Novel dipeptidyl hydroxamic acids that inhibit human and bacterial dipeptidyl peptidase III

References

• Abramić M, Zubanović M, Vitale L. Dipeptidyl peptidase III from human erythrocytes. Biol Chem Hoppe-Seyler 1988;369:29–38
   PubMed Web of Science ®Google Scholar
• Chen J-M, Barrett AJ. Dipeptidyl-peptidase III. In: Barrett AJ, Rawlings ND, Woessner JF, eds. Handbook of proteolytic enzymes. Vol. 1. Amsterdam, The Netherlands: Elsevier Academic Press; 2004:809–12
   Google Scholar
• Ellis S, Nuenke JM. Dipeptidyl arylamidase III of the pituitary: purification and characterization. J Biol Chem 1967;242:4623–9
   PubMed Web of Science ®Google Scholar
• Lee C-M, Snyder SH. Dipeptidyl-aminopeptidase III of rat brain. Selective affinity for enkephalin and angiotensin. J Biol Chem 1982;257:12043–50
   PubMed Web of Science ®Google Scholar
• Baršun M, Jajčanin N, Vukelić B, et al. Human dipeptidyl peptidase III acts as a post-proline-cleaving enzyme on endomorphins. Biol Chem 2007;388:343–8
   PubMed Web of Science ®Google Scholar
• Liu Y, Kern JT, Walker JR, et al. A genomic screen for activators of the antioxidant response element. Proc Natl Acad Sci USA 2007;104:5205–10
   PubMed Web of Science ®Google Scholar
• Hast BE, Goldfarb D, Mulvaney KM, et al. Proteomic analysis of ubiquitin ligase KEAP1 reveals associated proteins that inhibit NRF2 ubiquitination. Cancer Res 2013;73:2199–210
   PubMed Web of Science ®Google Scholar
• Zhang H, Yamamoto Y, Shumiya S, et al. Peptidases play an important role in cataractogenesis: an immunohistochemical study on lenses derived from Shumiya cataract rats. Histochem J 2001;33:511–21
   PubMedGoogle Scholar
• Šimaga Š, Babić D, Osmak M, et al. Dipeptidyl peptidase III in malignant and non-malignant gynaecological tissue. Eur J Cancer 1998;34:399–405
   PubMed Web of Science ®Google Scholar
• Šimaga Š, Babić D, Osmak M, et al. Tumor cytosol dipeptidyl peptidase III activity is increased with histological aggressiveness of ovarian primary carcinomas. Gynecol Oncol 2003;91:194–200
   PubMed Web of Science ®Google Scholar
• Meliopoulos VA, Andersen LE, Brooks P, et al. MicroRNA regulation of human protease genes essential for influenza virus replication. PLoS One 2012;7:e37169
   Google Scholar
• He M, Mangiameli DP, Kachala S, et al. Expression signature developed from a complex series of mouse models accurately predicts human breast cancer survival. Clin Cancer Res 2010;16:249–59
   PubMed Web of Science ®Google Scholar
• Fukasawa K, Fukasawa KM, Kanai M, et al. Dipeptidyl peptidase III is a zinc metallo-exopeptidase: molecular cloning and expression. Biochem J 1998;329:275–82
   PubMed Web of Science ®Google Scholar
• Abramić M, Špoljarić J, Šimaga Š. Prokaryotic homologs help to define consensus sequences in peptidase family M49. Period Biol 2004;106:161–8
   Web of Science ®Google Scholar
• Rawlings ND, Waller M, Barrett AJ, Bateman A. MEROPS: the database of proteolytic enzymes, their substrates and inhibitors. Nucleic Acids Res 2014;42:D503–9
   PubMed Web of Science ®Google Scholar
• Vukelić B, Salopek-Sondi B, Špoljarić J, et al. Reactive cysteine in the active-site motif of Bacteroides thetaiotaomicron dipeptidyl peptidase III is a regulatory residue for enzyme activity. Biol Chem 2012;393:37–46
   PubMed Web of Science ®Google Scholar
• Baral PK, Jajčanin-Jozić N, Deller S, et al. The first structure of dipeptidyl-peptidase III provides insight into the catalytic mechanism and mode of substrate binding. J Biol Chem 2008;283:22316–24
   PubMed Web of Science ®Google Scholar
• Bezerra GA, Dobrovetsky E, Viertlmayr R, et al. Entropy-driven binding of opioid peptides induces a large domain motion in human dipeptidyl peptidase III. Proc Natl Acad Sci USA 2012;109:6525–30
   PubMed Web of Science ®Google Scholar
• Salopek-Sondi B, Vukelić B, Špoljarić J, et al. Functional tyrosine residue in the active center of human dipeptidyl peptidase III. Biol Chem 2008;389:163–7
   PubMed Web of Science ®Google Scholar
• Špoljarić J, Salopek-Sondi B, Makarević J, et al. Absolutely conserved tryptophan in M49 family of peptidases contributes to catalysis and binding of competitive inhibitors. Bioorg Chem 2009;37:70–6
   PubMed Web of Science ®Google Scholar
• Tomić A, Abramić M, Špoljarić J, et al. Human dipeptidyl peptidase III: insights into ligand binding from a combined experimental and computational approach. J Mol Recognit 2011;24:804–14
   PubMed Web of Science ®Google Scholar
• Abramić M, Karačić Z, Šemanjski M, et al. Aspartate 496 from the subsite S2 drives specificity of human dipeptidyl peptidase III. Biol Chem 2015;396:359–66
   PubMed Web of Science ®Google Scholar
• Jajčanin-Jozić N, Deller S, Pavkov T, et al. Identification of the reactive cysteine residues in yeast dipeptidyl peptidase III. Biochimie 2010;92:89–96
   PubMed Web of Science ®Google Scholar
• Agić D, Hranjec M, Jajčanin N, et al. Novel amidino-substituted benzimidazoles: Synthesis of compounds and inhibition of dipeptidyl peptidase III. Bioorg Chem 2007;35:153–69
   PubMed Web of Science ®Google Scholar
• Xu J, Bjursell MK, Himrod J, et al. A genomic view of the human-Bacteroides thetaiotaomicron symbiosis. Science 2003;299:2074–6
   PubMed Web of Science ®Google Scholar
• Zocco MA, Ainora ME, Gasbarrini G, Gasbarrini A. Bacteroides thetaiotaomicron in the gut: molecular aspects of their interaction. Dig Liver Dis 2007;39:707–12
   PubMedGoogle Scholar
• Odake S, Nakahashi K, Morikawa T, et al. Inhibition of urease activity of dipeptidyl hydroxamic acids. Chem Pharm Bull 1992;40:2764–8
   PubMed Web of Science ®Google Scholar
• Špoljarić J, Tomić A, Vukelić B, et al. Human dipeptidyl peptidase III: the role of Asn406 in ligand binding and hydrolysis. Croat Chem Acta 2011;84:259–68
   Web of Science ®Google Scholar
• Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970;227:680–5
   PubMed Web of Science ®Google Scholar
• Bradford MM. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 1976;72:248–54
   PubMed Web of Science ®Google Scholar
• Codd R. Traversing the coordination chemistry and chemical biology of hydroxamic acids. Coordin Chem Rev 2008;252:1387–408
   Web of Science ®Google Scholar
• Mock WL, Cheng H. Principles of hydroxamate inhibition of metalloproteases: carboxypeptidase A. Biochemistry 2000;39:13945–52
   PubMed Web of Science ®Google Scholar
• Nishino N, Powers JC. Peptide hydroxamic acids as inhibitors of thermolysin. Biochemistry 1978;17:2846–50
   PubMed Web of Science ®Google Scholar
• Izquierdo-Martin M, Stein RL. Mechanistic studies on the inhibition of thermolysin by a peptide hydroxamic acid. J Am Chem Soc 1992;114:325–31
   Web of Science ®Google Scholar
• Holmes MA, Matthews BW. Binding of hydroxamic acid inhibitors to crystalline thermolysin suggests a pentacoordinate zinc intermediate in catalysis. Biochemistry 1981;20:6912–20
   PubMed Web of Science ®Google Scholar
• Akiyama T, Harada S, Kojima F, et al. Fluostatins A and B, new inhibitors of dipeptidyl peptidase III, produced by Streptomyces sp. TA-3391 – I. Taxonomy of producing strain, production, isolation, physico-chemical properties and biological properties. J Antibiot 1998;51:553–9
   PubMed Web of Science ®Google Scholar
• Nishimura K, Hazato T. Isolation and identification of an endogenous inhibitor of enkephalin-degrading enzymes from bovine spinal cord. Biochem Biophys Res Commun 1993;194:713–19
   PubMed Web of Science ®Google Scholar
• Yamamoto Y, Hashimoto J-I, Shimamura M, et al. Characterization of tynorphin, a potent endogenous inhibitor of dipeptidyl peptidaseIII. Peptides 2000;21:503–8
   PubMed Web of Science ®Google Scholar
• Rubio-Aliaga I, Daniel H. Mammalian peptide transporters as targets for drug delivery. Trends Pharmacol Sci 2002;23:434–40
   PubMed Web of Science ®Google Scholar
• Schechter I, Berger A. On the size of the active site in proteases. I. Papain. Biochem Biophys Res Commun 1967;27:157–62
   PubMed Web of Science ®Google Scholar