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Information on EC 3.4.22.33 - Fruit bromelain

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EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.22 Cysteine endopeptidases
                3.4.22.33 Fruit bromelain
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This record set is specific for:
UNIPROT: Q6Q2T4 not found.
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Word Map
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The enzyme appears in viruses and cellular organisms
Reaction Schemes
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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, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ananase
-
-
-
-
Bromelain, juice
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-
-
-
Bromelase
-
-
-
-
Bromelin
-
-
-
-
Extranase
-
-
-
-
Fruit bromelain
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-
-
-
Fruit bromelain FA2
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-
-
-
Juice bromelain
-
-
-
-
Pinase
-
-
-
-
Traumanase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
preference for substrates possessing hydrophobic residues interacting with subsite S2, shows highest efficiency for Leu at P2
hydrolysis of peptide bond
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-
-
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CAS REGISTRY NUMBER
COMMENTARY hide
9001-00-7
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
benzyloxyxarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
?
casein + H2O
?
show the reaction diagram
-
-
-
?
epsilon-NH2-Cap-Ala-Cys(S-Bzl)-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
?
epsilon-NH2-Cap-Cys(S-Bzl)-Leu-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
?
epsilon-NH2-Cap-Leu-Cys(S-Bzl)-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
?
epsilon-NH2-Cap-Leu-Gly-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
?
epsilon-NH2-Cap-Phe-Arg-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
?
epsilon-NH2-Cap-Pro-Cys(S-Bzl)-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
?
N-alpha-benzoyl-DL-arginine-2-naphthylamide + H2O
N-alpha-benzoyl-DL-arginine + 2-naphthylamine
show the reaction diagram
-
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Cu2+
12% residual activity at 0.16 mM
Hg2+
14% residual activity at 0.16 mM
iodoacetic acid
5% residual activity at 2 mM
p-chloromercuribenzoate
15% residual activity at 2 mM
Phenylmethylsulfonylfluoride
84% residual activity at 2 mM
Urea
at 2.4 M urea the activity decreases continuously to 50% when using N-alpha-benzoyl-DL-arginine-2-naphthylamide as a substrate
additional information
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
highest activity at 96 mM, at 37°C and pH 7.0
dithiothreitol
highest activity at 2.5 mM, at pH 7.0 and 37°C
EDTA
28% increase of activity at 2 mM
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
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
55
using casein as a subatrate
65
using N-alpha-benzoyl-DL-arginine-2-naphthylamide as a substrate
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
fragment
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
Q6Q2T4_9POAL
324
0
35745
TrEMBL
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CM-Sepharose column chromatography, SP-Sepharose column chromatography, and Sephadex G-50 gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli Top10 cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Cabral, H.; Leopoldino, A.M.; Tajara, E.H.; Greene, L.J.; Faca, V.M.; Mateus, R.P.; Ceron, C.R.; de Souza Judice, W.A.; Julianod, L.; Bonilla-Rodriguez, G.O.
Preliminary functional characterization, cloning and primary sequence of Fastuosain, a cysteine peptidase isolated from fruits of Bromelia fastuosa
Protein Pept. Lett.
13
83-89
2006
Bromelia fastuosa (Q6Q2T4), Bromelia fastuosa
Manually annotated by BRENDA team