Stem bromelain

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Stem bromelain
Stem bromelain
Identifiers
EC no.	3.4.22.32
CAS no.	37189-34-7
Databases
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB structures	RCSB PDB PDBe PDBsum
PMC
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PMC	articles
PubMed	articles
NCBI	proteins

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.

References

^ 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.
^ ^a ^b 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.
^ 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.
^ 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.
^ 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.
^ 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.

External links

Stem+bromelain at the U.S. National Library of Medicine Medical Subject Headings (MeSH)

[pmid10384688-1] 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.

[pmid8298455-2] 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.

[pmid7548045-3] 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.

[pmid8180228-4] 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.

[pmid8757805-5] 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.

[pmid9466915-6] 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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v t e Proteases: cysteine proteases (EC 3.4.22)
Caspase	Caspase 1 Caspase 2 Caspase 3 Caspase 4 Caspase 5 Caspase 6 Caspase 7 Caspase 8 Caspase 9 Caspase 10 Caspase 12 Caspase 13 Caspase 14
Fruit-derived	Papain Ficain Bromelain Actinidain
Calpain	CAPN1 CAPN2 CAPN3 CAPN5 CAPN6 CAPN7 CAPN8 CAPN9 CAPN10 CAPN11 CAPN12 CAPN13 CAPN14 CAPNS1 CAPNS2
Cathepsin	B C F H K L1/L2 O S W Z
Other	Clostripain Cancer procoagulant Separase Autophagin Cruzipain 3C-like protease Gingipain R Gingipain K

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)