3.4.23.12: nepenthesin
This is an abbreviated version!
For detailed information about nepenthesin, go to the full flat file.
Word Map on EC 3.4.23.12
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3.4.23.12
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pitcher
-
carnivorous
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pepsin
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prey
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gracilis
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low-ph
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hdx-ms
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forbidden
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asteraceae
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acid-denatured
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carnivory
- 3.4.23.12
-
pitcher
-
carnivorous
- pepsin
-
prey
- gracilis
-
low-ph
-
hdx-ms
-
forbidden
- asteraceae
-
acid-denatured
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carnivory
Reaction
Similar to pepsin, but also cleaves on either side of Asp and at Lys-/-Arg =
Synonyms
EC 3.4.99.4, More, Nep I, Nep II, Nep1, nepenthacin, nepenthasin;aspartyl endopeptidase, nepenthes aspartic protease, Nepenthesin, nepenthesin I, nepenthesin II, nepenthesin IIa, nepenthesin IIb, NepI, NEPII, proteinase, nepenthes acid
ECTree
3.4.23.12 nepenthesinAdvanced search results
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results (Substrates Products
Substrates Products on EC 3.4.23.12 - nepenthesin
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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
FVNQHLCGSHLVEALYLVCGERGFFYTPKA + H2O
FVNQHL + CGSHLVE + Ala-Leu + Tyr + LVCGERGF + FYTPKA
-
substrate is the insulin B chain
-
-
?
oxidized insulin B chain + H2O
?
-
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
?
Nepenthes sp.
-
preferential cleavage: -Asp, Asp-, Lys-, Ala-
-
-
?
PFU-093 + H2O
FITC(Ahx)-L-Val + L-Val + L-Lys-Dbc
-
FITC(Ahx)-L-Val-L-Val-L-Lys-Dbc
-
-
?
PFU-093 + H2O
FITC(Ahx)-L-Val + L-Val + L-Lys-Dbc
FITC(Ahx)-L-Val-L-Val-L-Lys-Dbc
-
-
?
additional information
?
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-
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
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-
?
additional information
?
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isoform nepenthesin I has broad cleavage specificity with the exception of cleavage of C-terminal to proline and tryptophan
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-
?
additional information
?
-
isoform nepenthesin I has broad cleavage specificity with the exception of cleavage of C-terminal to proline and tryptophan
-
-
?
additional information
?
-
isoform nepenthesin II shares the broad cleavage specificity of isoform nepenthesin I, but in addition, it cleaves C-terminal to tryptophan
-
-
?
additional information
?
-
isoform nepenthesin II shares the broad cleavage specificity of isoform nepenthesin I, but in addition, it cleaves C-terminal to tryptophan
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-
?
