The influence of alpha-aminophosphonic acids on the activity of aminopeptidase from barley seeds-an approach to determine the enzyme specificity

• Autorzy: Oszywa B. , Pawelczak M. , Kafarski P.
• Języki publikacji: EN

Abstrakty

EN

Inhibitory potencies of 24 α-aminophosphonic acids against barley seeds (Hordeum vulgare L.) metalloaminopeptidase have been determined to evaluate structural requirements of this enzyme. The enzyme was sensitive mostly to the influence of phosphonic acid analogues of phenylalanine and its homologues, thus showing narrow specificity if compared with porcine aminopeptidases M1 and M17 and with Plasmodium aminopeptidase M17.

• Wydawca: -
• Czasopismo: Acta Physiologiae Plantarum
• Rocznik: 2015
• Tom: 37
• Numer: 03
• Opis fizyczny: Article 44 [6 p.], fig.,ref.

Twórcy

autor

Oszywa B.

• Faculty of Chemistry, University of Opole, ul.Oleska 48, 45-052 Opole, Poland

autor

Pawelczak M.

• Faculty of Chemistry, University of Opole, ul.Oleska 48, 45-052 Opole, Poland

autor

Kafarski P.

• Faculty of Chemistry, University of Opole, ul.Oleska 48, 45-052 Opole, Poland
• Department of Bioorganic Chemistry, Faculty of Chemistry, Wroclaw University of Technology, Wybrzeze Wyspianskiego 27, 50-370 Wroclaw, Poland

Bibliografia

• Bae C, Kim SM, Lee DJ, Choi D (2013) Multiple classes of immunerelated proteases associated with the cell death response in pepper plants. PLoS One 8:e63533
• Bartling D, Weiler EW (1992) Leucine aminopeptidase from Arabidopsis thaliana. Eur J Biochem 205:425–431
• Chien HCR, Lin LL, Chao SH, Chen CC, Wang WC, Sham CY, Tsai YC, Hu H, Hsu WH (2002) Purification, characterization, and genetic analysis of a leucine aminopeptidase from Aspergillus sojae. Biochim Biophys Acta 1576:119–126
• Cunningham E, Dra˛g M, Kafarski P, Bell A (2008) Chemical target validation studies of aminopeptidase in malaria parasites using α-aminoalkylphosphonate and phosphonopeptide inhibitors. Antimicrob Agents Chemother 52:3221–3228
• Desimone M, Krüger M, Wessel T, Wehofsky M, Hoffmann R, Wagner E (2000) Purification and characterization of an aminopeptidase from the chloroplast stroma of barley leaves by chromatographic and electrophoretic methods. J Chromatogr B Biomed Sci Appl 737:285–293
• Dive V, Georgiadis D, Matziari M, Makaritis A, Beau F, Cuniasse P, Yiotakis A (2004) Phosphinic peptides as zinc metalloproteinase inhibitors. CMLS 61:2010–2019
• Drąg M, Grembecka J, Pawełczak M, Kafarski P (2005) α-Aminoalkylphosphonates as a tool in experimental optimization of P1 side chain shape of potential inhibitors in S1 pocket of leucine and neutral aminopeptidases. Eur J Med Chem 40:764–771
• Drąg M, Bogyo M, Ellman JA, Salvesen GS (2010) Aminopeptidase fingerprints. An integrated approach for identification of good substrates and optimal inhibitors. J Biol Chem 285:3310–3318
• Dziuganowska Z, Andrasiak I, Ślepokura K, Kafarski P (2014) Amidoalkylation of phosphorus trichloride with acetamide and functionalized cyclic ketones––evidence of dominating role of side-reactions. Phosphorus Sulfur Silicon Relat Elem 189:1–8
• Fowler JH, Návaes-Vásques J, Aromdee DN, Pautot V, Holzer FM, Walling LL (2009) Leucine aminopeptidase regulates defense and wound signaling in tomato downstream of jasmonic acid. Plant Cell 21:1239–1251
• Giannousis PP, Bartlett PA (1987) Phosphorus amino acid analogues as inhibitors of leucine aminopeptidase. J Med Chem 30:1603–1609
• Hooper NM, Lendeckel U (eds) (2004) Aminopeptidases in biology and disease, proteases in biology and disease, vol 2. Kluwer Academic/Plenum, New York
• Inokuma S, Setoguchi K, Ohta T, Matsuzaki Y, Yoshida A (1999) Serum leucine aminopeptidase as an activity indicator in systemic lupus erythematosus: a study of 46 consecutive cases. Rheumatol (Oxf) 38:705–708
• Jankiewicz U, Bielawski W (2003) The properties and functions of bacterial aminopeptidases. Acta Microbiol Pol 52:217–231
• Kasperkiewicz P, Gajda AD, Drąg M (2012) Current and prospective applications of non-proteinogenic amino acids in profiling of proteases substrate specificity. Biol Chem 393:843–851
• Lejczak B, Kafarski P, Zygmunt J (1989) Inhibition of aminopeptidases by aminophosphonates. Biochemistry 28:3549–3555
• Lowther WT, Matthews BW (2002) Metalloaminopeptidases: common functional themes in disparate structural surroundings. Chem Rev 102:4581–4608
• Mathe G (1991) Bestatin, an aminopeptidase inhibitor with a multipharmacological function. Biomed Pharmacother 45:49–54
• Matsui M, Fowler JH, Walling LL (2006) Leucine aminopeptidases: diversity in structure and function. Biol Chem 387:1535–1544
• Mucha A, Lämmerhofer M, Lindner W, Pawełczak M, Kafarski P (2008) Individual stereoisomers of phosphinic dipeptide inhibitor of leucine aminopeptidase. Bioorg Med Chem Lett 18:1550–1554
• Mucha A, Drag M, Dalton JP, Kafarski P (2010) Metallo-aminopeptidase inhibitors. Biochimie 92:1509–1529
• Ogiwara N, Amano T, Satoh M, Shioi Y (2005) Leucine aminopeptidase from etiolated barley seedlings: characterization and partial purification of isoforms. Plant Sci 168:575–581
• Oszywa B, Makowski M, Pawełczak M (2013) Purification and partial characterization of Aminopeptidase from barley (Hordeum vulgare L.) seeds. Plant Physiol Biochem 65:75–80
• Poras H, Ouimet T, Orng S-V, Dangé E, Fournié-Zaluski MC, Roques BP (2011) Pluripotentialities of a quenched fluorescent peptide substrate library: enzymatic detection, characterization, and isoenzymes differentiation. Anal Biochem 419:95–105
• Poras H, Duquesnoy S, Fournié-Zaluski MC, Ratinaud-Giraud C, Roques BP, Ouimet T (2013) A sensitive fluorigenic substrate for selective in vitro and in vivo assay of leukotriene A4 hydrolase activity. Anal Biochem 441:152–161
• Poręba M, Mihelic M, Krai P, Rajkovic J, Kre˛ _zel A, Pawełczak M, Klemba M, Turk D, Turk B, Latajka R, Dra˛g M (2014) Unnatural amino acids increase activity and specificity of synthetic substrates for human and malarial cathepsin C. Amino Acids 46:931–943
• Pretlow TG, Nagabhushan M, Sy M, Guo Y, Pretlow TPJ (1994) Putative preneoplastic foci in the human prostate. Cell Biochem Suppl 19:224–231
• Pulido-Cejudo G, Conway B, Proulx P, Brown R, Izaguirre CA (1997) Bestatin-mediated inhibition of leucine aminopeptidase may hinder HIV infection. Antiviral Res 36:167–177
• Sanderink GJ, Artur Y, Siest G (1988) Human aminopeptidases: a review of the literature. J Clin Chem Clin Biochem 26:795–807
• Sanz Y (2007) Aminopeptidases. In: Polaina J, MacCabe AP (eds) Industrial enzymes, Springer, Heidelberg, pp 243–260
• Sharma KK, Elser NJ, Kester K (1996) Comparison of leucine aminopeptidase and aminopeptidase III activities in lens. Curr Eye Res 15:774–781
• Soroka M (1989) Comments on the synthesis of aminomethylphosphonic acid. Synthesis 7:547–548
• Taylor A (1993) Aminopeptidases: structure and function. FASEB J 7:290–298
• Taylor A, Daims M, Lee J, Surgenor T (1982) Identification and quantification of leucine aminopeptidase in aged normal and cataractous human lenses and ability of bovine lens LAP to cleave bovine crystallins. Curr Eye Res 2:47–56
• Thayer SS, Choe HT, Rausser S, Huffaker RC (1988) Characterization and subcellular localization of aminopeptidases in senescing barley leaves. Plant Physiol 87:894–897
• Umezawa H (1980) Screening of small molecular microbial products modulating immune responses and bestatin. Recent Results Cancer Res 40:115–125
• Węglarz-Tomczak E, Poręba M, Byzia A, Berlicki Ł, Nocek B, Mulligan R, Joachimiak A, Drąg M, Mucha A (2013) An integrated approach to the ligand binding specificity of Neisseria meningitidis M1 alanine aminopeptidase by fluorogenic substrate profiling, inhibitory studies and molecular modeling. Biochimie 95:419–428

Identyfikatory

DOI

10.1007/s11738-015-1789-8