Information on EC 3.4.23.12 - nepenthesin

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.4.23.12
-
RECOMMENDED NAME
GeneOntology No.
nepenthesin
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
Similar to pepsin, but also cleaves on either side of Asp and at Lys-/-Arg
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
-
-
endopeptidase
-
CAS REGISTRY NUMBER
COMMENTARY hide
9073-80-7
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
subsp. flavescens
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Nepenthes dormaniana
-
-
-
Manually annotated by BRENDA team
Nepenthes mixta
-
-
-
Manually annotated by BRENDA team
Nepenthes neufvilleana
-
-
-
Manually annotated by BRENDA team
Nepenthes sp.
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
acid-denatured haemoglobin + H2O
?
show the reaction diagram
-
-
-
?
Bovine hemoglobin + H2O
?
show the reaction diagram
-
-
-
-
?
casein + H2O
?
show the reaction diagram
Egg albumin + H2O
?
show the reaction diagram
-
-
-
-
?
EQAGGDATEDFEDVGHSTDAR + H2O
EQAGGDATED + FEDVGHST + DAR
show the reaction diagram
Nepenthes sp.
-
-
-
?
Fibrin + H2O
?
show the reaction diagram
-
-
-
-
?
FVNQHLCGSHLVEALYLVCGERGFFYTPKA + H2O
FVNQHL + CGSHLVE + Ala-Leu + Tyr + LVCGERGF + FYTPKA
show the reaction diagram
-
substrate is the insulin B chain
-
-
?
Hemoglobin + H2O
?
show the reaction diagram
KDEAASDVK + H2O
KDEAAS + DVK
show the reaction diagram
Nepenthes sp.
-
-
-
?
KIYKDTEGY + H2O
KIY + KD + TEGY
show the reaction diagram
Nepenthes sp.
-
-
-
?
LFNQDVDAAVR + H2O
LFNQDVD + AAVR
show the reaction diagram
LKPVYDSLDAVRR + H2O
LKPVY + DSL + DAVRR
show the reaction diagram
Nepenthes sp.
-
-
-
?
LQQKRWDEAA + H2O
LQQK + RW + DEAA
show the reaction diagram
Nepenthes sp.
-
-
-
?
NQDVDAAVRGIK + H2O
NQDV + L-Asp + AAVRGIK
show the reaction diagram
Nepenthes sp.
-
-
-
?
oxidized insulin B chain + H2O
?
show the reaction diagram
-
nepenthesin I: 80% cleavage of Phe24-Phe25, 67% cleavage of Glu13-Ala14, 50% cleavage of Leu6-cysteic-acid7, 38% cleavage of Leu15-Tyr16 and 33% cleavage of Tyr16-Leu17
-
?
Peptides + H2O
?
show the reaction diagram
Ribonuclease + H2O
?
show the reaction diagram
-
-
-
-
?
TGTWDAYK + H2O
TGTWDA + YK
show the reaction diagram
Nepenthes sp.
-
-
-
?
TGTYDATK + H2O
TGTYDA + T-K
show the reaction diagram
Nepenthes sp.
-
-
-
?
Thr-Ile-Asp-Glu + H2O
Thr-Ile-Asp + Glu
show the reaction diagram
Nepenthes sp.
-
-
-
?
WDEAVNLAK + H2O
WDEA + VNLAK
show the reaction diagram
Nepenthes sp.
-
-
-
?
additional information
?
-
-
cleavage site specificity with preference for the carboxy and amino sides of Asp, cleavage of the carboxy side of Ala, Leu, Ser, Thr, and Tyr also occurs, and cleavage on the amino side of Ala, Phe, Thr, Tyr, and Lys
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
Peptides + H2O
?
show the reaction diagram
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
CoSO4
CuCl2
cupric ions
-
strong inhibition of nepenthesin I and II by diazoacetyl-DL-norleucine in presence of cupric ions, no inactivation in absence of cupric ions
diazoacetyl-DL-norleucine
-
strong inhibition of nepenthesin I and II in presence of cupric ions, no inactivation in absence of cupric ions
Diazoacetyl-DL-norleucine methyl ester
-
i.e. DAN
dithiothreitol
-
isoforms nethepsin I, IIa and IIb are completely inactivated in the presence of 40-70 mM dithiothreitol
DL-Norleucine methyl ester
HgCl2
N-(diazoacetyl)-N-(2,4-dinitrophenyl)ethylenediamine
-
-
Pepstatin
pepstatin A
-
0.1 mM, complete inhibition of nepenthesin I and II
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2.6
-
reaction with acid-denatured haemoglobin, nepenthesin I and II
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1.7 - 3.2
-
-
1.7 - 6
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
assay at
40
Nepenthes sp.
-
assay at
45
-
nepenthesin II
55
-
nepenthesin I
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
-
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.09
-
nepenthesin II, calculation from nucleotide sequence
3.94
-
nepenthesin Ia and Ib, calculation from nucleotide sequence
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
the enzyme is secreted to the pitcher fluid
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45000
-
nepenthesin II, gel filtration
51000
-
nepenthesin I, gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
-
nepenthesin I contains 6 potential N-glycosylation sites, nepenthesin II has none
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2.9
-
at pH 2.9 at 37C, activity decreased very slowly on longer incubation, about 60% and 30% of the original activity are retained after 30 days and 65 days, respectively
717394
3 - 9
-
40C, highest stability at pH 3.0-9.0
36773
3 - 10
-
when nepenthesin I is incubated at pH 3.0 at 60C for 30 days, about 30% of the original activity remains. When incubated at pH 3.0-10.0 at 37C for 30 days, the enzyme retains 80% or more of activity
717394
5
-
60C, highest stability at pH 5
36773
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
pH 3.0, nepenthesin I loses 4% of its activity after 7 days, nepenthesin II loses 10% of its activity after 7 d
40
-
pH 3.0-9.0
50
-
pH 3.0, nepenthesin I loses 40% of its activity after 30 d, nepenthesin II loses 56% of its activity after 30 d
53
-
stable up to 53C during 1 h of incubation
60
-
highest stability at pH 5
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dithiothreitol
-
isoforms nethepsin I, IIa and IIb are completely inactivated in the presence of 40-70 mM dithiothreitol
guanidine-HCl
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
by gel filtration, ion exchange chromatography, and pepstatin affinity chromatography, native enzyme to homogeneity
-
DEAE-cellulose column chromatography, pepstatin column chromatography, MonoQ column chromatography, and Sephacryl S-200 gel filtration
nepenthesin I and II
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
nepenthesin I and II
-