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MYP_160460
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Basic Information
Unnamed
Cardiovascular ▸ Blood pressure regulation ▸ Antihypertensive
Enzyme / Catalytic activity ▸ Isomerase
Enzyme modulation ▸ Enzyme inhibition ▸ ACE inhibition ▸ ACE inhibitory
Enzyme modulation ▸ Enzyme inhibition ▸ DPP-IV inhibition ▸ DPP-IV inhibitory
Enzyme modulation ▸ Enzyme inhibition ▸ Tripeptidyl Peptidase II Inhibitory
Hormonal / Endocrine ▸ Hormone peptide
Insecticidal/Pest control ▸ Insecticidal activity
Metabolic ▸ Glucose metabolism ▸ Antidiabetic
Other / Curated residual function label ▸ Generic enzyme inhibition annotation
Sensory / Food function ▸ Taste-active peptide
Standard
2 amino acids
C8H14N2O3
Standard
Sequence
AP
Physicochemical Analysis
186.21 Da
5.57
-0.20
-0.39
-0.1021
0.10
0.31
0.37
101.30
50.00
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
83.63
-0.59
2.0
3.0
2.0
13.0
1.0
1.0
Structural Visualization
3D PDB MODEL
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2D CHEMICAL STRUCTURE
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Experimental Records
RECORD: Rec_0305377 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_0325638 VERIFIED: YES
Provenance & Taxonomy
synthetic construct [Synthetic]
32630.0
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
Bio-Activity Profile
Tripeptidyl Peptidase II Inhibitory
Tripeptidyl peptidase II / CCK-8-inactivating peptidase
PaperGanellin C. R., Bishop P. B., Bambal R. B., Chan S. M., Law J. K., Marabout B., Luthra P. M., Moore A. N., Peschard O., Bourgeat P., Rose C., Vargas F.. Inhibitors of tripeptidyl peptidase II. 2. Generation of the first novel lead inhibitor of cholecystokinin-8-inactivating peptidase: a strategy for the design of peptidase inhibitors. J. Med. Chem., 43, 664-674, 2000. PMID10691692 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/10691692/
RECORD: Rec_0328028 VERIFIED: YES
Provenance & Taxonomy
not reported [other]
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
Bio-Activity Profile
Antidiabetic DPP-IV Inhibitory
Dipeptidyl peptidase IV
7950.0
IC50
PaperHatanaka T., Inoue Y., Arima J., Kumagai Y., Usuki H., Kawakami K., Kimura M., Mukaihara T.. Production of dipeptidyl peptidase IV inhibitory peptides from defated rice bran. Food Chem., 134, 797-802.
RECORD: Rec_0372966 VERIFIED: YES
Provenance & Taxonomy
not reported [other]
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
Bio-Activity Profile
Peptidylprolyl Isomerase Isnhibitor
30000.0
PaperDemange L., Moutiez M., Vaudry K., Dugave C.. Interaction of human cyclophilin hCyp-18 with short peptides suggests the existence of two functionally independent subsites. FEBS Lett., 505, 191-195, 2001.
RECORD: Rec_0395301 VERIFIED: YES
Provenance & Taxonomy
Amaranthus hypochondriacus [Plant]
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
Bio-Activity Profile
Enzyme inhibitory
230 μM
IC50
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