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Peptide record

TPDB48059

ACE inhibitor ACE inhibitors Antihypertensive Neuropeptide standard
3 amino acids
Basic Information
3D PDB MODEL
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TPDB48059
ACE inhibitor
ACE inhibitors Antihypertensive Neuropeptide
Cardiometabolic peptides Neuroactive peptides
Peptipedia AHTPDB AHTpin
standard
No
A 3-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
FNQ
Physicochemical Analysis
C18H25N5O6
ARDCEGHILKMPSTWYV
NQF
407.43
6.02
0
0
1
-0
-0.13
-1.400
0.00
Mammalian: 1.1 hour Yeast: 3 min E.coli: 2 min
0
0.00
2
Residue Composition
number
0
A
0
R
1
N
0
D
0
C
0
E
1
Q
0
G
0
H
0
I
0
L
0
K
0
M
1
F
0
P
0
S
0
T
0
W
0
Y
0
V
Amino Acid Distribution
A: 0 R: 0 N: 1 D: 0 C: 0 E: 0 Q: 1 G: 0 H: 0 I: 0 L: 0 K: 0 M: 0 F: 1 P: 0 S: 0 T: 0 W: 0 Y: 0 V: 0
Chemical Descriptors
3
C18H25N5O6
407.43
6.02
-0
-0.13
-1.400
407.4200
407.1799
Evidence Records 2 records
Evidence 1 Activity

Activity

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

Source & Reference

NA
Yano S., Suzuki K., Funatsu G.
Isolation from alpha-zein of thermolysin peptides with angiotensin I-converting enzyme inhibitory activity. Biosci. Biotech. Biochem., 60(4), 661-663 (1996)
1996
Journal

Other

3
BIOPEP-UWM database of bioactive peptides SMILES: [H][C@](N)(Cc1ccccc1)C(=O)N[C@@]([H])(CC(N)=O)C(=O)N[C@@]([H])(CCC(N)=O)C(O)=O InChI=1S/C18H25N5O6/c19-11(8-10-4-2-1-3-5-10)16(26)23-13(9-15(21)25)17(27)22-12(18(28)29)6-7-14(20)24/h1-5,11-13H,6-9,19H2,(H2,20,24)(H2,21,25)(H,22,27)(H,23,26)(H,28,29)/t11-,12-,13-/m0/s1 InChIKey=MRNRMSDVVSKPGM-AVGNSLFASA-N Information concerning Angiotensin-Converting Enzyme (ACE) is available in MEROPS database of proteolytic enzymes (http://merops.sanger.ac.uk/) ID: XM02-00. 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
335.00 µM
Inhibitor of Angiotensin-Converting Enzyme (ACE) (EC 3.4.15.1) (MEROPS ID: XM02-001)
ACE inhibitor
ah

Source & Reference

AHTPDB
Yano S., Suzuki K., Funatsu G.
Isolation from alpha-zein of thermolysin peptides with angiotensin I-converting enzyme inhibitory activity. Biosci. Biotech. Biochem., 60(4), 661-663 (1996)
1996
Journal

Other

Source Activity Label Source Definition
Antihypertensive
AHTPDB manually curated experimentally validated antihypertensive peptide annotation.
3
BIOPEP-UWM database of bioactive peptides SMILES: [H][C@](N)(Cc1ccccc1)C(=O)N[C@@]([H])(CC(N)=O)C(=O)N[C@@]([H])(CCC(N)=O)C(O)=O InChI=1S/C18H25N5O6/c19-11(8-10-4-2-1-3-5-10)16(26)23-13(9-15(21)25)17(27)22-12(18(28)29)6-7-14(20)24/h1-5,11-13H,6-9,19H2,(H2,20,24)(H2,21,25)(H,22,27)(H,23,26)(H,28,29)/t11-,12-,13-/m0/s1 InChIKey=MRNRMSDVVSKPGM-AVGNSLFASA-N Information concerning Angiotensin-Converting Enzyme (ACE) is available in MEROPS database of proteolytic enzymes (http://merops.sanger.ac.uk/) ID: XM02-00. 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