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2011 | 58 | 1 |

Tytuł artykułu

Plant nucleoside 5'-phosphoramidate hydrolase; simple purification from yellow lupin (Lupinus luteus) seeds and properties of homogeneous enzyme

Warianty tytułu

Języki publikacji

EN

Abstrakty

EN
Adenosine 5'-phosphoramidate (NH2-pA) is an uncommon natural nucleotide of poorly understood biochemistry and function. We studied a plant enzyme potentially involved in the catabolism of NH2-pA. A fast and simple method comprising extraction of yellow lupin (Lupinus luteus) seed-meal with a low ionic strength buffer, ammonium sulfate and acetone fractionations, removal of contaminating proteins by heat denaturation, and affinity chromatography on AMP-agarose, yielded homogenous nucleoside 5'-phosphoramidase. Mass spectrometric analysis showed that the lupin hydrolase exhibits closest similarity to Arabidopsis thaliana Hint1 protein. The substrate specificity of the lupin enzyme, in particular its ability to split the P-S bond in adenosine 5'-phosphorothioate, is typical of known Hint1 proteins. Adenosine 5'-phosphofluoride and various derivatives of guanosine 5'-phosphoramidate were also substrates. Neither common divalent metal cations nor 10 mM EDTA or EGTA affected the hydrolysis of NH2-pA. The enzyme functions as a homodimer (2 × 15 800 Da). At the optimum pH of 7.0, the Km for NH2-pA was 0.5 µM and kcat 0.8 s-1 (per monomer active site). The properties of the lupin nucleoside 5'-phosphoramidase are compared with those of its counterparts from other organisms.

Wydawca

-

Rocznik

Tom

58

Numer

1

Opis fizyczny

p.131-136,fig.,ref.

Twórcy

  • Department of Biochemistry and Biotechnology, Poznań University of Life Sciences, Poznan, Poland
autor
autor
autor
autor

Bibliografia

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  • Frankhauser H, Berkowitz GA, Schiff JA (1981a) A nucleotide with the properties of adenosine 5'-phosphoramidate from Chlorella cells. Biochem Biophys Res Commun 101: 524-532. 
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  • Guranowski A, Starzynska E, Bojarska E, Stepinski J, Darzynkiewicz E (1996) Dinucleoside 5',5'''-P1,P3-triphosphate hydrolase from yellow lupin (Lupinus luteus) seeds: purification to homogeneity and hydrolysis of mRNA 5'-cap analogs. Protein Expr Purif 8: 416-422. 
  • Guranowski A, Wojdyła AM, Pietrowska-Borek M, Bieganowski P, Khurs EN, Cliff MJ, Blackburn GM, Błaziak D, Stec, W J (2008) Fhit proteins can also recognize substrates other than dinucleoside polyphosphates. FEBS Lett 582: 3152-3158. 
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  • Guranowski A, Wojdyła AM, Zimny J, Wypijewska A, Kowalska J, Jemielity J, Davis RE, Bieganowski P (2010a) Dual activity of certain HIT-proteins: A. thaliana Hint4 and C. elegans DcpS act on adenosine 5'-phosphosulfate as hydrolases (forming AMP) and as phosphorylases (forming ADP). FEBS Lett 584: 93-98. 
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Bibliografia

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