Detailed Peptide Information
This page shows detailed information of individual peptides present in PlantPepDB database. The page is majorly divided into 3 sections. The first sections contains primary information like peptide activity, source, sequence, etc. In the secondary information section user can access the tertiary structure as well as the physico-chemical properties by clicking the respective links. Further there is also link of the source database and research article from which the peptide data is retrieved. Download the information by clicking
| Primary Information |
|---|
| PPepDB ID | PPepDB_4171 |
| Peptide Name | NEP2_NEPGR |
| PMID(s) | --NA-- |
| Plant Source (Scientific Name) | Nepenthes gracilis |
| Plant Source (Common Name) | Slender pitcher plant |
| Plant Family | Nepenthaceae |
| Peptide Family | --NA-- |
| Peptide Function | Signaling-peptide |
| Peptide Function Description | Aspartyl protease; Glycoprotein; Hydrolase; Protease; Secreted; Signal; Zymogen | Aspartic proteinase nepenthesin-2 precursor (EC 3.4.23.12),(Nepenthesin-II).Secreted (By similarity). |
| Activity Against | --NA-- |
| IC50 value | --NA-- |
| Sequence | AFGCGEDNQGFGQGNGAGLIGMGWGPLSLPSQLGVGQFSYCMTSYGSSSPAIGTPDSSFSAIMDTGSDLIWTQCEPCTQCFSQPTPIFNPQDSSSFSTLPCESQYCQDLPSETCNNNECQYTYGYGDGSTTQGYMATETFTFETSSVPNILSTCFQQPSDGSTVQVPEISMQFDGGVLNLGEQNILISPAEGVICLAMGSMASPLYSVVLGLAIVSAIVAPTSSTSRGTLLHHGQKRPQPGLRVDLEQVDSGKNLTKYELIKRAIKRGERRMRSINAMLQSSSGIETPVYAGDGEYLMNVSSQLGISIFGNIQQQETQVLYDLQNLAVSFVPTQCGASSTLALGSAASGVPEGSPSTTLIHSSLNPTYYYITLQGITVGGDNLGIPSSTFQLQDDGTGGMIIDSGTTLTYLPQDAYNAVAQAFTDQINLPTVDESSSG |
| Sequence Length | 438 |
| Validation | Experimental evidence at protein level |
| Average Molecular Weight (Da) | 46174.31 |
| Monoisotopic Molecular Weight (Da) | 46144.92 |
| Isoelectric Point (pI) | 4.1 |
| Method / Extraction | --NA-- |
| External links (Uniprot, PDB and Source Information Database) |
|---|
| Uniprot | Q766C2 |
| NCBI | --NA-- |
| EMBL | AB114915 |
| Link to Source Databases | SPdb168630 |
|---|
| Addtional Information | FUNCTION:Extracellular proteinase found in the pitcher fluid of carnivorous plants. Digest prey for nitrogen uptake.CATALYTIC ACTIVITY:Similar to pepsin, but also cleaves on either side of Asp and at Lys-|-Arg.ENZYME REGULATION:Inhibited by pepstatin and by diazoacetyl-D,L- norleucine methyl ester (DAN) in the presence of Cu(2) ions (By similarity).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; 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;SIMILARITY:Belongs to the peptidase A1 family. |
