BIOPEP-UWM: Report

ID 337
Name Bitter peptide
sequence
LW
Function:
Bitter taste
 
Number of residues
2
Activity code
bi
Activity :
bitter
Chemical mass 317.3819 Monoisotopic mass 317.1734
EC50 :
0.00 µM


Bibliographic data:
Authors
Asao M., Iwamura H., Akamatsu M., Fujita T.
Title
Quantitative structure-activity relationships of the bitter thresholds of amino acids, peptides, and their derivatives. J. Med. Chem., 30, 1873-1879, 1987
Year Source
1987 Journal


Additional information:

BIOPEP-UWM database of sensory peptides and amino acids


SMILES: N[C@H](C(=O)N[C@H](C(=O)O)Cc1c[nH]c2c1cccc2)CC(C)C

InChI=1S/C17H23N3O3/c1-10(2)7-13(18)16(21)20-15(17(22)23)8-11-9-19-14-6-4-3-5-12(11)14/h3-6,9-10,13,15,19H,7-8,18H2,1-2H3,(H,20,21)(H,22,23)/t13-,15-/m0/s1

InChIKey: BQVUABVGYYSDCJ-ZFWWWQNUSA-N


Another references concerning bitterness:

Guigoz Y., Solms J., 1974, Isolation of a bitter peptide from „Alpkase”, a Swiss mountains-cheese. Lebensm. Wiss. Technol., 7, 356-357

Lemieux L., Simard R. E., 1992, Bitter flavour in dairy products. II. A review of bitter peptides from caseins: their formation, isolation and identification, structure masking and inhibition. Lait, 72, 335-382

Collantes E. R., Dunn W. J., 1995, Amino acid side chain descriptors for quantitative structure-activity relationship studies of peptide analogues. J. Med. Chem., 38, 2705-2713

Kohl S., Behrens M., Dunkel A., Hofmann T., Meyerhof W., 2013, Amino acids and peptides activate at least five members of the human bitter taste receptor family. J. Agric. Food Chem., 61, 53-60


Peptide found in chum salmon muscle protein hydrolysate.

Ono S., Hosokawa M., Miyashita K., Takahashi K., 2003, Isolation of peptides with angiotensin I-converting enzyme inhibitory effect derived from hydrolysate of upstream chum salmon muscle. J. Food Sci., 68, 1611-1614

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


Inhibitor of Dipeptidyl-peptidase III (EC 3.4.14.4) (MEROPS ID: M49.001) according to the BIOPEP-UWM database of bioactive peptides; the BRENDA database
Inhibitor of Dipeptidyl-peptidase IV (EC 3.4.14.5) (MEROPS ID: S09.003) according to the BIOPEP-UWM database of bioactive peptides (ID 8688)
Inhibitor of Angiotensin-converting enzyme (EC 3.4.15.1) (MEROPS ID: M02-001) according to the AHTPDB database; the BindingDB database; the BIOPEP-UWM database of bioactive peptides (ID 3389); the BRENDA database; the EROP-Moscow database
Inhibitor of Renin (EC 3.4.23.15) (MEROPS ID: A01.007) according to the BIOPEP database of bioactive peptides (ID 2832); the BRENDA database
Antioxidative peptide according to the BIOPEP-UWM database of bioactive peptides (ID 8462)


Database reference:
AHTPDB: ID 1086; 1172; 1378; 1385; 1445; 1469; 1860; 2043; 2079; 2105; 2150; 2606; 2789; 3298; 3575; 3763; 3855; 3992; 4098; 4141; 4201; 4238; 4389; 4468; 4714; 4952; 5162; 5612; 6161; 6273; 6373

BindingDB: ID 50049754

BioPepDB: ID biopep00934

BIOPEP-UWM database of bioactive peptides: ID 2832; 3389; 8462; 8688; 9498

BitterDB: ID 828

BRENDA: Ligand Leu-Trp

ChEBI: ID 73590

ChEMBL: ID CHEMBL56154

ChemSpider: ID 5360459

EROP-Moscow: ID E09194

J-GLOBAL: ID 200907041657441765

MBPDB: peptide LW

Metabolights: ID MTBLC73590

Nikkaji: ID J151.283H

PubChem: ID 6992319

SATPdb: ID satpdb27808

SureChEMBL: ID SCHEMBL5369872

ZINC: ID ZINC01570252