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MYP_127521
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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
C12H21N3O5
Standard
Sequence
TAP
Physicochemical Analysis
287.31 Da
5.18
-0.60
-0.79
-0.2006
-0.17
0.21
0.23
70.87
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
132.96
-1.73
4.0
5.0
5.0
20.0
1.0
2.0
Structural Visualization
3D PDB MODEL
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2D CHEMICAL STRUCTURE
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Experimental Records
RECORD: Rec_0213665 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
5.46 pIC50
pIC50
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_0231085 VERIFIED: YES
Provenance & Taxonomy
not reported [other]
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
None
None
Bio-Activity Profile
Antihypertensive
PaperAHTPDB: a comprehensive platform for analysis and presentation of antihypertensive peptides PMID25392419 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/25392419/
RECORD: Rec_0263899 VERIFIED: NO
Provenance & Taxonomy
Amaranthus hypochondriacus [Plant]
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
Bio-Activity Profile
Enzyme inhibitory Neuropeptide
Angiotensin-converting enzyme
RECORD: Rec_0267098 VERIFIED: YES
Provenance & Taxonomy
Homo sapiens [Animal]
9606;0
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
Bio-Activity Profile
Antihypertensive ACE inhibitory
Angiotensin-converting enzyme (ACE)
3.5
IC50
PaperKohmura M., Nio N., Kubo K., Minoshima Y., Munekata E., Ariyoshi Y.. Inhibition of angiotensin-converting enzyme by synthetic peptides of human beta-casein. Agric. Biol. Chem., 53, 2107-2114, 1989.
RECORD: Rec_0272196 VERIFIED: YES
Provenance & Taxonomy
Amaranthus hypochondriacus [Plant]
ACE inhibitory peptide
28502
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
Bio-Activity Profile
Enzyme inhibitory Neuropeptide ACE inhibitory Antihypertensive
Angiotensin-converting enzyme
PaperBioactive peptides in amaranth (Amaranthus hypochondriacus) seed PMID18211015 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/18211015/
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