Peptide properties

1Top 2Function-activity relationship 3Calculated physicochemical properties 4Peptide source & Food-borne protein(s) search 5Biological/Functional activity & target protein 6Taste properties & Structure 7Preparation method 8Stability & Cytotoxicity 9Additional information 10Database cross-references 11Reference(s)

List of peptide properties

DFBP ID - DFBPACEI0586(ACE-inhibitory peptide)

DFBP ID	DFBPACEI0586
Peptide sequence	IYPR
Type	Native peptide
Peptide/Function name	ACE-inhibitory peptide

Function-activity relationship

Main bioactivity	ACE-inhibitory activity
Otheir bioactivity	N.D

Calculated physicochemical properties

Three-letter amino acid

Ile-Tyr-Pro-Arg

Single-letter amino acid

IYPR

Peptide length

Peptide mass

Experimental mass	Theoretical mass
N.D	547.64 Da ^c

Net charge

0.00 ^c

Isoelectric point (pI)

9.82 ^c

IC₅₀

10 μM

pIC₅₀

-1.0

GRAVY

-0.7250^c

Hydrophilic residue ratio

50%^c

Peptide calculator

Peptide source & Food-borne protein(s) search

Classification	Plant
Organism/Source	Grains
Precursor protein	Sake lees
Residue position	N.D
Precursor protein(s) search	Source.1: DFBPPR2608 ---- Plant proteins ---- Prolamin PPROL 14E Source.2: DFBPPR3194 ---- Plant proteins ---- G patch domain-containing protein TGH homolog Source.3: DFBPPR4276 ---- Plant proteins ---- CRS2-associated factor 2, mitochondrial Source.4: DFBPPR4751 ---- Plant proteins ---- Zinc finger CCCH domain-containing protein 30 Source.5: DFBPPR4928 ---- Plant proteins ---- Copper-transporting ATPase HMA4 Source.6: DFBPPR5325 ---- Plant proteins ---- Nodulin-C51 Source.7: DFBPPR5356 ---- Plant proteins ---- Nodulin-23 Source.8: DFBPPR6214 ---- Plant proteins ---- Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta, chloroplastic Source.9: DFBPPR16330 ---- Animal proteins ---- Pachytene checkpoint protein 2 homolog Source.10: DFBPPR16671 ---- Animal proteins ---- Forkhead box protein I3 Source.11: DFBPPR17018 ---- Animal proteins ---- Bifunctional arginine demethylase and lysyl-hydroxylase JMJD6 Source.12: DFBPPR17903 ---- Animal proteins ---- Transcription initiation factor IIB Source.13: DFBPPR8746 ---- Animal proteins ---- Electron transfer flavoprotein-ubiquinone oxidoreductase, mitochondrial Source.14: DFBPPR9549 ---- Animal proteins ---- Pachytene checkpoint protein 2 homolog Source.15: DFBPPR10076 ---- Animal proteins ---- Bifunctional arginine demethylase and lysyl-hydroxylase JMJD6 Source.16: DFBPPR11004 ---- Animal proteins ---- Pachytene checkpoint protein 2 homolog Source.17: DFBPPR11304 ---- Animal proteins ---- Vitamin D3 hydroxylase-associated protein Source.18: DFBPPR11343 ---- Animal proteins ---- Transcription factor Sp8 Source.19: DFBPPR11478 ---- Animal proteins ---- Gastrin-releasing peptide Source.20: DFBPPR15190 ---- Microorganism protein ---- Pescadillo homolog Source.21: DFBPPR15820 ---- Microorganism protein ---- 6-phospho-beta-galactosidase Source.22: DFBPPR15839 ---- Microorganism protein ---- Citrate synthase
Link-research Inductive analysis	There are no literature reports on the discovery of this sequence in other food-source proteins.

Biological/Functional activity & target protein

ACE-inhibitory activity	The peptide exhibited strong Angiotensin-Converting Enzyme (ACE) (EC 3.4.15.1) inhibitory activity with an IC₅₀ value of 10 μM.
Specific target protein(s)	Specific Target Protein(s): Angiotensin-converting enzyme

Taste properties & Structure

Bitterness

Literature report	N.D
Bitter prediction tools	Bitter taste ^prediction

SMILES

N[C@@]([H])([C@]([H])(CC)C)C(=O)N[C@@]([H])(Cc1ccc(O)cc1)C(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])(CCCNC(=N)N)C(=O)O

Preparation method

Mode of preparation	Synthesis
Enzyme(s)/starter culture	Solid-phase peptide synthesis was done with a peptide synthesizer (PEPTICOUPLER 2200; Vega Co., Ltd.).

Stability & Cytotoxicity

Peptide stability

Literature report:	N.D
EHP-Tool:	Enzymatic Hydrolysis Prediction Tool (EHP-Tool)

Peptide cytotoxicity

Literature report:	N.D
Prediction:	ToxinPred

Additional information

N.D

Database cross-references

[D1]

[D2]

[D3]

[D4]

Reference(s)

Primary literature	Saito Y, Wanezaki K, Kawato A, Imayasu S. Structure and activity of angiotensin I converting enzyme inhibitory peptides from sake and sake lees. Biosci Biotechnol Biochem. 1994 Oct;58(10):1767-71. PMID: 7765503 DOI: 10.1271/bbb.58.1767
Other literature(s)	N.D
PubDate	1994