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MYP_149313
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Basic Information
Unnamed
Cardiovascular ▸ Blood pressure regulation ▸ Antihypertensive
Enzyme modulation ▸ Enzyme inhibition ▸ ACE inhibition ▸ ACE inhibitory
Neurological / Signaling ▸ Neuropeptide activity ▸ Neuropeptide
Other / Curated residual function label ▸ Generic enzyme inhibition annotation
Standard
4 amino acids
C26H42N4O5
Standard
Sequence
VIIF
Physicochemical Analysis
490.64 Da
5.50
-0.27
-0.48
-0.0665
4.00
0.05
1.26
7.50
267.50
0.2500
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
150.62
1.84
5.0
5.0
14.0
35.0
1.0
3.0
Structural Visualization
3D PDB MODEL
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2D CHEMICAL STRUCTURE
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Experimental Records
RECORD: Rec_0272599 VERIFIED: NO
Provenance & Taxonomy
Sepia officinalis [Animal]
ACE-inhibitory peptide
6610
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
Bio-Activity Profile
Antihypertensive ACE inhibitory
ACE
1190 μg/mL
IC50
PaperENZYMATIC METHOD FOR ACE INHIBITORY PEPTIDE DERIVED FROM AQUATIC RESOURCES: A REVIEW
RECORD: Rec_0282328 VERIFIED: NO
Provenance & Taxonomy
Sepia officinalis [Animal]
ACE-inhibitory peptide
6610
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
Bio-Activity Profile
Antihypertensive
Spontaneously hypertensive rat (SHR)
19.4 mmHg
SBP decrease
PaperIs the structural diversity of tripeptides sufficient for developing functional food additives with satisfactory multiple bioactivities?
RECORD: Rec_0348997 VERIFIED: NO
Provenance & Taxonomy
Actinopterygii [Animal]
7898
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
Bio-Activity Profile
Antihypertensive
PaperReview on the angiotensin-I-converting enzyme (ACE) inhibitor peptides from marine proteins PMID23271625 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/23271625/
RECORD: Rec_0358177 VERIFIED: YES
Provenance & Taxonomy
not reported [other]
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
Bio-Activity Profile
Antihypertensive ACE inhibitory
Angiotensin-converting enzyme (ACE)
8.7
IC50
PaperBalti R., Nedjar-Arroume N., Bougatef A., Guillochon D., Nasri M.. Three novel angiotensin I-converting enzyme (ACE) inhibitory peptides from cuttlefish (Sepia officinalis) using digestive proteases. Food Res. Int., 43, 1136-1143, 2010.
RECORD: Rec_0376740 VERIFIED: NO
Provenance & Taxonomy
Sepia officinalis [Animal]
ACE-inhibitory peptide
6610
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
Bio-Activity Profile
Antihypertensive ACE inhibitory
ACE
8.7 μM
IC50
PaperReview on the angiotensin-I-converting enzyme (ACE) inhibitor peptides from marine proteins. PMID23271625 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/23271625/
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