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MYP_146723
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Basic Information
49-61
Cardiovascular ▸ Blood pressure regulation ▸ Antihypertensive
Enzyme modulation ▸ Enzyme inhibition ▸ ACE inhibition ▸ ACE inhibitory
Other / Curated residual function label ▸ Generic enzyme inhibition annotation
Standard
13 amino acids
C71H105N17O19
Standard
Sequence
IHPFAQTQSLVYP
Physicochemical Analysis
1500.70 Da
6.74
-0.15
-0.41
-0.0118
0.07
0.26
0.27
63.02
90.00
0.1538
1490.00
1490.00
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
570.49
-3.94
18.0
20.0
42.0
107.0
5.0
14.0
Structural Visualization
3D PDB MODEL
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2D CHEMICAL STRUCTURE
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Experimental Records
RECORD: Rec_0367099 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)
19.0
IC50
PaperKohmura M., Nio N., Ariyoshi Y.. Inhibition of angiotensin-converting enzyme by synthetic peptide fragments of various beta-caseins. Agric. Biol. Chem., 54, 1101-1102, 1990.
RECORD: Rec_0412631 VERIFIED: YES
Provenance & Taxonomy
Bos taurus [Animal]
beta-Casein-derived
9913
Structure & Mods
synthetic linear peptide [Linear]
canonical L-amino-acid peptide [L]
Bio-Activity Profile
ACE inhibitory Antihypertensive
Angiotensin-converting enzyme (ACE)
19 μM
IC50
PaperInhibition of angiotensin-converting enzyme by synthetic peptide fragments of various β-caseins | Kohmura, M. et al. | DOI: 10.1271/bbb1961.54.1101 Evidence URLhttps://www.uniprot.org/uniprotkb/P02666/entry
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