BIOPEP-UWM: Report

ID 3167
Name dipeptidyl peptidase IV inhibitor (DPP IV inhibitor); diprotin A
sequence
IPI
Function:
Inhibitor of Dipeptidyl Peptidase IV (EC 3.4.14.5) (MEROPS ID: S09.003)
 
Number of residues
3
Activity code
dpp
Activity :
dipeptidyl peptidase IV inhibitor
Chemical mass 341.4445 Monoisotopic mass 341.2307
IC50 :
7.40 µM


Bibliographic data:
Authors
Maruyama S., Ohmori T., Nakagami T.
Title
Prolylendopeptidase inhibitory activity of a glial fibrillary acidic protein fragment and other proline-rich peptides. Biosci. Biotech. Biochem., 60, 358-359 (1996)
Year Source
1996 Journal


Additional information:
BIOPEP-UWM database of bioactive peptides


SMILES: N[C@H](C(=O)N1[C@H](C(=O)N[C@H](C(=O)O)[C@H](CC)C)CCC1)[C@H](CC)C

InChI=1S/C17H31N3O4/c1-5-10(3)13(18)16(22)20-9-7-8-12(20)15(21)19-14(17(23)24)11(4)6-2/h10-14H,5-9,18H2,1-4H3,(H,19,21)(H,23,24)/t10-,11-,12-,13-,14-/m0/s1

InChIKey=JNTMAZFVYNDPLB-PEDHHIEDSA-N


Information concerning Dipeptidyl Peptidase IV (synonym: Dipeptidyl Aminopeptidase IV) (EC 3.4.14.5) is available in MEROPS database of proteolytic enzymes (http://merops.sanger.ac.uk/); ID: S09.003

Another measured value of IC50 (EC50) of peptide is 3.50 um (Leiting B., Pryor K. D., Wu J. K., Marsilio F., Patel R. A., Craik C. S., Ellman J. A., Cummings R. T., Thornberry N. A., 2003, Catalytic properties and inhibition of proline-specific dipeptidyl peptidases II, IV and VII. Biochem. J., 371, 525-532) and 4.23 um (Nongonierma A. B., Mooney C., Shields D. C., FitzGerald R. J., 2013, Inhibition of dipeptidyl peptidase IV and xanthine oxidase by amino acids and dipeptides. Food Chemistry, 141, 644-653).

Another references concerning peptide:
Lacroix I. M. E., Li-Chan E. C. Y., 2012, Evaluation of the potential of dietary proteins as precursors of dipeptidyl peptidase (DPP)-IV inhibitors by an in silico approach. J. Funct. Foods, 4, 403-422
Nongonierma A. B., FitzGerald R. J., 2013, Inhibition of dipeptidyl peptidase IV (DPP-IV) by proline containing casein-derived peptides. J. Funct. Foods, 5, 1909-1917
Davy A., Thomsen K. K., Juliano M. A., Alves L. C., Svendsen I., Simpson D. J., Purification and characterization of barley dipeptidyl peptidase IV. Plant Physiology, 122, 425-431 (2000).


Inhibitor of tripeptidyl aminopeptidase (MEROPS ID: S08.A56) according to the ChEMBL database
Inhibitor of Tripeptidyl peptidase 2 (EC 3.4.14.10) (MEROPS ID: S08.090) according to the BRENDA database
Inhibitor of Angiotensin-converting enzyme (EC 3.4.15.1) (MEROPS ID: M02-001) according to the AHTPDB database


Database reference:
ACToR: ID 90614-48-5

AHTPDB: ID 2290

BindingDB: ID 50229666

BRENDA: Ligand Ile-Pro-Ile; Ile-Pro-Ile-OH

CAS: Registry No 90614-48-5

ChEBI: ID 93213

ChemBank: ID KBio3_003020, SPBio_001439, Spectrum2_001480, Spectrum3_001838

ChEMBL: ID CHEMBL214381

ChemIDplus: ID 090614485

ChemSpider: ID 85449

DFBP: ID DFBPDPIV0159

EPA CompTox: ID DTXSID80920277

EROP-Moscow: ID E09227

FeptideDB: ID 3167

J-GLOBAL: ID 200907012372258533

MeSH: terms diprotin A; Ile-Pro-Ile; isoleucyl-prolyl-isoleucine

Metabolomics Workbench: ID 82945

MMDB: ID 33482.3

Natural Product Atlas: ID NPA020918

Nikkaji: ID J122.663K

NMRShiftDB: ID 70109396

ProbesDrugs: ID PD079971

PubChem: CID 94701

SATPdb: ID satpdb25992

SureChEMBL: ID SCHEMBL6404766

Wikidata: Q27164930

ZINC: ID ZINC04899477