‹ ›
MYP_016841
← PREVIOUS NEXT → BACK
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
C18H25N5O6
Standard
Sequence
FNQ
Physicochemical Analysis
407.42 Da
5.53
-0.24
-0.44
-0.0800
-1.40
0.73
-0.15
-18.47
0.00
0.3333
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
207.70
-2.25
6.0
6.0
12.0
29.0
1.0
4.0
Structural Visualization
3D PDB MODEL
Drag to rotate. Click a residue or atom to inspect it; the selected residue is highlighted in amber in the current view mode. Use the buttons to zoom.
2D CHEMICAL STRUCTURE
Drag to move
Drag to move. Use the buttons to zoom.
Experimental Records
RECORD: Rec_0231842 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)
335.0
IC50
PaperYano S., Suzuki K., Funatsu G.. Isolation from alpha-zein of thermolysin peptides with angiotensin I-converting enzyme inhibitory activity. Biosci. Biotech. Biochem., 60(4), 661-663 (1996).
RECORD: Rec_0308590 VERIFIED: NO
Provenance & Taxonomy
Amaranthus hypochondriacus [Plant]
ACE-inhibitory peptide
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
Bio-Activity Profile
Antihypertensive
PaperBioactive peptides in amaranth (Amaranthus hypochondriacus) seed PMID18211015 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/18211015/
RECORD: Rec_0362279 VERIFIED: YES
Provenance & Taxonomy
Amaranthus hypochondriacus [Plant]; Zea mays [Plant]
ACE inhibitory peptide
28502, 4577
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
Bio-Activity Profile
Enzyme inhibitory Neuropeptide ACE inhibitory Antihypertensive
Angiotensin-converting enzyme
335 μM
IC50
PaperBioactive peptides in amaranth (Amaranthus hypochondriacus) seed | Isolation from alpha-zein of thermolysin peptides with angiotensin I-converting enzyme inhibitory activity PMID18211015;8829536 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/18211015/
RECORD: Rec_0367484 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
335 μM
IC50
PaperIntegration of QSAR modelling and QM/MM analysis to investigate functional food peptides with antihypertensive activity
RECORD: Rec_0377433 VERIFIED: YES
Provenance & Taxonomy
Viridiplantae [Plant]; Poaceae [Plant]; Insecta [Animal]
33090; 4479; 50557
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
Bio-Activity Profile
Antihypertensive
PaperBioactive peptides in amaranth (Amaranthus hypochondriacus) seed PMID18211015 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/18211015/
FIRST PREV 1 2 3 NEXT LAST
Showing 5 records on this page · Page 2 of 3