Information on EC 3.4.23.12 - nepenthesin

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The expected taxonomic range for this enzyme is: Eukaryota

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
isozymes nepenthesin I and II
-
-
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
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
?
-
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
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
nepenthesin I and II show a high cysteine content which form disulfide bonds, molecular modeling
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
dithiothreitol
-
isoforms nethepsin I, IIa and IIb are completely inactivated in the presence of 40-70 mM dithiothreitol
DL-Norleucine methyl ester
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
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1.7 - 3.2
-
-
1.7 - 6
additional information
-
pH profile, nepenthesin I and II
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
assay at
40
Nepenthes sp.
-
assay at
45
-
nepenthesin II
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
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45000
-
nepenthesin II, gel filtration
51000
-
nepenthesin I, gel filtration
58000
-
purified nepenthesin I, gel filtration
600000
-
multicomplex structured enzyme
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
no glycoprotein
-
nepenthesin II
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
5
-
60C, highest stability at pH 5
36773
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
-
pH 3.0-9.0
53
-
stable up to 53C during 1 h of incubation
60
-
highest stability at pH 5
70
-
highly reduced activity of nepenthesin I and II after 7 days
80
-
nepenthesin I and II, complete loss of activity after 7 days
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
native nepenthesin I and II 200fold and 186fold, respectively, from pitcher fluid to homogeneity by two steps of anion exchange chromatography, gel filtration, pepstatin affinity chromatography, and another different step of exchange chromatography
-
nepenthesin I and II
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
nepenthesin I and II
-
nepenthesin I and II, DNA and amino acid sequence determination and analysis, phylogenetic analysis