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MYP_027165
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Basic Information
Unnamed
Enzyme modulation ▸ Enzyme inhibition ▸ ACE inhibition ▸ ACE inhibitory
Enzyme modulation ▸ Enzyme inhibition ▸ BChE Inhibitory
Neurological / Signaling ▸ Neuroactive peptide
Standard
6 amino acids
C32H52N10O9
Standard
Sequence
QVFRAT
Physicochemical Analysis
720.82 Da
9.75
0.76
0.56
0.1267
0.02
0.72
-0.09
-4.23
65.00
0.1667
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
334.04
-3.35
12.0
10.0
22.0
51.0
1.0
6.0
Structural Visualization
3D PDB MODEL
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2D CHEMICAL STRUCTURE
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Experimental Records
RECORD: Rec_0275467 VERIFIED: YES
Provenance & Taxonomy
Pisum sativum [Plant]
3888.0
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
Bio-Activity Profile
Acetylcholinesterase inhibitory
437.0
PaperAsen N.D., Okagu O.D., Udenigwe C.C., Aluko R.E.. In vitro inhibition of acetylcholinesterase activity by yellow field pea (Pisum sativum) protein-derived peptides as revealed by kinetics and molecular docking. Front. Nutr., 9, 2022.
RECORD: Rec_0412995 VERIFIED: YES
Provenance & Taxonomy
Pisum sativum [Plant]
3888.0
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
Bio-Activity Profile
Neuroactive BChE Inhibitory
436.52
IC50
PaperAsen N.D., Okagu O.D., Udenigwe C.C., Aluko R.E.. Butyrylcholinesterase inhibitory activity of peptides identified from yellow field pea (Pisum sativum) enzymatic protein hydrolysates. J. Funct. Foods, 106, 105590, 2023.