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Peptide record

TPDB48062

ACE inhibitor ACE inhibitors Antihypertensive Neuropeptide standard
3 amino acids
Basic Information
3D PDB MODEL
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TPDB48062
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
LQQ
Physicochemical Analysis
C16H29N5O6
ARNDCEGHIKMFPSTWYV
Q
387.44
6.02
0
0
1
-0
0.60
-1.067
130.00
Mammalian: 5.5 hour Yeast: 3 min E.coli: 2 min
0
0.00
2
Residue Composition
number
0
A
0
R
0
N
0
D
0
C
0
E
2
Q
0
G
0
H
0
I
1
L
0
K
0
M
0
F
0
P
0
S
0
T
0
W
0
Y
0
V
Amino Acid Distribution
A: 0 R: 0 N: 0 D: 0 C: 0 E: 0 Q: 2 G: 0 H: 0 I: 0 L: 1 K: 0 M: 0 F: 0 P: 0 S: 0 T: 0 W: 0 Y: 0 V: 0
Chemical Descriptors
3
C16H29N5O6
387.44
6.02
-0
0.60
-1.067
387.4302
387.2111
Evidence Records 2 records
Evidence 1 Activity

Activity

IC50
ACE inhibitors
100.00 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)(CC(C)C)C(=O)N[C@@]([H])(CCC(N)=O)C(=O)N[C@@]([H])(CCC(N)=O)C(O)=O InChI=1S/C16H29N5O6/c1-8(2)7-9(17)14(24)20-10(3-5-12(18)22)15(25)21-11(16(26)27)4-6-13(19)23/h8-11H,3-7,17H2,1-2H3,(H2,18,22)(H2,19,23)(H,20,24)(H,21,25)(H,26,27)/t9-,10-,11-/m0/s1 InChIKey=KAFOIVJDVSZUMD-DCAQKATOSA-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
100.00 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)(CC(C)C)C(=O)N[C@@]([H])(CCC(N)=O)C(=O)N[C@@]([H])(CCC(N)=O)C(O)=O InChI=1S/C16H29N5O6/c1-8(2)7-9(17)14(24)20-10(3-5-12(18)22)15(25)21-11(16(26)27)4-6-13(19)23/h8-11H,3-7,17H2,1-2H3,(H2,18,22)(H2,19,23)(H,20,24)(H,21,25)(H,26,27)/t9-,10-,11-/m0/s1 InChIKey=KAFOIVJDVSZUMD-DCAQKATOSA-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
3