BIOPEP-UWM: Report

ID 3486
Name ACE inhibitor from sake lees
sequence
VW
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 303.3554 Monoisotopic mass 303.1578
EC50 :
1.40 µM


Bibliographic data:
Authors
Saito Y., Wanezaki K., Kawato A., Imayasu S.
Title
Structure and activity of angiotensin I converting enzyme inhibitory peptides from sake and sake lees. Biosci. Biotech. Biochem. 58(10), 1767-1771 (1994)
Year Source
1994 Journal


Additional information:
BIOPEP-UWM database of bioactive peptides


SMILES: N[C@@H](C(C)C)C(=O)N[C@@H](Cc1c2ccccc2[nH]c1)C(=O)O

InChI=1S/C16H21N3O3/c1-9(2)14(17)15(20)19-13(16(21)22)7-10-8-18-12-6-4-3-5-11(10)12/h3-6,8-9,13-14,18H,7,17H2,1-2H3,(H,19,20)(H,21,22)/t13-,14-/m0/s1

InChIKey: LZDNBBYBDGBADK-KBPBESRZSA-N


Information concerning Angiotensin-Converting Enzyme (ACE) is available in MEROPS database of proteolytic enzymes (http://merops.sanger.ac.uk/); ID: M02-001

Another value of peptide IC50(EC50)=1,6 uM

Cushman D. W., 1981. Angiotensin converting enzyme inhibitors:Evolution of a new class of antihypertensive drugs (page 19). in: Horovitz Z. P. (Ed.)(1981), Mechanisms of action and clinical implications, Urban & Schwarzenberg.

Another value of peptide IC50(EC50)=2,4 uM

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 muszle. J. Food Sci., 68, 1611-1614

Peptide found also 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 also 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

Antioxidative peptide according to the BIOPEP-UWM database of bioactive peptides (ID 8461)
Prolactin releasing activity according to the EROP-Moscow database
Inhibitor of Xanthine oxidase (EC 1.17.3.2) according to the EROP-Moscow 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 8928)
Inhibitor of alpha-glucosidase (EC 3.2.1.20) according to the BIOPEP-UWM database of bioactive peptides (ID 9387)


Database reference:
ACToR: ID 24587-37-9

AHTPDB: ID 1082; 1201; 1367; 1403; 1443; 1458; 1465; 1494; 1511; 1667; 1858; 1902; 1906; 1913; 1950; 2027; 2121; 2170; 2586; 2703; 2751; 2776; 2785; 2849; 2954; 3546; 3779; 4049; 4124; 4234; 4243; 4245; 4452; 4485; 4646; 4940; 4941; 4942; 5178; 5568; 5578; 5632; 5648; 6139; 6146; 6147; 6157; 6261; 6271; 6405; 6877

BindingDB: ID 50038066

BioPepDB: ID biopep01495

BIOPEP-UWM database of bioactive peptides: 8461; 8928; 9387

BRENDA: Ligand Val-Trp