Back to search

Peptide record

TPDB47616

ACE inhibitor ACE inhibitors Antihypertensive Neuropeptide standard
3 amino acids
Basic Information
3D PDB MODEL
Drag to rotate. Click a residue or atom to inspect it; the selected residue is highlighted in amber.
TPDB47616
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
IKP
Physicochemical Analysis
C17H32N4O4
ARNDCEQGHLMFSTWYV
IKP
356.47
10.10
1
0
1
+1
1.13
-0.333
130.00
Mammalian: 20 hour Yeast: 30 min E.coli: >10 hour
0
0.00
0
Residue Composition
number
0
A
0
R
0
N
0
D
0
C
0
E
0
Q
0
G
0
H
1
I
0
L
1
K
0
M
0
F
1
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: 0 G: 0 H: 0 I: 1 L: 0 K: 1 M: 0 F: 0 P: 1 S: 0 T: 0 W: 0 Y: 0 V: 0
Chemical Descriptors
3
C17H32N4O4
356.47
10.10
+1
1.13
-0.333
356.4591
356.2416
Evidence Records 2 records
Evidence 1 Activity

Activity

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

Source & Reference

NA
Yokoyama K., Chiba H., and Yoshikawa M., 1992
Peptide inhibitors for angiotensin I-converting enzyme from thermolysin digest of dried bonito. Biosci. Biotech. Biochem., 56, 1541-1545
1992
Journal

Other

3
BIOPEP-UWM database of bioactive peptides SMILES: [H][C@](N)([C@@H](C)CC)C(=O)N[C@@]([H])(CCCCN)C(=O)N1CCC[C@@]1([H])C(O)=O InChI=1S/C17H32N4O4/c1-3-11(2)14(19)15(22)20-12(7-4-5-9-18)16(23)21-10-6-8-13(21)17(24)25/h11-14H,3-10,18-19H2,1-2H3,(H,20,22)(H,24,25)/t11-,12-,13-,14-/m0/s1 InChIKey=GLYJPWIRLBAIJH-XUXIUFHCSA-N Information concerning Angiotensin-Converting Enzyme (ACE) is available in MEROPS database of proteolytic enzymes (http://merops.sanger.ac.uk/) ID: XM02-001 IC50(EC50) of the peptide ranges from 2.5 to 7. Loponen J., 2004, Angiotensin converting enzyme inhibitory peptides in Finnish cereals: a database survey. Agric. Food Sci., 13, 39-45 Jimsheena V. K., Gowda L. R., 2010, Arachin derived peptides as selective angiotensin I-converting enzyme (ACE) inhibitors: structure-activity relationship. Peptides, 31, 1165-1176
Evidence 2 Activity

Activity

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

Source & Reference

AHTPDB
Yokoyama K., Chiba H., and Yoshikawa M., 1992
Peptide inhibitors for angiotensin I-converting enzyme from thermolysin digest of dried bonito. Biosci. Biotech. Biochem., 56, 1541-1545
1992
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)([C@@H](C)CC)C(=O)N[C@@]([H])(CCCCN)C(=O)N1CCC[C@@]1([H])C(O)=O InChI=1S/C17H32N4O4/c1-3-11(2)14(19)15(22)20-12(7-4-5-9-18)16(23)21-10-6-8-13(21)17(24)25/h11-14H,3-10,18-19H2,1-2H3,(H,20,22)(H,24,25)/t11-,12-,13-,14-/m0/s1 InChIKey=GLYJPWIRLBAIJH-XUXIUFHCSA-N Information concerning Angiotensin-Converting Enzyme (ACE) is available in MEROPS database of proteolytic enzymes (http://merops.sanger.ac.uk/) ID: XM02-001 IC50(EC50) of the peptide ranges from 2.5 to 7. Loponen J., 2004, Angiotensin converting enzyme inhibitory peptides in Finnish cereals: a database survey. Agric. Food Sci., 13, 39-45 Jimsheena V. K., Gowda L. R., 2010, Arachin derived peptides as selective angiotensin I-converting enzyme (ACE) inhibitors: structure-activity relationship. Peptides, 31, 1165-1176
Additional Detail Fields 1 fields
3