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 IDPPepDB_3829
Peptide NameACE inhibitory peptide
PMID(s)20929253, 15135150, 24915368, PPepDB_3829_ref1
Plant Source (Scientific Name)Pisum sativum, Undaria pinnatifida
Plant Source (Common Name)Garden pea, Wakame
Plant FamilyFabaceae, Alariaceae
Peptide Family--NA--
Peptide FunctionACE-inhibitor, Antihypertensive, Enzyme-inhibitor
Peptide Function DescriptionShows weak inhibitory properties toward calmodulin-dependent phosphodiesterase 1 (CaMPDE) but strong inhibitions of angiotensin-converting enzyme (ACE) and renin. Had higher potency against ACE than against renin. Used as potential ingredients to formulate multifunctional food products and nutraceuticals.
Activity AgainstAngiotensin Converting Enzyme(IC50=2.7-43.7 µg/ml)
IC50 value2.7-43.7 µg/ml
SequenceKF
Sequence Length2
ValidationExperimental evidence at protein level
Average Molecular Weight (Da)293.37
Monoisotopic Molecular Weight (Da)293.17
Isoelectric Point (pI)8.75
Method / ExtractionUPLC, GFC, IEC, RP-HPLC, FAB-MS


Secondary Information
Tertiary Structure and DSSP ReportTertiary structure of this peptide is not available as the sequence length is < 5 residues
Physico-Chemical Properties of peptidesClick to View Physico-Chemical Details of PPepDB_3829


External links (Uniprot, PDB and Source Information Database)
Uniprot--NA--
NCBI--NA--
EMBL--NA--
Link to Source DatabasesEROP-Moscow_10439, AHTPDB_3966, AHTPDB_2774, AHTPDB_6875, AHTPDB_6259
Addtional Informationassay: Cushman and Cheung (1971)