BIOPEP-UWM: Report

ID 248
Name Umami peptide
sequence
EE

Function:
Umami taste; threshold 2.73 mM
 
Number of residues
2
Activity code
um
Activity :
umami
Chemical mass 276.2426 Monoisotopic mass 276.0953
EC50 :
0.00 µM



Bibliographic data:
Authors
Tamura M., Nakatsuka T., Tada M., Kawasaki Y., Kikuchi E., Okai H.
Title
The relationship between taste and primary structure of "Delicious Peptide" (Lys-Gly-Asp-Glu-Glu-Ser-Leu-Ala) from beef soup. Agric. Biol. Chem., 53, 319-325, 1989
Year Source
1989 Journal



Additional information:
BIOPEP database of sensory peptides and amino acids


SMILES: N[C@H](C(=O)N[C@H](C(=O)O)CCC(=O)O)CCC(=O)O

InChI=1S/C10H16N2O7/c11-5(1-3-7(13)14)9(17)12-6(10(18)19)2-4-8(15)16/h5-6H,1-4,11H2,(H,12,17)(H,13,14)(H,15,16)(H,18,19)/t5-,6-/m0/s1

InChIKey: KOSRFJWDECSPRO-WDSKDSINSA-N


Umami/salty at pH = 6;

Kuramitsu R., Takahashi M., Tahara K., Nakamura K., Okai H., 1996, Tastes produced by peptides containing ionic groups and by related compounds. Biosci., Biotech., Biochem., 60, 1637-1642

Another references concerning umami taste:

Arai S., Yamashita M., Noguchi M., Fujimaki M., 1973, Tastes of L-glutamyl oligopeptides in relation to their chromatographic properties. Agric. Biol. Chem., 37, 151-156

Noguchi M., Arai S., Yamashita M., Kato H., Fujimaki M., 1975, Isolation and identification of acidic oligopeptides occurring in a flavor potentiating fraction from a fish protein hydrolysate. J. Agric. Food Chem., 23, 49-53

Maehashi K., Matsuzaki M., Yamamoto Y., Udaka, S. 1999, Isolation of peptides from an enzymatic hydrolysate of food proteins and characterization of their taste properties. Biosci. Biotech. Biochem., 63, 555-559;

Monastyrskaia K., Lundstrom K., Plahl D., Acuna G., Schweitzer C., Malherbe P., Mutel V., 1999, Effect of the umami peptides on the ligand binding and function of rat mGlu4a receptor might implicate this receptor in the monosodium glutamate taste transduction. Brit. J. Pharmacol., 128, 1027-1034

Peptide found in chicken meat protein hydrolysate:

Maehashi K., Matsuzaki M., Yamamoto Y., Udaka, S. 1999, Isolation of peptides from an enzymatic hydrolysate of food proteins and characterization of their taste properties. Biosci. Biotech. Biochem., 63, 555-559


Inhibitor of Thymidylate synthase (EC 2.1.1.45) according to the BRENDA database
Inhibitor of Citrate-lyase deacetylase (EC 3.1.2.16) according to the BRENDA database
Inhibitor of Glutamate carboxypeptidase (EC 3.4.17.11) (MEROPS ID: M20.001) according to the BRENDA database
Inhibitor of Glutamate carboxypeptidase II (EC 3.4.17.21) (MEROPS ID: M28.010) according to the BRENDA database; the ChEMBL database; the PubChem database
Inhibitor of citrulline uptake in yeasts according to the ChEMBL database; the PubChem database
Peptide stimulating vasoactive substance release according to the BIOPEP database of bioactive peptides

Salty peptide according to the BIOPEP database of sensory peptides and amino acids (ID 249)
Bitterness suppressing peptide according to the BIOPEP database of sensory peptides and amino acids (ID 331)
Bitter peptide according to the BIOPEP database of sensory peptides and amino acids (ID 355)
Sweetness suppressing peptide according to the BIOPEP database of sensory peptides and amino acids (ID 368)



Database reference:
BindingDB: ID 50102260

BIOPEP database of bioactive peptides: ID 8329

BIOPEP database of sensory peptides and amino acids: ID 249; 331; 355; 368

BRENDA: Ligand Glu-Glu

ChEBI: ID 5390

ChEMBL: ID CHEMBL318315

ChemSpider: ID 388598

EROP-Moscow: ID E01846

KEGG Ligand: ID C01425

PubChem: ID 439500

ZINC: ID ZINC01529201