Caricain
Caricain (EC 3.4.22.30, papaya peptidase A, papaya peptidase II, papaya proteinase, papaya proteinase III, papaya proteinase 3, proteinase omega, papaya proteinase A, chymopapain S, Pp) is an enzyme.[1][2][3][4][5][6] This enzyme catalyses the following chemical reaction
- Hydrolysis of proteins with broad specificity for peptide bonds, similar to those of papain and chymopapain
This enzyme is isolated from papaya plant, Carica papaya.
References
- ^ Schack P (1967). "Fractionation of proteolytic enzymes of dried papaya latex. Isolation and preliminary characterization of a new proteolytic enzyme". Comptes Rendus des Travaux du Laboratoire Carlsberg. 36 (4): 67–83. PMID 6043136.
- ^ Robinson GW (August 1975). "Isolation and characterization of papaya peptidase A from commercial chymopapain". Biochemistry. 14 (16): 3695–700. doi:10.1021/bi00687a028. PMID 240390.
- ^ Polgár L (July 1984). "Problems of classification of papaya latex proteinases". The Biochemical Journal. 221 (2): 555–6. doi:10.1042/bj2210555. PMC 1144075. PMID 6383350.
- ^ Brocklehurst K, Salih E, McKee R, Smith H (June 1985). "Fresh non-fruit latex of Carica papaya contains papain, multiple forms of chymopapain A and papaya proteinase omega". The Biochemical Journal. 228 (2): 525–7. doi:10.1042/bj2280525. PMC 1145013. PMID 4015629.
- ^ Zucker S, Buttle DJ, Nicklin MJ, Barrett AJ (April 1985). "The proteolytic activities of chymopapain, papain, and papaya proteinase III". Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 828 (2): 196–204. doi:10.1016/0167-4838(85)90057-3. PMID 3919769.
- ^ Dubois T, Kleinschmidt T, Schnek AG, Looze Y, Braunitzer G (August 1988). "The thiol proteinases from the latex of Carica papaya L. II. The primary structure of proteinase omega". Biological Chemistry Hoppe-Seyler. 369 (8): 741–54. doi:10.1515/bchm3.1988.369.2.741. PMID 3063283.
External links
- Caricain at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
