Hint2, the mitochondrial nucleoside 5’-phosphoramidate hydrolase; properties of the homogeneous protein from sheep (Ovis aries) liver

• Autorzy: Bretes E. , Wojdyla-Mamon A. M. , Kowalska J. , Jamielity J. , Kaczmarek R. , Baraniak J. , Guranowski A.
• Języki publikacji: EN

Abstrakty

EN

Adenosine 5'-phosphoramidate (NH2-pA) is a rare natural nucleotide and its biochemistry and biological functions are poorly recognized. All organisms have proteins that may be involved in the catabolism of NH2-pA. They are members of the HIT protein family and catalyze hydrolytic splitting of NH2-pA to 5'-AMP and ammonia. At least five HIT proteins have been identified in mammals; however, the enzymatic and molecular properties of only Fhit and Hint1 have been comprehensively studied. Our study focuses on the Hint2 protein purified by a simple procedure to homogeneity from sheep liver mitochondrial fraction (OaHint2). Hint1 protein was also prepared from sheep liver (OaHint1) and the molecular and kinetic properties of the two proteins compared. Both function as homodimers and behave as nucleoside 5'-phosphoramidate hydrolases. The molecular mass of the OaHint2 monomer is 16 kDa and that of the OaHint1 monomer 14.9 kDa. Among potential substrates studied, NH2-pA appeared to be the best; the Km and kcat values estimated for this compound are 6.6 µM and 68.3 s-1, and 1.5 µM and 11.0 s-1 per natively functioning dimer of OaHint2 and OaHint1, respectively. Studies of the rates of hydrolysis of different NH2-pA derivatives show that Hint2 is more specific towards compounds with a P-N bond than Hint1. The thermostability of these two proteins is also compared.

Słowa kluczowe

EN

Hint2 gene; Hint1 gene; histidine triad nucleotide binding protein; mitochondrion; nucleoside 5’-phosphoramidate hydrolase; protein; liver; sheep; Ovis aries; hydrolase

• Wydawca: -
• Czasopismo: Acta Biochimica Polonica
• Rocznik: 2013
• Tom: 60
• Numer: 2
• Opis fizyczny: p.249-254,fig.,ref.

Twórcy

autor

Bretes E.

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

autor

Wojdyla-Mamon A. M.

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

autor

Kowalska J.

• Division of Biophysics, Institute of Experimental Physics, Faculty of Physics, University of Warsaw, Warsaw, Poland

autor

Jamielity J.

• Division of Biophysics, Institute of Experimental Physics, Faculty of Physics, University of Warsaw, Warsaw, Poland
• Centre of New Technologies, University of Warsaw, Warsaw, Poland

autor

Kaczmarek R.

• Department of Bioorganic Chemistry, Center of Molecular and Macromolecular Studies, Polish Academy of Sciences, Lodz, Poland

autor

Baraniak J.

• Department of Bioorganic Chemistry, Center of Molecular and Macromolecular Studies, Polish Academy of Sciences, Lodz, Poland

autor

Guranowski A.

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

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