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    Wyświetlanie 1-4 z 4
    Tytuł:
    Analogs of diadenosine tetraphosphate (Ap4A).
    Autorzy:
    Guranowski, Andrzej
    Powiązania:
    https://bibliotekanauki.pl/articles/1043366.pdf
    Data publikacji:
    2003
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    dinucleoside polyphosphates
    Ap4A
    biological effects of Ap4A analogs
    Ap4A analogs
    diadenosine tetraphosphate
    Opis:
    This review summarizes our knowledge of analogs and derivatives of diadenosine 5',5'''-P1,P4-tetraphosphate (Ap4A), the most extensively studied member of the dinucleoside 5',5'''-P1,Pn-polyphosphate (NpnN) family. After a short discussion of enzymes that may be responsible for the accumulation and degradation of Np4N's in the cell, this review focuses on chemically and/or enzymatically produced analogs and their practical applications. Particular attention is paid to compounds that have aided the study of enzymes involved in the metabolism of Ap4A (Np4N'). Certain Ap4A analogs were alternative substrates of Ap4A-degrading enzymes and/or acted as enzyme inhibitors, some other helped to establish enzyme mechanisms, increased the sensitivity of certain enzyme assays or produced stable enzyme:ligand complexes for structural analysis.
    Źródło:
    Acta Biochimica Polonica; 2003, 50, 4; 947-972
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Selective splitting of 3-adenylated dinucleoside polyphosphates by specific enzymes degrading dinucleoside polyphosphates.
    Autorzy:
    Guranowski, Andrzej
    Sillero, Antonio
    Günther Sillero, María
    Powiązania:
    https://bibliotekanauki.pl/articles/1043653.pdf
    Data publikacji:
    2003
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    diadenosine triphosphate
    diadenosine tetraphosphatase
    diadenosine triphosphatase
    3'-adenylated dinucleoside polyphosphates
    diadenosine tetraphosphate
    diguanosine tetraphosphate
    Opis:
    Several 3'-[32P]adenylated dinucleoside polyphosphates (NpnN'p*As) were synthesized by the use of poly(A) polymerase (Sillero MAG et al., 2001, Eur J Biochem.; 268 : 3605-11) and three of them, ApppA[32P]A or ApppAp*A, AppppAp*A and GppppGp*A, were tested as potential substrates of different dinucleoside polyphosphate degrading enzymes. Human (asymmetrical) dinucleoside tetraphosphatase (EC 3.6.1.17) acted almost randomly on both AppppAp*A, yielding approximately equal amounts of pppA + pAp*A and pA + pppAp*A, and GppppGp*, yielding pppG + pGp*A and pG + pppGp*A. Narrow-leafed lupin (Lupinus angustifolius) tetraphosphatase acted preferentially on the dinucleotide unmodified end of both AppppAp*A (yielding 90% of pppA + pAp*A and 10 % of pA + pppAp*A) and GppppGp*A (yielding 89% pppG + pGp*A and 11% of pG + pppGp*A). (Symmetrical) dinucleoside tetraphosphatase (EC 3.6.1.41) from Escherichia coli hydrolyzed AppppAp*A and GppppGp*A producing equal amounts of ppA + ppAp*A and ppG + ppGp*A, respectively, and, to a lesser extent, ApppAp*A producing pA + ppAp*A. Two dinucleoside triphosphatases (EC 3.6.1.29) (the human Fhit protein and the enzyme from yellow lupin (Lupinus luteus)) and dinucleoside tetraphosphate phosphorylase (EC 2.7.7.53) from Saccharomyces cerevisiae did not degrade the three 3'-adenylated dinucleoside polyphosphates tested.
    Źródło:
    Acta Biochimica Polonica; 2003, 50, 1; 123-130
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Plant nucleoside 5-phosphoramidate hydrolase; simple purification from yellow lupin (Lupinus luteus) seeds and properties of homogeneous enzyme
    Autorzy:
    Guranowski, Andrzej
    Wojdyła, Anna
    Rydzik, Anna
    Stepiński, Janusz
    Jemielity, Jacek
    Powiązania:
    https://bibliotekanauki.pl/articles/1039966.pdf
    Data publikacji:
    2011
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    yellow lupin
    Lupinus luteus
    adenosine 5'-phosphoramidate
    purification to homogeneity
    nucleoside 5'-phosphoramidase
    Opis:
    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.
    Źródło:
    Acta Biochimica Polonica; 2011, 58, 1; 131-136
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Hint2, the mitochondrial nucleoside 5-phosphoramidate hydrolase; properties of the homogeneous protein from sheep (Ovis aries) liver
    Autorzy:
    Bretes, Ewa
    Wojdyła-Mamoń, Anna
    Kowalska, Joanna
    Jemielity, Jacek
    Kaczmarek, Renata
    Baraniak, Janina
    Guranowski, Andrzej
    Powiązania:
    https://bibliotekanauki.pl/articles/1039587.pdf
    Data publikacji:
    2013
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    Hint1
    Hint2
    histidine triad nucleotide binding proteins
    purification to homogeneity
    nucleoside 5'-phosphoramidase
    Opis:
    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.
    Źródło:
    Acta Biochimica Polonica; 2013, 60, 2; 249-254
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
      Wyświetlanie 1-4 z 4

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