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MYP_125635
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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
3 amino acids
C8H15N3O5
Standard
Sequence
AGS
Physicochemical Analysis
233.22 Da
5.57
-0.20
-0.39
-0.0680
0.20
0.30
0.31
6.67
33.33
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
141.75
-2.99
5.0
5.0
6.0
16.0
0.0
2.0
Structural Visualization
3D PDB MODEL
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2D CHEMICAL STRUCTURE
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Experimental Records
RECORD: Rec_0027246 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
527.9 μM
IC50
PaperIntegration of QSAR modelling and QM/MM analysis to investigate functional food peptides with antihypertensive activity
RECORD: Rec_0048218 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
527.9 μM
IC50
PaperReview on the angiotensin-I-converting enzyme (ACE) inhibitor peptides from marine proteins. PMID23271625 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/23271625/
RECORD: Rec_0055327 VERIFIED: NO
Provenance & Taxonomy
Actinopterygii [Animal]
7898
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
Bio-Activity Profile
Antihypertensive
PaperWhat are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach PMID23871047 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/23871047/
RECORD: Rec_0092548 VERIFIED: YES
Provenance & Taxonomy
Sepia officinalis [Animal]
Angiotensin
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
Bio-Activity Profile
Enzyme inhibitory Neuropeptide ACE inhibitory
Angiotensin-converting enzyme
527.9 μM
IC50
RECORD: Rec_0175537 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)
527.9
IC50
PaperBalti R., Nedjar-Arroume N., Adje E. Y., Guillochon D., Nasri M.. Analysis of novel angiotensin I-converting enzyme inhibitory peptides from enzymatic hydrolysates of cuttlefish (Sepia officinalis) muscle proteins. J. Agric. Food Chem., 58, 5763-5769, 2010.
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