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Peptide record

TPDB47695

ACE inhibitor ACE inhibitors Antihypertensive Neuropeptide standard
3 amino acids
Basic Information
3D PDB MODEL
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TPDB47695
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
IRA
Physicochemical Analysis
C15H30N6O4
NDCEQGHLKMFPSTWYV
ARI
358.44
11.05
1
0
2
+1
0.33
0.600
163.33
Mammalian: 20 hour Yeast: 30 min E.coli: >10 hour
0
0.00
0
Residue Composition
number
1
A
1
R
0
N
0
D
0
C
0
E
0
Q
0
G
0
H
1
I
0
L
0
K
0
M
0
F
0
P
0
S
0
T
0
W
0
Y
0
V
Amino Acid Distribution
A: 1 R: 1 N: 0 D: 0 C: 0 E: 0 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: 0
Chemical Descriptors
3
C15H30N6O4
358.44
11.05
+1
0.33
0.600
358.4353
358.2322
Evidence Records 2 records
Evidence 1 Activity

Activity

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

Source & Reference

NA
Miyoshi S., Ishikawa H., Kaneko T., Fukui F., Tanaka H.
Structure and activity of angiotensin-converting enzyme inhibitors in alpha-zein hydrolysate. Agric. Biol. Chem., 55(5), 1313-1318 (1991)
1991
Journal

Other

3
BIOPEP-UWM database of bioactive peptides SMILES: [H][C@@](C)(NC(=O)[C@]([H])(CCCNC(N)=N)NC(=O)[C@@]([H])(N)[C@@]([H])(C)CC)C(O)=O InChI=1S/C15H30N6O4/c1-4-8(2)11(16)13(23)21-10(6-5-7-19-15(17)18)12(22)20-9(3)14(24)25/h8-11H,4-7,16H2,1-3H3,(H,20,22)(H,21,23)(H,24,25)(H4,17,18,19)/t8-,9-,10-,11-/m0/s1 InChIKey=TZCGZYWNIDZZMR-NAKRPEOUSA-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
6.40 µM
Inhibitor of Angiotensin-Converting Enzyme (ACE) (EC 3.4.15.1) (MEROPS ID: XM02-001)
ACE inhibitor
ah

Source & Reference

AHTPDB
Miyoshi S., Ishikawa H., Kaneko T., Fukui F., Tanaka H.
Structure and activity of angiotensin-converting enzyme inhibitors in alpha-zein hydrolysate. Agric. Biol. Chem., 55(5), 1313-1318 (1991)
1991
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@@](C)(NC(=O)[C@]([H])(CCCNC(N)=N)NC(=O)[C@@]([H])(N)[C@@]([H])(C)CC)C(O)=O InChI=1S/C15H30N6O4/c1-4-8(2)11(16)13(23)21-10(6-5-7-19-15(17)18)12(22)20-9(3)14(24)25/h8-11H,4-7,16H2,1-3H3,(H,20,22)(H,21,23)(H,24,25)(H4,17,18,19)/t8-,9-,10-,11-/m0/s1 InChIKey=TZCGZYWNIDZZMR-NAKRPEOUSA-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