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Literature summary extracted from

  • Amagase, S.; Nakayama, S.; Tsugita, A.
    Acid protease in Nepenthes. II. Study on the specificity of nepenthesin (1969), J. Biochem., 66, 431-439.
    View publication on PubMed

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.4.23.12 Peptides + H2O Nepenthes sp. preferential cleavage: -Asp, Asp-, Lys-, Ala- ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.4.23.12 Nepenthes sp.
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
3.4.23.12 Similar to pepsin, but also cleaves on either side of Asp and at Lys-/-Arg predominantly specific for aspartic acid residues at its carboxyl side or at its amino side, also to tyrosine and alanine residues at carboxyl sides Nepenthes sp.
a

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.4.23.12 pitcher
-
 Nepenthes sp.
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.23.12 EQAGGDATEDFEDVGHSTDAR + H2O
-
 Nepenthes sp. EQAGGDATED + FEDVGHST + DAR
-
 ?
3.4.23.12 KDEAASDVK + H2O
-
 Nepenthes sp. KDEAAS + DVK
-
 ?
3.4.23.12 KIYKDTEGY + H2O
-
 Nepenthes sp. KIY + KD + TEGY
-
 ?
3.4.23.12 LFNQDVDAAVR + H2O
-
 Nepenthes sp. LFNQDVD + AAVR
-
 ?
3.4.23.12 LKPVYDSLDAVRR + H2O
-
 Nepenthes sp. LKPVY + DSL + DAVRR
-
 ?
3.4.23.12 Peptides + H2O preferential cleavage: -Asp, Asp-, Lys-, Ala- Nepenthes sp. ?
-
 ?
3.4.23.12 TGTYDATK + H2O
-
 Nepenthes sp. TGTYDA + L-Thr-L-Lys
-
 ?
3.4.23.12 WDEAVNLAK + H2O
-
 Nepenthes sp. WDEA + VNLAK
-
 ?