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MYP_157921
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Basic Information
Unnamed
Cardiovascular ▸ Blood pressure regulation ▸ Antihypertensive
Enzyme modulation ▸ Enzyme inhibition ▸ ACE inhibition ▸ ACE inhibitory
Membrane / Ion-channel modulation ▸ Calcium channel modulation ▸ Calcium channel inhibitor
Neurological / Signaling ▸ Neuropeptide activity ▸ Neuropeptide
Other / Curated residual function label ▸ Generic enzyme inhibition annotation
Standard
3 amino acids
C14H25N3O4
Standard
Sequence
IAP
Physicochemical Analysis
299.37 Da
5.53
-0.24
-0.44
-0.0800
1.57
0.43
0.71
70.87
163.33
0.0000
0.00
0.00
The radar chart summarizes major physicochemical dimensions for quick comparison, while exact numerical values remain listed on the left.
Residue Composition
Amino Acid Composition
Chemical Descriptors
112.73
-0.06
3.0
4.0
6.0
21.0
1.0
2.0
Structural Visualization
3D PDB MODEL
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2D CHEMICAL STRUCTURE
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Experimental Records
RECORD: Rec_0180070 VERIFIED: NO
Provenance & Taxonomy
Triticum aestivum [Plant]
ACE-inhibitory peptide
4565
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
Bio-Activity Profile
Antihypertensive ACE inhibitory Antioxidant
ACE
2.7 μM
IC50
PaperVegetable foods: A cheap source of proteins and peptides with antihypertensive, antioxidant, and other less occurrence bioactivities. PMID23598136 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/23598136/
RECORD: Rec_0195483 VERIFIED: YES
Provenance & Taxonomy
Triticum aestivum [Plant]
Gliadin-derived
4565;0
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
Bio-Activity Profile
Antihypertensive ACE inhibitory
Angiotensin-converting enzyme (ACE)
2.7
IC50
PaperMotoi H., Kodama T.. Isolation and characterization of angiotensin I-converting enzyme inhibitory peptides from wheat gliadin hydrolysate. Nahrung/Food, 47, 354-358, 2003.
RECORD: Rec_0211088 VERIFIED: NO
Provenance & Taxonomy
Poaceae [Plant]
4479
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
Bio-Activity Profile
Antihypertensive
PaperStructural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides PMID16448176 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/16448176/
RECORD: Rec_0215130 VERIFIED: NO
Provenance & Taxonomy
not reported [other]
ACE-inhibitory peptide
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
Bio-Activity Profile
Antihypertensive ACE inhibitory
ACE
25120 μM
IC50
PaperComparison of analytical methods to assay inhibitors of angiotensin I-converting enzyme PMID23993489 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/23993489/
RECORD: Rec_0267796 VERIFIED: YES
Provenance & Taxonomy
Triticum aestivum [Plant]
ACE inhibitory peptide
4565
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
Bio-Activity Profile
ACE inhibitory Antihypertensive Enzyme inhibitory Neuropeptide
Angiotensin-converting enzyme
PaperAntihypertensive peptides from animal products, marine organisms, and plants | Isolation and characterization of peptides with antihypertensive activity in foodstuffs | Vegetable foods: a cheap source of proteins and peptides with antihypertensive, antioxidant, and other less occurrence bioactivities | PubMed PMID 14609094 PMID14609094;28317;7500000 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/14609094/
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