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MYP_054636
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Basic Information
Unnamed
Antimicrobial
Antiparasitic ▸ Antimalarial
Antiparasitic ▸ Antiprotozoal ▸ Antimalarial ▸ Anti-Plasmodium
Antiparasitic ▸ General antiparasitic ▸ Antiparasitic
Cardiovascular ▸ Blood pressure regulation ▸ Antihypertensive
Enzyme modulation ▸ Enzyme inhibition ▸ ACE inhibition ▸ ACE inhibitory
Enzyme modulation ▸ Enzyme inhibition ▸ Protease inhibition
Enzyme modulation ▸ Enzyme inhibition ▸ Renin inhibition ▸ Renin inhibitory
Membrane / Ion-channel modulation ▸ Calcium channel modulation ▸ Calcium channel inhibitor
Neurological / Signaling ▸ Neuropeptide activity ▸ Neuropeptide
Other / Curated residual function label ▸ Generic enzyme inhibition annotation
Sensory / Food function ▸ Taste-active peptide ▸ Bitter peptide
Standard
2 amino acids
C15H22N2O4
Standard
Sequence
LY
Physicochemical Analysis
294.35 Da
5.52
-0.24
-0.45
-0.1205
1.25
0.52
0.66
5.00
195.00
0.5000
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
112.65
0.88
4.0
4.0
7.0
21.0
1.0
1.0
Structural Visualization
3D PDB MODEL
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2D CHEMICAL STRUCTURE
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Experimental Records
RECORD: Rec_0088892 VERIFIED: YES
Provenance & Taxonomy
synthetic construct [Synthetic]
Synthetic peptide
32630
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
Phenylsulfonyl
Aldehyde
Bio-Activity Profile
Antimicrobial Cysteine protease inhibitor Antiparasitic Antimalarial
Plasmodium falciparum W2
0.03 μM
IC50; Microscopy (Giemsa staining)
PMID14638488 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/14638488/
RECORD: Rec_0098434 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
PaperThree-dimensional holograph vector of atomic interaction field (3D-HoVAIF): a novel rotation-translation invariant 3D structure descriptor and its applications to peptides. PMID17654623 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/17654623/
RECORD: Rec_0109537 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)
18.0
IC50
PaperMatsufuji H., Matsui T., Seki E., Osajima K., Nakashima M., Osajima Y.. Angiotensin I-converting enzyme inhibitory peptides in an alkaline proteinase hydrolysate derived from sardine muscle. Biosci. Biotech. Biochem., 58, 2244-2245, 1994.
RECORD: Rec_0111946 VERIFIED: YES
Provenance & Taxonomy
Glycine max [Plant]
3847;0
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
Bio-Activity Profile
Antioxidant
PaperBeermann C., Euler M., Herzberg J., Stahl B.. Anti-oxidative capacity of enzymatically released peptides from soybean protein isolate. Eur. Food Res. Technol., 229 (2009), 637-644.
RECORD: Rec_0113691 VERIFIED: YES
Provenance & Taxonomy
Actinopterygii [Animal]
7898
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
Bio-Activity Profile
Antihypertensive
PaperAngiotensin I-converting enzyme inhibitory peptides in an alkaline protease hydrolyzate derived from sardine muscle PMID7765718 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/7765718/
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