The Enzyme Database

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Accepted name: fruit bromelain
Reaction: Hydrolysis of proteins with broad specificity for peptide bonds. Bz-Phe-Val-Arg┼NHMec is a good synthetic substrate, but there is no action on Z-Arg-Arg-NHMec (c.f. stem bromelain)
Other name(s): juice bromelain; ananase; bromelase; bromelin; extranase; juice bromelain; pinase; pineapple enzyme; traumanase; fruit bromelain FA2
Comments: From the pineapple plant, Ananas comosus. Scarcely inhibited by chicken cystatin. Another cysteine endopeptidase, with similar action on small molecule substrates, pinguinain, is obtained from the related plant, Bromelia pinguin, but pinguinain differs from fruit bromelain in being inhibited by chicken cystatin [4].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, CAS registry number: 9001-00-7
1.  Sasaki, M., Kato, T. and Iida, S. Antigenic determinant common to four kinds of thiol proteases of plant origin. J. Biochem. (Tokyo) 74 (1973) 635–637. [PMID: 4127920]
2.  Yamada, F., Takahashi, N. and Murachi, T. Purification and characterization of a proteinase from pineapple fruit, fruit bromelain FA2. J. Biochem. (Tokyo) 79 (1976) 1223–1234. [PMID: 956152]
3.  Ota, S., Muta, E., Katanita, Y. and Okamoto, Y. Reinvestigation of fractionation and some properties of the proteolytically active components of stem and fruit bromelains. J. Biochem. (Tokyo) 98 (1985) 219–228. [PMID: 4044551]
4.  Rowan, A.D., Buttle, D.J. and Barrett, A.J. The cysteine proteinases of the pineapple plant. Biochem. J. 266 (1990) 869–875. [PMID: 2327970]
[EC created 1965 as EC, transferred 1972 to EC, part transferred 1992 to EC]

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