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Peptide record

TPDB00275

ACE inhibitor (from bovine beta-CN) ACE inhibitors Antihypertensive Antioxidant standard
6 amino acids
Basic Information
3D PDB MODEL
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TPDB00275
ACE inhibitor (from bovine beta-CN)
ACE inhibitors Antihypertensive Antioxidant
Cardiometabolic peptides Functional / health-promoting peptides
FermFooDB pep-lab Peptipedia AHTPDB AHTpin AODB AoXpDb Multi-AOP
standard
No
A 6-aa standard natural multi-activity (ACE inhibitors, Antihypertensive, and Antioxidant) peptide sequence curated from FermFooDB, pep-lab, Peptipedia, and other sources, with an available 3D structural model.
Sequence
DKIHPF
Physicochemical Analysis
C36H53N9O9
ARNCEQGLMSTWYV
DHIKFP
755.87
7.81
2
1
2
+0
2.19
-0.817
65.00
Mammalian: 1.1 hour Yeast: 3 min E.coli: >10 hour
0
0.00
0
Residue Composition
number
0
A
0
R
0
N
1
D
0
C
0
E
0
Q
0
G
1
H
1
I
0
L
1
K
0
M
1
F
1
P
0
S
0
T
0
W
0
Y
0
V
Amino Acid Distribution
A: 0 R: 0 N: 0 D: 1 C: 0 E: 0 Q: 0 G: 0 H: 1 I: 1 L: 0 K: 1 M: 0 F: 1 P: 1 S: 0 T: 0 W: 0 Y: 0 V: 0
Chemical Descriptors
6
C36H53N9O9
755.87
7.81
+0
2.19
-0.817
755.8588
755.3954
Evidence Records 2 records
Evidence 1 Activity

Activity

IC50
ACE inhibitors
257.00 µM
Inhibitor of Angiotensin-Converting Enzyme (ACE) (EC 3.4.15.1) (MEROPS ID: M02-001)
ACE inhibitor
ah

Source & Reference

FermFooDB
Gobbetti M., Ferranti P., Smacchi E., Goffredi F., Addeo F.
Production of angiotensin-I-converting-enzyme-inhibitory peptides in fermented milks started by Lactobacillus delbrueckii subsp. bulgaricus SS1 and Lactococcus lactis subsp. cremoris FT4. Appl. Env. Microbiol., 66, 3898-3904, 2000
2000
Journal

Other

6
BIOPEP-UWM database of bioactive peptides SMILES: N[C@@H](CC(=O)O)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H]([C@H](CC)C)C(=O)N[C@@H](CC1=C[N]([H])C=N1)C(=O)N2[C@@H](CCC2)C(=O)N[C@@H](CC3=CC=CC=C3)C(=O)O InChI=1S/C36H53N9O9/c1-3-21(2)30(44-32(49)25(12-7-8-14-37)41-31(48)24(38)18-29(46)47)34(51)42-26(17-23-19-39-20-40-23)35(52)45-15-9-13-28(45)33(50)43-27(36(53)54)16-22-10-5-4-6-11-22/h4-6,10-11,19-21,24-28,30H,3,7-9,12-18,37-38H2,1-2H3,(H,39,40)(H,41,48)(H,42,51)(H,43,50)(H,44,49)(H,46,47)(H,53,54)/t21-,24-,25-,26-,27-,28-,30-/m0/s1 InChIKey=KDBXTZUSBPMDFS-YYNHRMGXSA-N Information concerning Angiotensin-Converting Enzyme (ACE) is available in MEROPS database of proteolytic enzymes (http://merops.sanger.ac.uk/) ID: M02-001 Peptide found in yoghurt: Farvin K. H. S., Baron C. P., Nielsen N. S., Jacobsen C., 2010, Antioxidant activity of yoghurt peptides: part 2 – Characterisation of peptide fractions. Food Chem., 123, 1090-1097 IC50 according to: Van der Ven C., 2002, Biochemical and functional characterisation of casein and whey protein hydrolysates. A study on correlations between biochemical and functional properties using multivariate data analysis. Dissertation
Evidence 2 Activity

Activity

IC50
Antihypertensive
257.00 µM
Inhibitor of Angiotensin-Converting Enzyme (ACE) (EC 3.4.15.1) (MEROPS ID: M02-001)
ACE inhibitor
ah

Source & Reference

AHTPDB FermFooDB
Gobbetti M., Ferranti P., Smacchi E., Goffredi F., Addeo F.
Production of angiotensin-I-converting-enzyme-inhibitory peptides in fermented milks started by Lactobacillus delbrueckii subsp. bulgaricus SS1 and Lactococcus lactis subsp. cremoris FT4. Appl. Env. Microbiol., 66, 3898-3904, 2000
2000
Journal

Other

Source Activity Label Source Definition
Antihypertensive
AHTPDB manually curated experimentally validated antihypertensive peptide annotation.
6
BIOPEP-UWM database of bioactive peptides SMILES: N[C@@H](CC(=O)O)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H]([C@H](CC)C)C(=O)N[C@@H](CC1=C[N]([H])C=N1)C(=O)N2[C@@H](CCC2)C(=O)N[C@@H](CC3=CC=CC=C3)C(=O)O InChI=1S/C36H53N9O9/c1-3-21(2)30(44-32(49)25(12-7-8-14-37)41-31(48)24(38)18-29(46)47)34(51)42-26(17-23-19-39-20-40-23)35(52)45-15-9-13-28(45)33(50)43-27(36(53)54)16-22-10-5-4-6-11-22/h4-6,10-11,19-21,24-28,30H,3,7-9,12-18,37-38H2,1-2H3,(H,39,40)(H,41,48)(H,42,51)(H,43,50)(H,44,49)(H,46,47)(H,53,54)/t21-,24-,25-,26-,27-,28-,30-/m0/s1 InChIKey=KDBXTZUSBPMDFS-YYNHRMGXSA-N Information concerning Angiotensin-Converting Enzyme (ACE) is available in MEROPS database of proteolytic enzymes (http://merops.sanger.ac.uk/) ID: M02-001 Peptide found in yoghurt: Farvin K. H. S., Baron C. P., Nielsen N. S., Jacobsen C., 2010, Antioxidant activity of yoghurt peptides: part 2 – Characterisation of peptide fractions. Food Chem., 123, 1090-1097 IC50 according to: Van der Ven C., 2002, Biochemical and functional characterisation of casein and whey protein hydrolysates. A study on correlations between biochemical and functional properties using multivariate data analysis. Dissertation
Additional Detail Fields 1 fields
6