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Peptide record

TPDB47665

ACE inhibitor ACE inhibitors Antihypertensive Bitter Neuropeptide Umami standard
3 amino acids
Basic Information
3D PDB MODEL
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TPDB47665
ACE inhibitor
ACE inhibitors Antihypertensive Bitter Neuropeptide Umami
Cardiometabolic peptides Neuroactive peptides Food sensory peptides
Peptipedia AHTPDB AHTpin Tastepeptides-Meta
standard
No
A 3-aa standard natural multi-activity (ACE inhibitors, Antihypertensive, Bitter, and other sources) peptide sequence curated from Peptipedia, AHTPDB, AHTpin, and other sources, with an available 3D structural model.
Sequence
GGY
Physicochemical Analysis
C13H17N3O5
ARNDCEQHILKMFPSTWV
G
295.30
5.94
0
0
1
-0
-0.92
-0.700
0.00
Mammalian: 30 hour Yeast: >20 hour E.coli: >10 hour
1490
504.58
1
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
1
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: 1 V: 0
Chemical Descriptors
3
C13H17N3O5
295.30
5.94
-0
-0.92
-0.700
295.2905
295.1164
Evidence Records 2 records
Evidence 1 Activity

Activity

IC50
ACE inhibitors
1.30 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

3
BIOPEP database of bioactive peptides SMILES: NCC(=O)NCC(=O)N[C@@H](Cc1ccc(O)cc1)C(=O)O InChI=1S/C13H17N3O5/c14-6-11(18)15-7-12(19)16-10(13(20)21)5-8-1-3-9(17)4-2-8/h1-4,10,17H,5-7,14H2,(H,15,18)(H,16,19)(H,20,21)/t10-/m0/s1 InChIKey: INLIXXRWNUKVCF-JTQLQIEISA-N Information concerning Angiotensin-Converting Enzyme (ACE) is available in MEROPS database of proteolytic enzymes (http://merops.sanger.ac.uk/) ID: XM02-001 Inhibitor of citruline uptake in yeasts according to ChEMBL database 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
1.30 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.
3
BIOPEP database of bioactive peptides SMILES: NCC(=O)NCC(=O)N[C@@H](Cc1ccc(O)cc1)C(=O)O InChI=1S/C13H17N3O5/c14-6-11(18)15-7-12(19)16-10(13(20)21)5-8-1-3-9(17)4-2-8/h1-4,10,17H,5-7,14H2,(H,15,18)(H,16,19)(H,20,21)/t10-/m0/s1 InChIKey: INLIXXRWNUKVCF-JTQLQIEISA-N Information concerning Angiotensin-Converting Enzyme (ACE) is available in MEROPS database of proteolytic enzymes (http://merops.sanger.ac.uk/) ID: XM02-001 Inhibitor of citruline uptake in yeasts according to ChEMBL database 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
3