BIOPEP-UWM: Report

ID 29
Name bitter peptide
sequence
GRP

Function:
(Rcaf) 1.25
 
Number of residues
3
Activity code
bi
Activity :
bitter
Chemical mass 328.3665 Monoisotopic mass 328.1854
EC50 :
0.00 µM



Bibliographic data:
Authors
Otagiri K., Nosho Y., Shinoda I., Fukui H., Okai H.
Title
Studies on a model bitter peptides including arginine, proline and phenylalanine residues. I. Bitter taste of di- and tripeptides and bitterness increase of the model peptides by extension of the peptide chain. Agric. Biol. Chem., 49, 1019-1026, 1985
Year Source
1985 Journal



Additional information:
BIOPEP database of sensory peptides and amino acids


SMILES: NCC(=O)N[C@@H](CCCNC(=N)N)C(=O)N1CCC[C@@H]1C(=O)O

InChI=1S/C13H24N6O4/c14-7-10(20)18-8(3-1-5-17-13(15)16)11(21)19-6-2-4-9(19)12(22)23/h8-9H,1-7,14H2,(H,18,20)(H,22,23)(H4,15,16,17)/t8-,9+/m0/s1

InChIKey: VXKCPBPQEKKERH-DTWKUNHWSA-N


Inhibitor of Angiotensin-Converting Enzyme (ACE) (EC 3.4.15.1) (MEROPS ID: XM02-001) according to AHTPDB database; BIOPEP database of bioactive peptides and EROP-Moscow database


Peptide found in sardine muscle protein hydrolysate.

Matsufuji H., Matsui T., Seki E., Osajima K., Nakashima M., Osajima Y., 1994, Angiotensin I-converting enzyme inhibitory peptides in an alkaline proteinase hydrolysate derived from sardine muscle. Biosci. Biotech. Biochem., 58, 2244-2245

Peptide found in amaranth protein hydrolysate.

Barba de la Rosa A. P., Barba Montoya A., Martínez-Cuevas P., Hernández-Ledesma B., León-Galván M. F., De León-Rodríguez A., González C., 2010, Tryptic amaranth glutelin digests induce endothelial nitric oxide production through inhibition of ACE: antihypertensive role of amaranth peptides. Nitric Oxide, 23, 106-111



Database reference:
AHTPDB: ID 1100; 1139; 1529; 3082; 3492; 4074; 4545; 4630; 4826; 5081; 5211; 5590; 6179; 6362

BIOPEP database of bioactive peptides: ID 3378

EROP-Moscow: ID E01338