Peptide record

TPDB48084

ACE inhibitor from sake ACE inhibitors Antihypertensive Neuropeptide standard
4 amino acids
Basic Information
3D PDB MODEL
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TPDB48084
ACE inhibitor from sake
ACE inhibitors Antihypertensive Neuropeptide
Cardiometabolic peptides Neuroactive peptides
Peptipedia AHTPDB AHTpin
standard
No
A 4-aa standard natural multi-activity (ACE inhibitors, Antihypertensive, and Neuropeptide) peptide sequence curated from Peptipedia, AHTPDB, and AHTpin, with an available 3D structural model.
Sequence
YGGY
Physicochemical Analysis
C22H26N4O7
ARNDCEQHILKMFPSTWV
GY
458.47
5.88
0
0
2
-0
-1.86
-0.850
0.00
Mammalian: 2.8 hour Yeast: 10 min E.coli: 2 min
2980
649.99
2
Residue Composition
number
0
A
0
R
0
N
0
D
0
C
0
E
0
Q
2
G
0
H
0
I
0
L
0
K
0
M
0
F
0
P
0
S
0
T
0
W
2
Y
0
V
Amino Acid Distribution
A: 0 R: 0 N: 0 D: 0 C: 0 E: 0 Q: 0 G: 2 H: 0 I: 0 L: 0 K: 0 M: 0 F: 0 P: 0 S: 0 T: 0 W: 0 Y: 2 V: 0
Chemical Descriptors
4
C22H26N4O7
458.47
5.88
-0
-1.86
-0.850
458.4634
458.1795
Evidence Records 2 records
Evidence 1 Activity

Activity

IC50
ACE inhibitors
3.40 µM
Inhibitor of Angiotensin-Converting Enzyme (ACE) (EC 3.4.15.1) (MEROPS ID: XM02-001)
ACE inhibitor
ah

Source & Reference

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

Other

4
BIOPEP-UWM database of bioactive peptides SMILES: [H][C@](N)(Cc1ccc(O)cc1)C(=O)NCC(=O)NCC(=O)N[C@@]([H])(Cc1ccc(O)cc1)C(O)=O InChI=1S/C22H26N4O7/c23-17(9-13-1-5-15(27)6-2-13)21(31)25-11-19(29)24-12-20(30)26-18(22(32)33)10-14-3-7-16(28)8-4-14/h1-8,17-18,27-28H,9-12,23H2,(H,24,29)(H,25,31)(H,26,30)(H,32,33)/t17-,18-/m0/s1 InChIKey=KRSNERDYZXTSTQ-ROUUACIJSA-N Information concerning Angiotensin-Converting Enzyme (ACE) is available in MEROPS database of proteolytic enzymes (http://merops.sanger.ac.uk/) ID: XM02-001 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
Evidence 2 Activity

Activity

IC50
Antihypertensive
3.40 µM
Inhibitor of Angiotensin-Converting Enzyme (ACE) (EC 3.4.15.1) (MEROPS ID: XM02-001)
ACE inhibitor
ah

Source & Reference

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

Other

Source Activity Label Source Definition
Antihypertensive
AHTPDB manually curated experimentally validated antihypertensive peptide annotation.
4
BIOPEP-UWM database of bioactive peptides SMILES: [H][C@](N)(Cc1ccc(O)cc1)C(=O)NCC(=O)NCC(=O)N[C@@]([H])(Cc1ccc(O)cc1)C(O)=O InChI=1S/C22H26N4O7/c23-17(9-13-1-5-15(27)6-2-13)21(31)25-11-19(29)24-12-20(30)26-18(22(32)33)10-14-3-7-16(28)8-4-14/h1-8,17-18,27-28H,9-12,23H2,(H,24,29)(H,25,31)(H,26,30)(H,32,33)/t17-,18-/m0/s1 InChIKey=KRSNERDYZXTSTQ-ROUUACIJSA-N Information concerning Angiotensin-Converting Enzyme (ACE) is available in MEROPS database of proteolytic enzymes (http://merops.sanger.ac.uk/) ID: XM02-001 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
Additional Detail Fields 1 fields
4