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Information on EC 3.4.22.33 - Fruit bromelain
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3.4.22.33 Fruit bromelainSpecify your search results
Word Map
The enzyme appears in viruses and cellular organisms
Reaction Schemes
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
bromelin, bromelain a, fruit bromelain, fastuosain, pinase, bromelase, bromelain b, fruit bromelain fa2, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Ananase
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-
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Bromelain
Bromelain, juice
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Bromelase
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Bromelin
EC 3.4.22.4
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formerly, part transferred
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EC 3.4.22.5
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formerly
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EC 3.4.4.24
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formerly, part transferred
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Extranase
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Fruit bromelain
Fruit bromelain FA2
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Juice bromelain
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Pinase
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Traumanase
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-
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additional information
Bromelin
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Fruit bromelain
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additional information
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c.f. stem bromelain, enzyme belongs to the papain superfamily
additional information
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another cysteine endopeptidase, with similar action on small molecule substrates, pinguinain (formerly EC 3.4.99.18) is obtained from the related plant, Bromelia pinguin, but pinguinain differs from fruit bromelain in being inhibited by chicken cystatin
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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)
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
hydrolysis of peptide bond
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-
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hydrolysis of peptide bond
preference for substrates possessing hydrophobic residues interacting with subsite S2, shows highest efficiency for Leu at P2
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CAS REGISTRY NUMBER
COMMENTARY
9001-00-7
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
Benzoyl-Gly-Gly-Lys + H2O
?
-
enzyme form FBA is much more active than FBB
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-
?
benzoyl-Phe-Val-Arg-4-methylcoumarin 7-amide + H2O
benzoyl-Phe-Val-Arg + 7-amino-4-methylcoumarin
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convenient substrate for fruit bromelain, scarcely affected by stem bromelain
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-
?
benzoyl-Phe-Val-Arg-p-nitroanilide + H2O
benzoyl-Phe-Val-Arg + p-nitroaniline
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-
-
-
?
benzyl-Phe-Val-Arg-4-nitroanilide + H2O
benzyl-Phe-Val-Arg + 4-nitroaniline
preferred substrate of fruit bromelain
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-
?
Benzyloxycarbonyl-Ala-Leu + H2O
Benzyloxycarbonyl-Ala + Leu
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enzyme form FBA is much more active than FBB
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-
?
benzyloxycarbonyl-Arg-Arg-4-nitroanilide + H2O
benzyloxycarbonyl-Arg-Arg + 4-nitroaniline
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-
-
?
benzyloxycarbonyl-Arg-Arg-p-nitroanilide + H2O
benzyloxycarbonyl-Arg-Arg + p-nitroaniline
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?
Benzyloxycarbonyl-Gly-Leu + H2O
Benzyloxycarbonyl-Gly + Leu
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enzyme form FBA is much more active than FBB
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?
Benzyloxycarbonyl-Gly-Val + H2O
Benzyloxycarbonyl-Gly + Val
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enzyme form FBA is much more active than FBB
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?
bromelain + H2O
?
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rapid self-digestion in aqueous solution, can be prevented by addition of alpha2-macroglobulin
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?
Carbobenzoxy-Gly-Ala + H2O
Carbobenzoxy-Gly + Ala
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enzyme form FBA is much more active than FBB
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?
epsilon-NH2-Cap-Ala-Cys(S-Bzl)-7-amido-4-methylcoumarin + H2O
?
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?
epsilon-NH2-Cap-Cys(S-Bzl)-Leu-7-amido-4-methylcoumarin + H2O
?
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?
epsilon-NH2-Cap-Leu-Cys(S-Bzl)-7-amido-4-methylcoumarin + H2O
?
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?
epsilon-NH2-Cap-Pro-Cys(S-Bzl)-7-amido-4-methylcoumarin + H2O
?
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?
N-alpha-benzoyl-DL-arginine-2-naphthylamide + H2O
N-alpha-benzoyl-DL-arginine + 2-naphthylamine
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-
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?
Nalpha-Benzoyl-Arg amide + H2O
Nalpha-Benzoyl-Arg + NH3
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-
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?
Nalpha-Benzoyl-DL-Arg 4-nitroanilide + H2O
Nalpha-Benzoyl-DL-Arg + 4-nitroaniline
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?
angiotensin II + H2O
hydrolyzed angiotensin II
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cleavage between Tyr4-Ile5
cleavage between Tyr4-Ile5
?
angiotensin II + H2O
hydrolyzed angiotensin II
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cleavage between Tyr4-Ile5
cleavage between Tyr4-Ile5
?
bradykinin + H2O
fragments of bradykinin
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cleavage between Gly4-Phe5 and Phe5-Ser6
cleavage between Gly4-Phe5 and Phe5-Ser6
?
bradykinin + H2O
fragments of bradykinin
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cleavage between Gly4-Phe5 and Phe5-Ser6
cleavage between Gly4-Phe5 and Phe5-Ser6
?
casein + H2O
?
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enzyme is assayed using casein as a substrate with Coomassie dye to track completion of hydrolysis of casein, casein is hydrolysed to completion leading to a brown coloured solution, assay method development as a Bradford dye-binding-bromelain-casein system as an assay for heavy metals, based on colour development and its inhibition by Hg2+ and Cu2+
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?
additional information
?
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enzyme catalyzes synthesis of acylamino acid anilides
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?
additional information
?
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bromelain has a profound immunmodulatory effect, overview, bromelain affects blood coagulation, fibrinolysis, and platelet functions, mechanism, overview
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?
additional information
?
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enzyme is scarcely able to hydrolyze benzyloxycarbonyl-Arg-Arg-4-methylcoumarin 7-amide
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?
additional information
?
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bromelain is a cysteine protease containing a single thiol group in the active sites
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?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
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-
bromelain has a profound immunmodulatory effect, overview, bromelain affects blood coagulation, fibrinolysis, and platelet functions, mechanism, overview
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?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
additional information
additional information
-
poor or no inhibition by ions K+, Ca2+, Mg2+, Mn2+, Co2+, Bo3+, Al3+, Cr2+, Ni2+, Sn2+, Ag+, Fe2+, Cd2+, Zn2+, W3+, Se2+, As3+, and Pb2+, overview
additional information
modulation of fruit bromelain by divalent ions is pH dependent
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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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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Urea
activity decreases in the presence of 4 M urea and reaches the activity of the control again at 8 M when using casein as a substrate
additional information
high-pressure treatment of fruit bromelain with 300 MPa, at 20°C for 20 min: high pressure processing (HPP) affects the fibrinolytic activity of fruit bromelain in vivo, overview. Compared with untreated fruit bromelain, the fibrinolytic activity of high-pressure processing-treated fruit bromelain is obviously increased which might be attributed to the increase of alpha-helix and the exposure of tryptophan residues and tyrosine residues, overview. High-pressure processing-treated fruit bromelain shows an increase (7.67%) in alpha-helix and its fluorescence intensities are increased by 42.5% and 78.7% at the excitation wavelength of 295 nm and 280 nm, respectively
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Asthma
Allergic reactions, including asthma, to the pineapple protease bromelain following occupational exposure.
Carcinoma, Hepatocellular
Cytotoxic Effect of Bromelain on HepG2 Hepatocellular Carcinoma Cell Line.
Colitis
Corrigendum: Inhibition of Epithelial TNF-? Receptors by Purified Fruit Bromelain Ameliorates Intestinal Inflammation and Barrier Dysfunction in Colitis.
Colitis
Inhibition of Epithelial TNF-? Receptors by Purified Fruit Bromelain Ameliorates Intestinal Inflammation and Barrier Dysfunction in Colitis.
Escherichia coli Infections
Proteolytic inhibition of Salmonella enterica serovar typhimurium-induced activation of the mitogen-activated protein kinases ERK and JNK in cultured human intestinal cells.
Infections
Benefit of dietary integrators for treating functional dyspepsia: a prospective pilot study.
Infections
Bromelain: A Review on its Potential as a Therapy for the Management of Covid-19.
Infections
Proteolytic inhibition of Salmonella enterica serovar typhimurium-induced activation of the mitogen-activated protein kinases ERK and JNK in cultured human intestinal cells.
Inflammatory Bowel Diseases
Bromelain treatment decreases neutrophil migration to sites of inflammation.
Influenza, Human
Structure of bromelain-released influenza virus haemagglutinin as revealed by electrophoresis, sedimentation and electron microscopy.
Influenza, Human
[Characteristics of isolating influenza virus hemagglutinin using purified bromelin]
Ischemic Stroke
The Alteration of Plasma Matrix Metalloproteinase-9 Level after the Addition of Bromelin 500 mg to Standard Therapy of Acute Ischemic Stroke and Its Correlation with Outcome.
Lung Neoplasms
Antimetastatic effect of bromelain with or without its proteolytic and anticoagulant activity.
Lymphoma
Germline V genes encode viable motheaten mouse autoantibodies against thymocytes and red blood cells.
Melanoma
Antitumor effects in vitro and in vivo and mechanisms of protection against melanoma B16F10-Nex2 cells by fastuosain, a cysteine proteinase from Bromelia fastuosa.
Neoplasm Metastasis
Antimetastatic effect of bromelain with or without its proteolytic and anticoagulant activity.
Neoplasm Metastasis
Antitumor effects in vitro and in vivo and mechanisms of protection against melanoma B16F10-Nex2 cells by fastuosain, a cysteine proteinase from Bromelia fastuosa.
Neoplasms
Antitumor effects in vitro and in vivo and mechanisms of protection against melanoma B16F10-Nex2 cells by fastuosain, a cysteine proteinase from Bromelia fastuosa.
Neoplasms
Bromelain, the enzyme complex of pineapple (Ananas comosus) and its clinical application. An update.
Purpura, Thrombocytopenic, Idiopathic
Use of enzyme treatment to enhance reactivity of HLA and platelet-specific antibodies in solid-phase RBC adherence assays.
Rhinitis
Allergic reactions, including asthma, to the pineapple protease bromelain following occupational exposure.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics, kinetic modeling, detailed overview
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
inhibition kinetics, detailed overview
-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
1050.57
extracted crown bromelain, pH 6.0, 37°C, with substrate casein
1365.77
extracted peel bromelain, pH 6.0, 37°C, with substrate casein
1519.85
extracted pulp bromelain, pH 6.0, 37°C, with substrate casein
2512.44
purified native enzyme, pH and temperature not specified in the publication
additional information
4429.0 U/ml at pH 4.5, crude bromelain extract from fruit pulp
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2.9
6.5
7.5
7.7
additional information
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
55
59
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50 - 60
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most suitable hydrolysate temperature of casein acids for bromelain is 50-60°C
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.6
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Ananas comosus AGB 772
