistidine dipeptidase monomer, Vibrio alginolyticus | |||||||||
| Identifiers | |||||||||
| EC no. | 3.4.13.3 | ||||||||
| CAS no. | 9027-21-8 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Xaa-His dipeptidase (EC 3.4.13.3, aminoacylhistidine dipeptidase, carnosinase, homocarnosinase, dipeptidase M) is an enzyme.[1][2][3][4] This enzyme catalyses the following chemical reaction
- Hydrolysis of Xaa-His dipeptides
This mammalian cytosolic enzyme also acts on anserine and homocarnosine.
References[edit]
- ^ Hanson HT, Smith EL (June 1949). "Carnosinase; an enzyme of swine kidney". The Journal of Biological Chemistry. 179 (2): 789–801. doi:10.1016/S0021-9258(19)51272-8. PMID 18150012.
- ^ Rosenberg A (December 1960). "The activation of carnosinase by divalent metal ions". Biochimica et Biophysica Acta. 45: 297–316. doi:10.1016/0006-3002(60)91454-2. PMID 13743376.
- ^ Lenney JF, Kan SC, Siu K, Sugiyama GH (November 1977). "Homocarnosinase: a hog kidney dipeptidase with a broader specificity than carnosinase". Archives of Biochemistry and Biophysics. 184 (1): 257–66. doi:10.1016/0003-9861(77)90349-6. PMID 21630.
- ^ Lenney JF (May 1990). "Separation and characterization of two carnosine-splitting cytosolic dipeptidases from hog kidney (carnosinase and non-specific dipeptidase)". Biological Chemistry Hoppe-Seyler. 371 (5): 433–40. doi:10.1515/bchm3.1990.371.1.433. PMID 2378680.
External links[edit]
- Xaa-His+dipeptidase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
