3.4.22.32: Stem bromelain
This is an abbreviated version!
For detailed information about Stem bromelain, go to the full flat file.
Word Map on EC 3.4.22.32
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3.4.22.32
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papain
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ficin
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comosus
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chymotrypsin
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ananas
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hydrolysates
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allergen
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proteinases
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ige
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debridement
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neuraminidase
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alcalase
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cystatins
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virion
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hymenoptera
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flavourzyme
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medicine
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kininogens
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prick
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eschar
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tender
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haemagglutinins
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food industry
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actinidin
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ha2
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agriculture
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chymopapain
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mucolytic
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pharmacology
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pancreatin
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ige-binding
- 3.4.22.32
- papain
- ficin
- comosus
- chymotrypsin
- ananas
- hydrolysates
- allergen
- proteinases
- ige
-
debridement
- neuraminidase
- alcalase
- cystatins
- virion
- hymenoptera
- flavourzyme
- medicine
- kininogens
-
prick
-
eschar
-
tender
-
haemagglutinins
- food industry
- actinidin
- ha2
- agriculture
- chymopapain
-
mucolytic
- pharmacology
- pancreatin
-
ige-binding
Reaction
broad specificity for cleavage of proteins, but strong preference for Z-Arg-Arg-/-NHMec amongst small molecule substrates =
Synonyms
acidic bromelain stem proteinase, ACMD2_17643, BRM, Bromelain, Bromelain, stem, EC 3.4.22.4, EC 3.4.4.24, Pineapple stem bromelain, SBA, Sbm, stem bromelain
ECTree
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General Information
General Information on EC 3.4.22.32 - Stem bromelain
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physiological function
additional information
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bromelain increases expression of p53 as well as Bax in mouse skin papillomas, at the same time, bromelain decreases the activity of cell survival regulators such as Akt and Erk thus promoting apoptotic cell death in tumors. Bromelain reduces CD44 on the surface of mouse and human tumor cells accompanied by diminished cancer cell invasion and substrate attachment as well as by attenuation of de novo protein synthesis. Bromelain can stimulate the innate immune system by activating neutrophils to produce reactive oxygen species
physiological function
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bromelain decreases neutrophil interactions with P-selectin in vitro by proteolytic cleavage of P-selectin glycoprotein ligand-1
physiological function
antiproliferative effect of bromelain from different tissues against B16F10 murine melanoma cells, overview
physiological function
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chelating potential of stem bromelain for combating lead toxicity and oxidative stress, protective efficacy of stem bromelain against lead-induced toxicity in male Wistar rats, overview. Co-administration of stem bromelain with lead markedly reduces the lead accumulation in the kidney and spleen. The treatment of stem bromelain also reduces the serum malonaldehyde levels in the group exposed to lower dose of lead and serum triglyceride level in the group exposed to higher dose of lead. The lead-induced modulated levels of serum ALT and AST are also alleviated by bromelain treatment
physiological function
the highest anti-proliferation of the freeze-dried and the spray-dried bromelain versus A549 cells are observed with IC50 values of 0.0183 and 0.0264 mg/ml, respectively. For apoptotic induction, the highest activity of the freeze-dried and the spray-dried bromelain is observed on KB (7.53%) and A549 (6.29%) cell lines, respectively. Stem bromelain exhibits apoptotic induction activity on DU145, HT-29, A549, KB, HeLa, and HuTu-80 cells, but not on Hep-G2 cells
physiological function
Ananas comosus AGB 772
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antiproliferative effect of bromelain from different tissues against B16F10 murine melanoma cells, overview
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analysis of of macromolecular crowding on stem bromelain, i.e. effects of dextran (D70) and polyethylene glycol (P12 and P20) on native bromelain structure, by combining the results of absorption, circular dichroism, fluorescence and activity studies, detailed overview. The overall effect of the crowders on the enzyme is destabilization and deactivation. Molecular docking simulation of bromelain with PEG and dextran
additional information
comparative structural analysis of fruit and stem bromelain from Ananas comosus, structure homology modelling, model domain organisation, overview. The proteolytic fraction of pineapple stem is termed stem bromelain, while the one presents in the fruit is known as fruit bromelain (EC 3.4.22.33). NCBI conserved domain analysis reveals two domains of fruit and stem bromelain: cathepsin propeptide inhibitor (I29) and peptidase C1
additional information
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comparative structural analysis of fruit and stem bromelain from Ananas comosus, structure homology modelling, model domain organisation, overview. The proteolytic fraction of pineapple stem is termed stem bromelain, while the one presents in the fruit is known as fruit bromelain (EC 3.4.22.33). NCBI conserved domain analysis reveals two domains of fruit and stem bromelain: cathepsin propeptide inhibitor (I29) and peptidase C1
additional information
effects of bromelain on the pro-wound healing activities and the regenerative properties of mesenchymal stem cells, overview. The combination of bromelain and dexamethasone sodium phosphate induces a great activation of mesenchymal stem cells with an increase in hyaluronan and collagen production and antiinflammatory cytokines release, real-time polymerase chain reaction analysis of extracellular matrix proteins and remodeling enzymes in human mesenchymal stem cells, overview
additional information
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effects of bromelain on the pro-wound healing activities and the regenerative properties of mesenchymal stem cells, overview. The combination of bromelain and dexamethasone sodium phosphate induces a great activation of mesenchymal stem cells with an increase in hyaluronan and collagen production and antiinflammatory cytokines release, real-time polymerase chain reaction analysis of extracellular matrix proteins and remodeling enzymes in human mesenchymal stem cells, overview
additional information
three-dimensional structure homology modelling of stem bromelain using the procaricain enzyme structure as template, overview