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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Reaction
Reaction on EC 3.4.22.32 - Stem bromelain
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broad specificity for cleavage of proteins, but strong preference for Z-Arg-Arg-/-NHMec amongst small molecule substrates
broad specificity for cleavage of proteins, but strong preference for Z-Arg-Arg-/-NHMec amongst small molecule substrates
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broad specificity for cleavage of proteins, but strong preference for Z-Arg-Arg-/-NHMec amongst small molecule substrates
endopeptidase
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broad specificity for cleavage of proteins, but strong preference for Z-Arg-Arg-/-NHMec amongst small molecule substrates
The most abundant of the cysteine endopeptidases of the stem of the pineapple plant, Ananas comosus. Distinct from the bromelain found in the pineapple fruit (3.4.22.33). Scarcely inhibited by chicken cystatin and also very slowly inactivated by 3.4.22.4.
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