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MYP_071605
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Basic Information
Angiotensin I converting enzyme inhibitior 17
Cardiovascular ▸ Blood pressure regulation ▸ Antihypertensive
Enzyme modulation ▸ Enzyme inhibition ▸ ACE inhibition ▸ ACE inhibitory
Other / Curated residual function label ▸ Generic enzyme inhibition annotation
Standard
5 amino acids
C28H52N6O6S
Standard
Sequence
LLMPK
Physicochemical Analysis
600.81 Da
8.75
0.76
0.55
0.1518
0.80
0.17
0.28
95.88
156.00
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
196.95
0.82
6.0
8.0
19.0
41.0
1.0
4.0
Structural Visualization
3D PDB MODEL
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2D CHEMICAL STRUCTURE
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Experimental Records
RECORD: Rec_0241819 VERIFIED: YES
Provenance & Taxonomy
Mactra veneriformis [Animal]
Angiotensin
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
Bio-Activity Profile
Enzyme inhibitory ACE inhibitory
Angiotensin-converting enzyme
686.2 μM
IC50
RECORD: Rec_0310517 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)
686.2
PaperLiu R., Zhu Y., Chen J., Wu H., Shi L., Wang X., Wang L.. Characterization of ACE inhibitory peptides from Mactra veneriformis hydrolysate by nano-liquid chromatography electrospray ionization mass spectrometry (Nano-LC-ESI-MS) and molecular docking. Mar. Drugs, 12, 3917-3928, 2014. Evidence URLhttps://pmc.ncbi.nlm.nih.gov/articles/PMC4113806/