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MYP_134047
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Basic Information
Unnamed
Cardiovascular ▸ Blood pressure regulation ▸ Antihypertensive
Enzyme modulation ▸ Enzyme inhibition ▸ ACE inhibition ▸ ACE inhibitory
Enzyme modulation ▸ Enzyme inhibition ▸ DPP-IV inhibition ▸ DPP-IV inhibitory
Metabolic ▸ Glucose metabolism ▸ Antidiabetic
Other / Curated residual function label ▸ Generic enzyme inhibition annotation
Standard
2 amino acids
C11H21N3O5
Standard
Sequence
KE
Physicochemical Analysis
275.30 Da
6.22
-0.23
-0.44
-0.1164
-3.70
0.78
-1.12
5.00
0.00
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
155.74
-1.12
5.0
5.0
10.0
19.0
0.0
1.0
Structural Visualization
3D PDB MODEL
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2D CHEMICAL STRUCTURE
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Experimental Records
RECORD: Rec_0038979 VERIFIED: YES
Provenance & Taxonomy
Bos taurus [Animal]; Poaceae [Plant]; Sus scrofa [Animal]; Gallus gallus [Animal]
9913; 4479; 9823; 9031
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
Bio-Activity Profile
Antihypertensive
PaperPeptides with angiotensin I converting enzyme (ACE) inhibitory activity generated from porcine skeletal muscle proteins by the action of meat-borne Lactobacillus PMID23806758 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/23806758/
RECORD: Rec_0123191 VERIFIED: YES
Provenance & Taxonomy
synthetic construct [Synthetic]
32630.0
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
Bio-Activity Profile
Antidiabetic DPP-IV inhibitory
human dipeptidyl peptidase IV
PaperLan V. T. T., Ito K., Ohno M., Motoyama T., Ito S., Kawarasaki Y.. Analyzing a dipeptide library to identify human dipeptidyl peptidase IV inhibitor. Food Chemistry 175, 66-73. PMID25577052 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/25577052/
RECORD: Rec_0181486 VERIFIED: YES
Provenance & Taxonomy
Sus scrofa [Animal]
ACE-inhibitory peptide
9823
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
Bio-Activity Profile
Antihypertensive
PaperPeptides with angiotensin I converting enzyme (ACE) inhibitory activity generated from porcine skeletal muscle proteins by the action of meat-borne Lactobacillus. PMID23806758 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/23806758/
RECORD: Rec_0289315 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)
Papervan Platerink C. J., Janssen H.-G. M., Haverkamp J.. Application of at-line two-dimensional liquid chromatography-mass spectrometry for identification of small hydrophilic angiotensin I-inhibiting peptides in milk hydrolysates. Anal. Bioanal. Chem., 2008, 391, 299-307.
RECORD: Rec_0289514 VERIFIED: YES
Provenance & Taxonomy
not reported [other]
ACE inhibitory peptide
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
Bio-Activity Profile
Enzyme inhibitory ACE inhibitory Antihypertensive
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