Stem bromelain

Stem bromelain (SBM) (EC 3.4.22.32), a proteolytic enzyme, is a widely accepted phytotherapeutical drug member of the bromelain family of proteolytic enzymes obtained from Ananas comosus.[1] Some of the therapeutic benefits of SBM are reversible inhibition of platelet aggregation, angina pectoris, bronchitis, sinusitis, surgical traumas, thrombophlebitis, pyelonephritis and enhanced absorption of drugs, particularly of antibiotics.[2][3][4] Its anti-metastasis and anti-inflammatory activities are apparently independent of its proteolytic activity.[2] Although poorly understood, the diverse pleiotrophic effects of SBM seem to depend on its ability to traverse the membrane barrier,[5][6] a very unusual property of this protein.

Stem bromelain
Identifiers
EC number3.4.22.32
CAS number37189-34-7
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum

References
  1. Buck M (August 1998). "Trifluoroethanol and colleagues: cosolvents come of age. Recent studies with peptides and proteins". Q. Rev. Biophys. 31 (3): 297–355. doi:10.1017/s003358359800345x. PMID 10384688.
  2. Thomas PD, Dill KA (December 1993). "Local and nonlocal interactions in globular proteins and mechanisms of alcohol denaturation". Protein Sci. 2 (12): 2050–65. doi:10.1002/pro.5560021206. PMC 2142326. PMID 8298455.
  3. Liu Y, Bolen DW (October 1995). "The peptide backbone plays a dominant role in protein stabilization by naturally occurring osmolytes". Biochemistry. 34 (39): 12884–91. doi:10.1021/bi00039a051. PMID 7548045.
  4. Blanco FJ, Jiménez MA, Pineda A, Rico M, Santoro J, Nieto JL (May 1994). "NMR solution structure of the isolated N-terminal fragment of protein-G B1 domain. Evidence of trifluoroethanol induced native-like beta-hairpin formation". Biochemistry. 33 (19): 6004–14. doi:10.1021/bi00185a041. PMID 8180228.
  5. Schönbrunner N, Wey J, Engels J, Georg H, Kiefhaber T (July 1996). "Native-like beta-structure in a trifluoroethanol-induced partially folded state of the all-beta-sheet protein tendamistat". J. Mol. Biol. 260 (3): 432–45. doi:10.1006/jmbi.1996.0412. PMID 8757805.
  6. Hirota N, Mizuno K, Goto Y (January 1998). "Group additive contributions to the alcohol-induced alpha-helix formation of melittin: implication for the mechanism of the alcohol effects on proteins". J. Mol. Biol. 275 (2): 365–78. doi:10.1006/jmbi.1997.1468. PMID 9466915.
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