Caricain

Caricain
Identifiers
EC number 3.4.22.30
CAS number 39307-22-7
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum

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

  1. ↑ 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.
  2. ↑ 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.
  3. ↑ Polgár L (July 1984). "Problems of classification of papaya latex proteinases". The Biochemical Journal. 221 (2): 555–6. PMC 1144075. PMID 6383350.
  4. ↑ 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. PMC 1145013. PMID 4015629.
  5. ↑ Zucker S, Buttle DJ, Nicklin MJ, Barrett AJ (April 1985). "The proteolytic activities of chymopapain, papain, and papaya proteinase III". Biochimica et Biophysica Acta. 828 (2): 196–204. doi:10.1016/0167-4838(85)90057-3. PMID 3919769.
  6. ↑ 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.
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