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MYP_119536
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Basic Information
Angiotensin I-converting enzyme inhibitor 4
Cardiovascular ▸ Blood pressure regulation ▸ Antihypertensive
Enzyme modulation ▸ Enzyme inhibition ▸ ACE inhibition ▸ ACE inhibitory
Enzyme modulation ▸ Enzyme inhibition ▸ Calpain-1 inhibitory
Enzyme modulation ▸ Enzyme inhibition ▸ DPP-III Inhibitory
Enzyme modulation ▸ Enzyme inhibition ▸ DPP-IV inhibition ▸ DPP-IV inhibitory
Enzyme modulation ▸ Enzyme inhibition ▸ Tripeptidyl Peptidase II Inhibitory
Membrane / Ion-channel modulation ▸ Calcium channel modulation ▸ Calcium channel inhibitor
Metabolic ▸ Glucose metabolism ▸ Antidiabetic
Neurological / Signaling ▸ Neuropeptide activity ▸ Neuropeptide
Other / Curated residual function label ▸ Generic enzyme inhibition annotation
Sensory / Food function ▸ Taste-active peptide ▸ Bitter peptide
Standard
2 amino acids
C14H20N2O4
Standard
Sequence
VY
Physicochemical Analysis
280.32 Da
5.49
-0.27
-0.48
-0.1335
1.45
0.53
0.67
-32.70
145.00
0.5000
1490.00
1490.00
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
112.65
0.49
4.0
4.0
6.0
20.0
1.0
1.0
Structural Visualization
3D PDB MODEL
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2D CHEMICAL STRUCTURE
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Experimental Records
RECORD: Rec_0267791 VERIFIED: YES
Provenance & Taxonomy
Capra hircus [Animal]
9925.0
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
Bio-Activity Profile
DPP-III Inhibitory
Dipeptidyl peptidase III
PaperDhanda S.; Singh H.; Singh J.. Hydrolysis of various bioactive peptides by goat brain dipeptidylpeptidase-III. Cell Biochem. Funct. 23, 3, 339-345, 2008.
RECORD: Rec_0270746 VERIFIED: NO
Provenance & Taxonomy
Undaria pinnatifida [Protist]
ACE-inhibitory peptide
74381
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
Bio-Activity Profile
Antihypertensive
Spontaneously hypertensive rat (SHR)
17 mmHg
SBP decrease
PaperAntihypertensive peptides from food proteins: a review. PMID22249830 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/22249830/
RECORD: Rec_0271872 VERIFIED: YES
Provenance & Taxonomy
Oryza sativa [Plant]; Undaria pinnatifida [Protist]; Amaranthus hypochondriacus [Plant]; Triticum aestivum [Plant]
ACE inhibitory peptide
4530, 74381, 28502, 4565
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
Bio-Activity Profile
Enzyme inhibitory Neuropeptide ACE inhibitory Antihypertensive
Angiotensin-converting enzyme
35.2 μM
IC50
PaperAngiotensin I-converting enzyme inhibitory peptides derived from wakame (Undaria pinnatifida) and their antihypertensive effect in spontaneously hypertensive rats | Antihypertensive effects of Undaria pinnatifida (wakame) peptide on blood pressure in spontaneously hypertensive rats | Isolation and characterization of peptides with antihypertensive activity in foodstuffs | PubMed PMID 7765503 PMID7765503;12358510;151351;50000 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/7765503/
RECORD: Rec_0273200 VERIFIED: YES
Provenance & Taxonomy
synthetic construct [Synthetic]
32630.0
Structure & Mods
topology not specified [Not included yet]
noncanonical stereochemical modification [Modified]
noncanonical token ~!C1
Bio-Activity Profile
Tripeptidyl Peptidase II Inhibitory
Tripeptidyl peptidase II / CCK-8-inactivating peptidase
PaperGanellin C. R., Bishop P. B., Bambal R. B., Chan S. M., Law J. K., Marabout B., Luthra P. M., Moore A. N., Peschard O., Bourgeat P., Rose C., Vargas F.. Inhibitors of tripeptidyl peptidase II. 2. Generation of the first novel lead inhibitor of cholecystokinin-8-inactivating peptidase: a strategy for the design of peptidase inhibitors. J. Med. Chem., 43, 664-674, 2000. PMID10691692 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/10691692/
RECORD: Rec_0275057 VERIFIED: NO
Provenance & Taxonomy
Oryza sativa [Plant]
ACE-inhibitory peptide
4530
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
Bio-Activity Profile
Antihypertensive
Spontaneously hypertensive rat (SHR)
31 mmHg
SBP decrease
PaperIs the structural diversity of tripeptides sufficient for developing functional food additives with satisfactory multiple bioactivities?
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