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MYP_137961
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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
10 amino acids
C51H74N16O15
Standard
Sequence
VSRHFASYAN
Physicochemical Analysis
1151.23 Da
8.73
0.82
0.56
0.0820
-0.35
0.57
-0.03
60.83
49.00
0.2000
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
519.58
-6.26
19.0
17.0
34.0
82.0
3.0
10.0
Structural Visualization
3D PDB MODEL
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2D CHEMICAL STRUCTURE
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Experimental Records
RECORD: Rec_0314210 VERIFIED: NO
Provenance & Taxonomy
not reported [other]
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
Bio-Activity Profile
Enzyme inhibitory ACE inhibitory
ACE
RECORD: Rec_0366776 VERIFIED: YES
Provenance & Taxonomy
Stichopus horrens [Animal]
Angiotensin
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
Bio-Activity Profile
Enzyme inhibitory ACE inhibitory
Angiotensin-I converting enzyme
210±0 μM
IC50
RECORD: Rec_0418689 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)
210.0
PaperForghani B., Zarei M., Ebrahimpour A., Philip R., Bakar J., Hamid A. A., Saari N.. Purification and characterization of angiotensin converting enzyme-inhibitory peptides derived from Stichopus horrens: Stability study against the ACE and inhibition kinetics. J. Funct. Foods, 20, 276-290, 2016.