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2011 | 33 | 2 |

Tytuł artykułu

Identification of a second pyridoxine (pyridoxamine) 5'-phosphate oxidase in Arabidopsis thaliana

Warianty tytułu

Języki publikacji

EN

Abstrakty

EN
Pyridoxine (pyridoxamine) 5'-phosphate oxidase (PPOX) is involved in the biosynthetic pathway of vitamin B₆, converting pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP). PLP is a well-known cofactor of numerous enzymes including transamination and decarboxylation reactions. We have previously identified a PPOX (AtPPOX-1) protein encoded by At5g49970 in Arabidopsis thaliana. Here, we report a second PPOX in Arabidopsis, which was named as AtPPOX-2 encoded by At2g46580. The RT-PCR amplified cDNA of AtPPOX-2 was cloned into an Escherichia coli expression vector and a yeast shuttle vector. Both PPOX enzyme assay and complementation of the oxidative stress sensitivity phenotype of a yeast PDX3 deletion mutant demonstrated that At2g46580 encodes a PPOX protein (AtPPOX-2). The catalytic efficiency of AtPPOX-1 is approximately 300-fold higher than that of AtPPOX-2 for PNP. Based on bioinformatic analysis, AtPPOX-2 has a putative mitochondrial transit peptide at the N-terminus. The truncated AtPPOX-2 without 18 amino acids at the N-terminal end lost PPOX activity, suggesting that the N-terminal 18 amino acids are necessary for the enzyme activity of AtPPOX-2. Phylogenetic analysis of AtPPOX-2 homologs from all domains of life suggests that AtPPOX-2 homologs in plants are the product of lateral gene transfer from the cyanobacterial endosymbionts from which plastids are derived.

Słowa kluczowe

Wydawca

-

Rocznik

Tom

33

Numer

2

Opis fizyczny

p.559-566,fig.,ref.

Twórcy

autor
  • Department of Biological Sciences, Auburn University, 101 Rouse Life Sciences Building, Auburn, AL 36849, USA
  • Department of Biological Sciences, Auburn University, 101 Rouse Life Sciences Building, Auburn, AL 36849, USA
autor
  • Department of Nutrition and Food Sciences, Auburn University, Auburn, AL 36849, USA
autor
  • Department of Biological Sciences, Auburn University, 101 Rouse Life Sciences Building, Auburn, AL 36849, USA
autor
  • Department of Biological Sciences, Auburn University, 101 Rouse Life Sciences Building, Auburn, AL 36849, USA

Bibliografia

  • Altschul SF, Madden TL, Schaffer AA, Zhang J, Zhang Z, Miller W, Lipman DJ (1997) Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. Nucleic Acids Res 25:3389–3402
  • Bilski P, Li MY, Ehrenshaft M, Daub ME, Chignell CF (2000) Vitamin B₆ (pyridoxine) and its derivatives are efficient singlet oxygen quenchers and potential fungal antioxidants. Photochem Photobiol 71:129–134
  • Burns KE, Xiang Y, Kinsland CL, McLafferty FW, Begley TP (2005) Reconstitution and biochemical characterization of a new pyridoxal 50-phosphate biosynthetic pathway. J Am Chem Soc 127:3682–3683
  • Choi JD, Bowers-komro DM, Davis MD, Edmondson DE, McCormick DB (1983) Kinetic properties of pyridoxamine (pyridoxine)-5'-phosphate oxidase from rabbit liver. J Biol Chem 258:840–845
  • Choi Y, Chruchich JE, Zaiden E, Kwok F (1987) Brain pyridoxine-5-phosphate oxidase: modulation of its catalytic activity by reaction with pyridoxal-5-phosphate and analogs. J Biol Chem 262:12013–12017
  • Felsenstein J (1985) Confidence limits on phylogenies: an approach using bootstrap. Evolution 39:783–791
  • Fitzpatrick TB, Amrhein N, Kappes B, Macheroux P, Tews I, Raschle T (2007) Two independent routes of de novo vitamin B₆ biosynthesis: not that different after all. Biochem J 407:1–13
  • Franco MG (2003) Pyridoxine 5'-phosphate synthase: de novo synthesis of vitamin B₆ and beyond. Biochim Biophys Acta 1647:92–97
  • Gietz RD, Woods RA (1994) High efficiency transformation with lithium acetate. In: Joohnston JR (ed) Molecular genetics of Yeast, pp 121–134
  • Gonzalez E, Danehower D, Daub ME (2007) Vitamer levels, stress response, enzyme activity, and gene regulation of Arabidopsis lines mutant in the pyridoxine/pyridoxamine 5'-phosphate oxidase (PDX3) and the pyridoxal kinase (SOS4) genes involved in the vitamin B₆ salvage pathway. Plant Physiol 145:985–996
  • John RA (1995) Pyridoxal phosphate-dependent enzymes. Biochim Biophys Acta 1248:81–96
  • Kazarinoff MN, McCormick DB (1975) Rabbit liver pyridoxamine (pyridoxine) 5'-phosphate oxidase. J Biol Chem 250:3436–3442
  • Laber B, Maurer W, Scharf S, Stepusin K, Schmidt FS (1999) Vitamin B₆ biosynthesis: formation of pyridoxine 5'-phosphate from 4-(phophohydroxy)-L-threonine and 1-deoxy-D-xylulose-5-phosphate by PdxA and PdxJ protein. FEBS Lett 449:45–48
  • Raschle T, Amrhein N, Fitzpatrick TB (2005) On the two components of pyridoxal 5'-phosphate synthase form Bacillus subtilis. J Biol Chem 282:6098–6105
  • Salvo MD, Safo MK, Musayev FN, Bossa F, Schirch V (2003) Structure and mechanism of Escherichia coli pyridoxine 5'-phosphate oxidase. Biochim Biophys Acta 1647:76–82
  • Sang Y, Barbosa JM, Wu H, Locy RD, Singh NK (2007) Identification of a pyridoxine (pyridoxamine) 5'-phosphate oxidase from Arabidopsis thaliana. FEBS Lett 581:344–348
  • Studart MT, Titiz O, Raschle T, Forster G, Amrhein N, Fitzpatrick TB (2005) Vitamin B₆ biosynthesis in higher plants. Proc Natl Acad Sci USA 102:13687–13692
  • Swofford DL (2002) PAUP*: Phylogenetic Analysis Using Parsimony (* and other methods. Version 4). Sinauer associates, Sunderland
  • Thompson JD, Higgins DG, Gibson TJ (1994) CLUSTALW: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res 22:4673–4680
  • Tsuge H, Kuroda Y, Amoto AI, Ohashi K (1982) Partial purification and property of pyridoxine (pyridoxamine) 5'-phosphate oxidase isozymes from wheat seedlings. Arch Bio Biophys 217:479–484
  • Wada H, Snell EE (1961) The enzymatic oxidation of pyridoxine and pyridoxamine phosphates. J Biol Chem 236:2089–2095
  • Yang ES, Schirch V (2000) Tight binding of pyridoxal 5'-phosphate to recombinant Escherichia coli pyridoxine 5'-phosphate oxidase. Arch Biochem Biophys 377:109–114
  • Zhao G, Winkler ME (1995) Kinetic limitation and cellular amount of pyridoxine (pyridoxamine) 5'-phosphate oxidase of Escherichia coli K-12. J Bacteriol 177:883–891

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Bibliografia

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