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_3852 |
| Peptide Name | WAMP-1b |
| PMID(s) | 25154438, 19583772 |
| Plant Source (Scientific Name) | Triticum kiharae |
| Plant Source (Common Name) | Wheat |
| Plant Family | Poaceae |
| Peptide Family | --NA-- |
| Peptide Function | Antimicrobial, Antifungal |
| Peptide Function Description | This block the fungalysin activity, keeping the chitinase intact. Thus, WAMPs represent novel protease inhibitors that are active against fungal metalloproteases. WAMPs directly inhibited hyphal elongation, and plays an important role in fungal development. Degradation of chitin cell wall. |
| Activity Against | F. verticillioides (IC50=2.7 ±0.15M) |
| IC50 value | 2.7 ±0.15M |
| Sequence | AQRCGDQARGAKCPNCLCCGKYGFCGSGDAYCGAGSCQSQCRGCR |
| Sequence Length | 45 |
| Validation | Experimental evidence at protein level |
| Average Molecular Weight (Da) | 4601.21 |
| Monoisotopic Molecular Weight (Da) | 4597.83 |
| Isoelectric Point (pI) | 8.62 |
| Method / Extraction | --NA-- |
| External links (Uniprot, PDB and Source Information Database) |
|---|
| Uniprot | P85966 |
| NCBI | --NA-- |
| EMBL | --NA-- |
| Link to Source Databases | EROP-Moscow_09067, CAMPSQ3261, APD_01470 |
|---|
| Addtional Information | Compared to WAMP-1a, WAMP-1b contains one additional Arg at the C-terminus. 10-Cys. MOA: This proteinase of fungi (fungalysin Fv-cmp) cleaves class IV chitinases, plant defense proteins that bind and degrade chitin of fungal cell walls. However, equal molar ratio of plant defensin WAMP-1b or WAMP-2 to chitinase was sufficient to block the fungalysin activity of fungi keeping the plant chitinase intact. Thus, WAMPs represent a novel type of protease inhibitors (enzyme inhibitor) being active against fungal metalloproteases (Slavokhotova etal., 2014). UPdated 8/2014. |
