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MYP_032054
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Basic Information
Unnamed
Cardiovascular ▸ Blood pressure regulation ▸ Antihypertensive
Enzyme modulation ▸ Enzyme inhibition ▸ ACE inhibition ▸ ACE inhibitory
Other / Curated residual function label ▸ Generic enzyme inhibition annotation
Standard
3 amino acids
C13H23N3O4
Standard
Sequence
PGL
Physicochemical Analysis
285.34 Da
5.96
-0.04
-0.10
-0.0138
0.60
0.32
0.55
6.67
130.00
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
107.53
-0.53
4.0
4.0
7.0
20.0
1.0
2.0
Structural Visualization
3D PDB MODEL
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2D CHEMICAL STRUCTURE
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Experimental Records
RECORD: Rec_0233967 VERIFIED: YES
Provenance & Taxonomy
not reported [other]
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
None
None
Bio-Activity Profile
Antihypertensive
PaperAHTPDB: a comprehensive platform for analysis and presentation of antihypertensive peptides PMID25392419 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/25392419/
RECORD: Rec_0269125 VERIFIED: YES
Provenance & Taxonomy
not reported [other]
Angiotensin
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
Bio-Activity Profile
Enzyme inhibitory
13.93 μM
IC50
RECORD: Rec_0395434 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)
13.93
PaperByun H.-G., Kim S.-K.. Structure and activity of angiotensin I-converting enzyme inhibitory peptides derived from Alaskan pollack skin. Bioch. Mol. Biol., 35, 2, 239-243, 2002.
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