Detail Information for IndEnz0002015835
IED ID IndEnz0002015835
Enzyme Type ID protease015835
Protein Name Aspartic proteinase nepenthesin-2
EC 3.4.23.12
Nepenthesin-II
Fragments
Gene Name
Organism Nepenthes distillatoria (Pitcher plant)
Taxonomic Lineage cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae eudicotyledons Gunneridae Pentapetalae Caryophyllales Nepenthaceae Nepenthes Nepenthes distillatoria (Pitcher plant)
Enzyme Sequence QTVQVEPPYYAGDGEYLMVDLIWTQCEPCTQCFSQDSSSFSTLPCESQYCQDLPSETCDCQYTYGYGDGSSTQGYMAXEDGSSVPNIAFGCGDNLQIDSGTTLTYLPQDAYNAVAQAFTDQINLPTVDESSSGLSTCFQEPSDGSTVQVPEISMQDGGVLNDLQNLAVSFFPTQCGAS
Enzyme Length 178
Uniprot Accession Number P69477
Absorption
Active Site ACT_SITE 98; /evidence=ECO:0000255|PROSITE-ProRule:PRU10094
Activity Regulation ACTIVITY REGULATION: Inhibited by pepstatin and by diazoacetyl-D,L-norleucine methyl ester (DAN) in the presence of Cu(2+) ions.
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=Similar to pepsin, but also cleaves on either side of Asp and at Lys-|-Arg.; EC=3.4.23.12;
DNA Binding
EC Number 3.4.23.12
Enzyme Function FUNCTION: Extracellular proteinase found in the pitcher fluid of carnivorous plants. Digest prey for nitrogen uptake.
Temperature Dependency BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 45 degrees Celsius. Thermostable up to 50 degrees Celsius. Retains 44% of the original activity after incubation for 30 days at 50 degrees Celsius.;
PH Dependency BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 3.0. Retains 80% and 60% of the original activity after incubation for 30 days at pH 3.0 and pH 4.0 respectively. Unstable at pH higher than 5.0.;
Pathway
nucleotide Binding
Features Active site (1); Chain (1); Natural variant (1); Non-adjacent residues (7)
Keywords Aspartyl protease;Direct protein sequencing;Hydrolase;Protease;Secreted;Zymogen
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15035659}.
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 19,106
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda