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MYP_054966
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Basic Information
Unnamed
Cardiovascular ▸ Blood pressure regulation ▸ Antihypertensive
Enzyme modulation ▸ Enzyme inhibition ▸ ACE inhibition ▸ ACE inhibitory
Enzyme modulation ▸ Enzyme inhibition ▸ Calpain-1 inhibitory
Enzyme modulation ▸ Enzyme inhibition ▸ DPP-IV inhibition ▸ DPP-IV inhibitory
Metabolic ▸ Glucose metabolism ▸ Antidiabetic
Neurological / Signaling ▸ Neuropeptide activity ▸ Neuropeptide
Other / Curated residual function label ▸ Generic enzyme inhibition annotation
Regulatory peptide ▸ Stimulation activity
Sensory / Food function ▸ Taste-active peptide ▸ Bitter peptide
Standard
2 amino acids
C12H24N2O3
Standard
Sequence
IL
Physicochemical Analysis
244.33 Da
5.53
-0.24
-0.44
-0.1200
4.15
0.79
1.22
101.30
390.00
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
92.42
0.98
3.0
3.0
7.0
17.0
0.0
1.0
Structural Visualization
3D PDB MODEL
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2D CHEMICAL STRUCTURE
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Experimental Records
RECORD: Rec_0151325 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
20000 μM
IC50
PaperStructural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides. PMID16448176 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/16448176/
RECORD: Rec_0152690 VERIFIED: YES
Provenance & Taxonomy
synthetic construct [Synthetic]
32630.0
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
Bio-Activity Profile
Antihypertensive ACE inhibitory
Angiotensin-converting enzyme (ACE)
54.95 μM
IC50
PaperWu J., Aluko R. E., Nakai S.. Structural requirements of angiotensin I-converting enzyme inhibitory activity: quantitative structure-activity relationship study of di- and tripeptides. J. Agric. Food Chem., 54, 732-738, 2006.
RECORD: Rec_0245690 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
PaperThree-dimensional holograph vector of atomic interaction field (3D-HoVAIF): a novel rotation-translation invariant 3D structure descriptor and its applications to peptides. PMID17654623 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/17654623/
RECORD: Rec_0284361 VERIFIED: YES
Provenance & Taxonomy
Glycine max [Plant]
Glycinin, beta-conGlycinin
3847
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
Bio-Activity Profile
ACE inhibitory Antihypertensive
Angiotensin-converting enzyme
43.9 μM
IC50
PaperLC-MS/MS coupled with QSAR modeling in characterising of angiotensin I-converting enzyme inhibitory peptides from soybean proteins PMID23871011 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/23871011/
RECORD: Rec_0327344 VERIFIED: YES
Provenance & Taxonomy
not reported [other]
Structure & Mods
branched peptide architecture [Branched]
canonical L-amino-acid peptide [L]
Bio-Activity Profile
Stimulatory
PaperMorifuji M., Koga J., Kawanaka K., Higuchi M.. Branched-chain amino acid-containing dipeptides, identified from whey protein hydrolysates, stimulate glucose uptake in L6 myotubes and isolated skeletal muscles. J. Nutr. Sci. Vitaminol., 55, 81-86, 2009.
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