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MYP_048622
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Basic Information
Unnamed
Cardiovascular ▸ Blood pressure regulation ▸ Antihypertensive
Enzyme modulation ▸ Enzyme inhibition ▸ ACE inhibition ▸ ACE inhibitory
Enzyme modulation ▸ Enzyme inhibition ▸ DPP-IV inhibition ▸ DPP-IV inhibitory
Enzyme modulation ▸ Enzyme inhibition ▸ Xanthine oxidase inhibition
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
C17H23N3O3
Standard
Sequence
IW
Physicochemical Analysis
317.38 Da
5.53
-0.24
-0.44
-0.1200
1.80
0.74
1.09
5.00
195.00
0.5000
5500.00
5500.00
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
108.21
1.65
4.0
3.0
7.0
23.0
2.0
1.0
Structural Visualization
3D PDB MODEL
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2D CHEMICAL STRUCTURE
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Experimental Records
RECORD: Rec_0136939 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
PaperMOTIFS WITH POTENTIAL PHYSIOLOGICAL ACTIVITY IN FOOD PROTEINS - BIOPEP DATABASE
RECORD: Rec_0137316 VERIFIED: YES
Provenance & Taxonomy
Katsuwonus pelamis [Animal] [Animal]; Undaria pinnatifida [Animal] [Animal]; Oncorhynchus keta [Animal]
Angiotensin
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
Bio-Activity Profile
Enzyme inhibitory Neuropeptide
2.0 μM
IC50
RECORD: Rec_0138360 VERIFIED: YES
Provenance & Taxonomy
Undaria pinnatifida [Protist]
176836
Structure & Mods
proteolytic peptide fragment [Linear]
canonical L-amino-acid peptide [L]
Bio-Activity Profile
Antihypertensive ACE inhibitory
Angiotensin-converting enzyme (ACE)
1.5 μM
IC50
PaperAngiotensin I-converting enzyme inhibitory peptides derived from wakame (Undaria pinnatifida) and their antihypertensive effect in spontaneously hypertensive rats PMID12358510 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/12358510/
RECORD: Rec_0141405 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
Spontaneously hypertensive rat (SHR)
55 mmHg
SBP decrease
PaperReview on the angiotensin-I-converting enzyme (ACE) inhibitor peptides from marine proteins. PMID23271625 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/23271625/
RECORD: Rec_0157857 VERIFIED: YES
Provenance & Taxonomy
Undaria pinnatifida [Plant]
Designed peptide
74381
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
Bio-Activity Profile
Antihypertensive
Angiotensin I-converting enzyme (ACE)
PaperAntihypertensive effects of Undaria pinnatifida (wakame) peptide on blood pressure in spontaneously hypertensive rats PMID15135150 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/15135150/
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