Cathepsin V
Appearance
Cathepsin V | |||||||||
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Identifiers | |||||||||
EC no. | 3.4.22.43 | ||||||||
CAS no. | 223670-00-6 | ||||||||
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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Cathepsin V (EC 3.4.22.43, Cathepsin L2, cathepsin U) is an enzyme.[1][2][3] This enzyme catalyses the following chemical reaction
- The recombinant enzyme hydrolyses proteins (serum albumin, collagen) and synthetic substrates (Z-Phe-Arg-NHMec > Z-Leu-Arg-NHMec > Z-Val-Arg-NHMec)
Cathepsin V is a human lysosomal cysteine endopeptidase.
See also
References
- ^ Brömme, D.; Li, Z.; Barnes, M.; Mehler, E. (1999). "Human cathepsin V functional expression, tissue distribution, electrostatic surface potential, enzymatic characterization, and chromosomal localization". Biochemistry. 38: 2377–2385. doi:10.1021/bi982175f. PMID 10029531.
- ^ Adachi, W.; Kawamoto, S.; Ohno, I.; Nishida, K.; Kinoshita, S.; Matsubara, K.; Okubo, K. (1998). "Isolation and characterization of human cathepsin V: a major proteinase in corneal epithelium". Invest. Ophthalmol. Vis. Sci. 39 (10): 1789–1796. PMID 9727401.
- ^ Santamaría, I.; Velasco, G.; Cazorla, M.; Fueyo, A.; Campo, E.; López-Otín, C. (1998). "Cathepsin L2, a novel human cysteine proteinase produced by breast and colorectal carcinomas". Cancer Res. 58 (8): 1624–1630. PMID 9563472.
External links
- Cathepsin+V at the U.S. National Library of Medicine Medical Subject Headings (MeSH)