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Peptide record

TPDB00165

ACE inhibitor dipeptidyl peptidase IV inhibitor (DPP IV inhibitor) ACE inhibitors Antihypertensive Antioxidant iDPPIV standard
2 amino acids
Basic Information
3D PDB MODEL
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TPDB00165
ACE inhibitor dipeptidyl peptidase IV inhibitor (DPP IV inhibitor)
ACE inhibitors Antihypertensive Antioxidant iDPPIV
Cardiometabolic peptides Functional / health-promoting peptides
FermFooDB Peptipedia AHTPDB AHTpin AnOxPePred - 1.0 AODB Multi-AOP iDPPIV
standard
No
A 2-aa standard natural multi-activity (ACE inhibitors, Antihypertensive, Antioxidant, and other sources) peptide sequence curated from FermFooDB, Peptipedia, AHTPDB, and other sources, with an available 3D structural model.
Sequence
AW
Physicochemical Analysis
C14H17N3O3
RNDCEQGHILKMFPSTYV
AW
275.31
6.02
0
0
2
-0
-2.02
0.450
50.00
Mammalian: 4.4 hour Yeast: >20 hour E.coli: >10 hour
5500
1997.77
0
Residue Composition
number
1
A
0
R
0
N
0
D
0
C
0
E
0
Q
0
G
0
H
0
I
0
L
0
K
0
M
0
F
0
P
0
S
0
T
1
W
0
Y
0
V
Amino Acid Distribution
A: 1 R: 0 N: 0 D: 0 C: 0 E: 0 Q: 0 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: 0
Chemical Descriptors
2
C14H17N3O3
275.31
6.02
-0
-2.02
0.450
275.3024
275.1266
Evidence Records 4 records
Evidence 1 Activity

Activity

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

Source & Reference

FermFooDB
Loponen J.
Angiotensin converting enzyme inhibitory peptides in Finnish cereals: a database survey. Agric. Food Sci., 2004, 13, 39-45.
2004
Journal

Other

2
Information concerning Angiotensin-Converting Enzyme (ACE) is available in MEROPS database of proteolytic enzymes (http://merops.sanger.ac.uk/) ID: XM02-001 Another value of peptide EC50 (IC 50) = 6.4 um Ono S., Hosokawa M., Miyashita K., Takahashi K., 2006, Inhibiton properties of dipeptides from salmon muscle hydrolysate on angiotensin I-converting enzyme. Int. J. Food Sci. Technol., 41, 383-387 Found in salmon protein hydrolysate. Ono S., Hosokawa M., Miyashita K., Takahashi K., 2006, Inhibiton properties of dipeptides from salmon muscle hydrolysate on angiotensin I-converting enzyme. Int. J. Food Sci. Technol., 41, 383-387
Evidence 2 Activity

Activity

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

Source & Reference

AHTPDB FermFooDB
Loponen J.
Angiotensin converting enzyme inhibitory peptides in Finnish cereals: a database survey. Agric. Food Sci., 2004, 13, 39-45.
2004
Journal

Other

Source Activity Label Source Definition
Antihypertensive
AHTPDB manually curated experimentally validated antihypertensive peptide annotation.
2
Information concerning Angiotensin-Converting Enzyme (ACE) is available in MEROPS database of proteolytic enzymes (http://merops.sanger.ac.uk/) ID: XM02-001 Another value of peptide EC50 (IC 50) = 6.4 um Ono S., Hosokawa M., Miyashita K., Takahashi K., 2006, Inhibiton properties of dipeptides from salmon muscle hydrolysate on angiotensin I-converting enzyme. Int. J. Food Sci. Technol., 41, 383-387 Found in salmon protein hydrolysate. Ono S., Hosokawa M., Miyashita K., Takahashi K., 2006, Inhibiton properties of dipeptides from salmon muscle hydrolysate on angiotensin I-converting enzyme. Int. J. Food Sci. Technol., 41, 383-387
Evidence 3 Activity

Activity

Antioxidative activity
Antioxidant

Source & Reference

AODB FermFooDB
DFBP
Evidence 4 Activity

Activity

IC50
iDPPIV
0.00 µM
Inhibitor of Dipeptidyl Peptidase IV (EC 3.4.14.5) (MEROPS ID: S09.003)
dipeptidyl peptidase IV inhibitor
dpp

Source & Reference

iDPPIV
Nongonierma A. B., Mooney C., Shields D. C., FitzGerald R. J.
In silico approaches to predict the potential of milk protein-derivedpeptides as dipeptidyl peptidase IV (DPP-IV) inhibitors. Peptides 57, 43-51
2014
Journal

Other

2
Also as ACE inhibitor (BIOPEP ID 7543) and antioxidative peptide (BIOPEP ID 8460)
Additional Detail Fields 1 fields
2