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_5197 |
| Peptide Name | PER1_ZINEL |
| PMID(s) | --NA-- |
| Plant Source (Scientific Name) | Zinnia elegans |
| Plant Source (Common Name) | Zinnia |
| Plant Family | Asteraceae |
| Peptide Family | --NA-- |
| Peptide Function | Signaling-peptide |
| Peptide Function Description | Calcium; Direct protein sequencing; Glycoprotein; Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase; Peroxidase; Pyrrolidone carboxylic acid; Secreted; Signal | Basic peroxidase precursor 1 (EC 1.11.1.7) (ZePrx33.44) (ZePrx34.70).Secreted (By similarity). |
| Activity Against | --NA-- |
| IC50 value | --NA-- |
| Sequence | DSTTSNAAQAATDLPRGNMVLSQLISNFANKGLNTREMVALSGSHTLGQALGYEVIDAAKAAVERVCPGVVSCADILAVAARDASVAVGGPSWTVRLGRRMSYHKSSGTILMVPLFMLLISVNYFMSCNAQLSTTFYDTTCPTALSTIRTNYYRNLVTSRGLLISDQVLFNADSTDSIVTEYVNNPATFAADFAAAMVKMRCIRFRGRIYNSTLRIEPNFNRSLSQACPPTGNDATLRPLDLVTPNSFDNSEIGVVTGTSGIVRTLCGNPSSIRSSVSSNRRNAALVIRLLFHDCFVQGCDASLLLSGAGSERASPANDGV |
| Sequence Length | 321 |
| Validation | Experimental evidence at protein level |
| Average Molecular Weight (Da) | 34244.91 |
| Monoisotopic Molecular Weight (Da) | 34223.18 |
| Isoelectric Point (pI) | 8.61 |
| Method / Extraction | --NA-- |
| External links (Uniprot, PDB and Source Information Database) |
|---|
| Uniprot | Q4W1I8 |
| NCBI | --NA-- |
| EMBL | AJ880395 |
| Link to Source Databases | SPdb187737 |
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| Addtional Information | FUNCTION:Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might be dependent on each isozyme/isoform in each plant tissue. Involved in the synthesis of highly polymerized lignins.CATALYTIC ACTIVITY:Donor H(2)O(2) = oxidized donor 2 H(2)O.COFACTOR:Binds 1 heme B (iron-protoporphyrin IX) group per subunit (By similarity).COFACTOR:Binds 2 calcium ions per subunit (By similarity).BIOPHYSICOCHEMICAL PROPERTIES:Kinetic parameters: KM=241 uM for p-coumaryl alcohol (in the presence of 10.2 uM H2O2, for a partially glycosylated enzyme); KM=432 uM for p-coumaryl alcohol (in the presence of 10.2 uM H2O2, for a fully glycosylated enzyme); KM=83 uM for coniferyl alcohol (in the presence of 10.2 uM H2O2, for a partially glycosylated enzyme); KM=124 uM for coniferyl alcohol (in the presence of 10.2 uM H2O2, for a fully glycosylated enzyme); KM=15 uM for sinapyl alcohol (in the presence of 10.2 uM H2O2, for a partially glycosylated enzyme); KM=13 uM for sinapyl alcohol (in the presence of 10.2 uM H2O2, for a fully glycosylated enzyme); Note=The full glycosylation reduces the affinity of the enzyme for both p-coumaryl and coniferyl, but not sinapyl, alcohol;TISSUE SPECIFICITY:Expressed in tracheary elements, roots, young and old hypocotyls, and stems in the partially glycosylated form and in roots and young hypocotyls in the fully glycosylated form.None of the isoforms is significantly expressed in leaves or cotyledons.PTM:N-glycosylated.MASS SPECTROMETRY:Mass=31460; Method=MALDI; Range=30-321; Note=Deglycosylated form; Source=PubMed:16258008;MASS SPECTROMETRY:Mass=33440; Method=MALDI; Range=30-321; Note=Partially glycosylated form; Source=PubMed:16258008;MASS SPECTROMETRY:Mass=34700; Method=MALDI; Range=30-321; Note=Fully glycosylated form; Source=PubMed:16258008;SIMILARITY:Belongs to the peroxidase family. Classical plant (class III) peroxidase subfamily.CAUTION:Four genes are encoding the same mature protein that may have different glycosylation degree. The two precursors produced differ by only one amino acid located in the signal peptide. |
