BIOPEP-UWM: Report
ID | 3381 |
Name | ACE inhibitor |
sequence |
Function: | |||
Inhibitor of Angiotensin-Converting Enzyme (ACE) (EC 3.4.15.1) (MEROPS ID: M02-001) | |||
Number of residues | 2 |
Activity code | ah |
Activity : | ACE inhibitor |
|||
Chemical mass | 294.3453 | Monoisotopic mass | 294.1574 | |
EC50 : | 18.00 µM |
Bibliographic data: | |
Authors | |
Matsufuji H., Matsui T., Seki E., Osajima K., Nakashima M., Osajima Y. | |
Title | |
Angiotensin I-converting enzyme inhibitory peptides in an alkaline proteinase hydrolysate derived from sardine muscle. Biosci. Biotech. Biochem., 58, 2244-2245, 1994 | |
Year | Source |
1994 | Journal |
Additional information: |
BIOPEP-UWM database of bioactive peptides SMILES: [H][C@](N)(CC(C)C)C(=O)N[C@@]([H])(Cc1ccc(O)cc1)C(O)=O InChI=1S/C15H22N2O4/c1-9(2)7-12(16)14(19)17-13(15(20)21)8-10-3-5-11(18)6-4-10/h3-6,9,12-13,18H,7-8,16H2,1-2H3,(H,17,19)(H,20,21)/t12-,13-/m0/s1 InChIKey=LHSGPCFBGJHPCY-STQMWFEESA-N Information concerning Angiotensin-Converting Enzyme (ACE) is available in MEROPS database of proteolytic enzymes (http://merops.sanger.ac.uk/); ID: M02-001 Peptide was obtained from the following resources: soybean protein hydrolysate Beermann C., Euler M., Herzberg J., Stahl B., 2009, Anti-oxidative capacity of enzymatically released peptides from soybean protein isolate. Eur. Food Res. Technol., 229, 637–644 amaranth proteins: 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 bovine collagen hydrolysate: Herregods G., Van Camp J., Morel N., Ghesquière B., Gevaert K., Vercruysse L., Dierckx S., Quanten E., Smagghe G., 2011, Angiotensin I-converting enzyme inhibitory activity of gelatin hydrolysates and identification of bioactive peptides. J. Agric. Food Chem., 59, 552-558 Peptide reveals antihypertensive activity in vivo in spontaneously hypertensive rats: He R., Yang Y.-J., Wang Z., Xing C., Yuan J., Wang L.-F., Udenigwe C., Ju X.-R., 2019, Rapeseed protein-derived peptides, LY, RALP, and GHS, modulates key enzymes and intermediate products of renin–angiotensin system pathway in spontaneously hypertensive rat. Sci. Food, 3, 1 Antioxidative peptide according to the BIOPEP-UWM database of bioactive peptides (ID 7872) Inhibitor of Renin (EC 3.4.23.15) (MEROPS ID A01.007) according to the BIOPEP-UWM database of bioactive peptides (ID 9470) Bitter peptide according to the BIOPEP-UWM database of sensory peptides and amino acids (ID 482) |
Database reference: |
ACToR: ID 968-21-8 AHTPDB: ID 1096, 1173, 1354, 1358, 1361, 1408, 1976, 2958, 3053, 3055, 3178, 3387, 3520, 3856, 3993, 4099, 4717, 5163, 5546, 5613, 5773, 6174, 6365 BindingDB: ID 50348865 BioPepDB: ID biopep00936 BIOPEP-UWM database of bioactive peptides: ID 7872 BIOPEP-UWM database of sensory peptides and amino acids: ID 482 BRENDA: Ligand Leu-Tyr ChEBI: ID 73591 ChEMBL: ID CHEMBL56099 ChemIDplus: ID 968-21-8 ChemSpider: ID 63589 CTD: ID 968-21-8 eChemPortal: ID 968-21-8 EROP-Moscow: ID E01336 J-GLOBAL: ID 200907084889987250 Metabolights: ID MTBLC73591 Nikkaji: ID J80.048A PubChem: CID 70410 SATPdb: ID satpdb19431 SureChEMBL: ID SCHEMBL2474675 ZINC: ID ZINC000001708202 |