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

• Autorzy: Guranowski A. , Wojdyla A.M. , Rydzik A.M. , Stepinski J. , Jemielity J.
• 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.

Słowa kluczowe

EN

guanosine 5'-phosphoramidate; Lupinus luteus; adenosine 5'-phosphoramidate; homogeneity; homogenous enzyme; nucleoside 5'-phosphoramidase; purification; seed; yellow lupin

• Wydawca: -
• Czasopismo: Acta Biochimica Polonica
• Rocznik: 2011
• Tom: 58
• Numer: 1
• Opis fizyczny: p.131-136,fig.,ref.

Twórcy

autor

Guranowski A.

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

autor

Wojdyla A.M.

autor

Rydzik A.M.

autor

Stepinski J.

autor

Jemielity J.

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