3.4.22.33: Fruit bromelain
This is an abbreviated version!
For detailed information about Fruit bromelain, go to the full flat file.
Word Map on EC 3.4.22.33
Reaction
Hydrolysis of proteins with broad specificity for peptide bonds. Bz-Phe-Val-Arg-/-NHMec is a good synthetic substrate, but there is no action on Z-Arg-Arg-NHMec (c.f. stem bromelain) =
Synonyms
ACMD2_17643, Ananase, Bromelain, bromelain A, bromelain B, Bromelain, juice, Bromelase, Bromelin, EC 3.4.22.4, EC 3.4.22.5, EC 3.4.4.24, Extranase, fastuosain, FBM, Fruit bromelain, Fruit bromelain FA2, Juice bromelain, More, Pinase, Traumanase
ECTree
3.4.22.33 Fruit bromelainAdvanced search results
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results (Inhibitors
Inhibitors on EC 3.4.22.33 - Fruit bromelain
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INHIBITOR 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
Ca2+
noncompetitive inhibition at pH 3.5, while both K-and V-type activations of bromelain are observed in the presence of 0.5 mM Ca2+ at pH 4.5 and pH 7.5
Urea
at 2.4 M urea the activity decreases continuously to 50% when using N-alpha-benzoyl-DL-arginine-2-naphthylamide as a substrate
Cu2+
competitive inhibition at pH 3.5 with 0.6 mM Cu2+, which changes to an uncompetitive inhibition at pH 4.5 and pH 7.5
cystatin
an extended AE-rich N-terminal trunk in secreted pineapple cystatin enhances inhibition of fruit bromelain and is posttranslationally removed during ripening, The AE-rich N-terminal trunk is required to inhibit fruit bromelain (above 95%), whereas its removal decreases inhibition to 20%. Recombinant cystatin containing the complete AE-rich N-terminal trunk and recombinant medium pineapple cystatin effectively inhibit bromelain compared to recombinant core pineapple cystatin
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additional information
stability of bromelain in the presence of EDTA and sodium benzoate; stability of bromelain in the presence of EDTA and sodium benzoate
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additional information
stability of bromelain in the presence of EDTA and sodium benzoate; stability of bromelain in the presence of EDTA and sodium benzoate
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