Ficain
Ficain | |||||||||
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Identifiers | |||||||||
EC number | 3.4.22.3 | ||||||||
CAS number | 9001-33-6 | ||||||||
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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Ficain (EC 3.4.22.3, ficin, debricin, higueroxyl delabarre) is an enzyme that is derived from figs latex.[1][2] It is of a family of proteases known as the cysteine endopeptidases, a group that also includes papain derived from papaya latex, bromelase (bromelain) extracted from pineapple stem, calpain, caspases, cathepsin B, and chymopapain. It is one of the most commonly used for differentiating many blood group antigens: For example, it destroys M, N, S, Duffy a, and Duffy b, and enhances some other antigens including antigens from the Rh, Kidd, Lewis, I, and P1 systems.
It is a common occurrence when eating the skins or the white pulp directly inside the skin of a fig to get a burning or itching sensation. This is due to the ficin in the latex (sap) of the fruit, particularly if it is unripened.
References
- ↑ Liener, I.E.; Friedenson, B. (1970). "Ficin". Methods Enzymol. 19: 261–273. doi:10.1016/0076-6879(70)19020-3.
- ↑ Brocklehurst, K.; Willenbrock, F.; Salih, E. (1987). "Cysteine proteinases". In Neuberger, A.; Brocklehurst, K. New Comprehensive Biochemistry: Hydrolytic Enzymes. Amsterdam: Elsevier. pp. 39–158.
External links
- Ficain at the US National Library of Medicine Medical Subject Headings (MeSH)
- EC 3.4.22.3
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