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
-
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
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Organic Solvent Stability
Organic Solvent Stability on EC 3.4.22.32 - Stem bromelain
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2,2,2-trifluoroethanol
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the enhanced binding of 1-anilino-8-naphthalene sulfonic acid to the specific/pre-molten globule (SMG) state of stem bromelain upon addition of 30% 2,2,2-trifluoroethanol suggests the presence of a large number of solvent-accessible non-polar clusters in the treated SMG. The formation of an molten globe (MG)-like state characterized by disordered side chain interactions but with considerable secondary structure when the specific/pre-molten globule (SMG) state of stem bromelain is subjected to 30% 2,2,2-trifluoroethanol (TFE). The TFE-induced MG conformation at alkaline pH could represent the conformation that allows stem bromelain to traverse membranes
Ethanol
guanidine-HCl
urea
Ethanol
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enzyme stabilized in 60-70% ethanol is non-functional, but retains all the elements of secondary structure
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6 M guanidine-HCl denatured state of stem bromelain is enzymatically inactive
urea
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stem bromelain is fully resistant against urea around neutral pH (5.5 to 10.0) and unfolds only below pH 5.0