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". C. R. Trav. Carlesberg 36: 67–83. PMID 6043136.
  2. ↑ Robinson, G.W. (1975). "Isolation and characterization of papaya peptidase A from commercial chymopapain". Biochemistry 16: 3695–3700. doi:10.1021/bi00687a028. PMID 240390.
  3. ↑ Polgár, L. (1984). "Problems of classification of papaya latex proteinases". Biochem. J. 221: 555–556. PMID 6383350.
  4. ↑ Brocklehurst, K., Salih, E., McKee, R. and Smith, H. (1985). "Fresh non-fruit latex of Carica papaya contains papain, multiple forms of chymopapain A and papaya proteinase". Biochem. J. 228: 525–527. PMID 4015629.
  5. ↑ Zucker, S., Buttle, D.J., Nicklin, M.J.H. and Barrett, A.J. (1985). "Proteolytic activities of papain, chymopapain and papaya proteinase III". Biochim. Biophys. Acta 828: 196–204. doi:10.1016/0167-4838(85)90057-3. PMID 3919769.
  6. ↑ Dubois, T., Kleinschmidt, T., Schnek, A.G., Looze, Y. and Braunitzer, G. (1988). "The thiol proteinases from the latex of Carica papaya L. II. The primary structure of proteinase". Biol. Chem. Hoppe-Seyler 369: 741–754. doi:10.1515/bchm3.1988.369.2.741. PMID 3063283.

External links

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