Biology:X-His dipeptidase
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Xaa-His dipeptidase | |||||||||
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Aminoacylhistidine dipeptidase monomer, Vibrio alginolyticus | |||||||||
Identifiers | |||||||||
EC number | 3.4.13.3 | ||||||||
CAS number | 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 | ||||||||
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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
- ↑ "Carnosinase; an enzyme of swine kidney". The Journal of Biological Chemistry 179 (2): 789–801. June 1949. doi:10.1016/S0021-9258(19)51272-8. PMID 18150012.
- ↑ "The activation of carnosinase by divalent metal ions". Biochimica et Biophysica Acta 45: 297–316. December 1960. doi:10.1016/0006-3002(60)91454-2. PMID 13743376.
- ↑ "Homocarnosinase: a hog kidney dipeptidase with a broader specificity than carnosinase". Archives of Biochemistry and Biophysics 184 (1): 257–66. November 1977. doi:10.1016/0003-9861(77)90349-6. PMID 21630.
- ↑ "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. May 1990. doi:10.1515/bchm3.1990.371.1.433. PMID 2378680.
External links
- Xaa-His+dipeptidase at the US National Library of Medicine Medical Subject Headings (MeSH)
Original source: https://en.wikipedia.org/wiki/X-His dipeptidase.
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