caa a22 4500 477119549 CHVBK 20180405111632.0 cr unu---uuuuu 170330e19960301xx s 000 0 eng 10.1007/BF00240036 doi (NATIONALLICENCE)springer-10.1007/BF00240036 Is cysteine residue important in FITC-sensitive ATP-binding site of P-type ATPases? A commentary to the state of the art [Elektronische Daten] [Albert Breier, Attila Ziegelhöffer, Konrad Famulsky, Marek Michalak, Ján Slezák] Treatment of P-type ATPases (from mammalian sources) by fluorescein isothiocyanate (ITC) revealed the ITC label on a lysine residue that was than considered as essential for binding of ATP in the ATP-binding site of these enzymes. On the other hand, experiments with site directed mutagenesis excluded the presence of an essential lysine residue that would be localized in the ATP binding sites of ATPases. Other previous studies, including those of ourselves, indicated that the primary site of isothiocyanate interaction may be the sulflhydryl group of a cysteine residue and this may be essential for binding of ATP. In addition considerable knowledge accumulated since yet also about the differences in stability of reaction product of isothiocyanates with SH- or NH2- groups. Based upon evaluation of the data available up to now, in present paper the following tentative roles for lysine and cysteine residues located in the ATP-binding site of P-type ATPases are proposed: The positively charged micro-domain of the lysine residue may probably attract the negatively charged phosphate moiety of the ATP molecule whereas the cysteine residue may probably be responsible for recognition and binding of ATP by creation of a proton bridge with the amino group in position 6 on the adenosine ring of ATP. Kluwer Academic Publishers, 1996 isothiocyanates nationallicence lysine and cysteine in the ATP-binding site nationallicence P-type ATPases nationallicence (Na++K+)-ATPase, Ca2+ ATPase nationallicence Breier Albert Institute of Molecular Physiology and Genetics, Slovak Academy of Sciences, Vlárska 5, 833 34, Bratislava, Slovak Republic aut Ziegelhöffer Attila Institute for Heart Research, Slovak Academy of Sciences, DÚbravská cesta 9, 842 33, Bratislava, Slovak Republic aut Famulsky Konrad Department of Biochemistry, Cardiovascular Disease Research Group, University of Alberta, Edmonton, 424 Heritage Medical Research Center, T6G 2S2, Edmonton, Alberta, Canada aut Michalak Marek Department of Biochemistry, Cardiovascular Disease Research Group, University of Alberta, Edmonton, 424 Heritage Medical Research Center, T6G 2S2, Edmonton, Alberta, Canada aut Slezák Ján Institute for Heart Research, Slovak Academy of Sciences, DÚbravská cesta 9, 842 33, Bratislava, Slovak Republic aut Molecular and Cellular Biochemistry Kluwer Academic Publishers; http://www.wkap.nl 160-161/1(1996-03-01), 89-93 0300-8177 160-161:1<89 1996 160-161 11010 https://doi.org/10.1007/BF00240036 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/BF00240036 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Breier Albert Institute of Molecular Physiology and Genetics, Slovak Academy of Sciences, Vlárska 5, 833 34, Bratislava, Slovak Republic aut NATIONALLICENCE 700 1- Ziegelhöffer Attila Institute for Heart Research, Slovak Academy of Sciences, DÚbravská cesta 9, 842 33, Bratislava, Slovak Republic aut NATIONALLICENCE 700 1- Famulsky Konrad Department of Biochemistry, Cardiovascular Disease Research Group, University of Alberta, Edmonton, 424 Heritage Medical Research Center, T6G 2S2, Edmonton, Alberta, Canada aut NATIONALLICENCE 700 1- Michalak Marek Department of Biochemistry, Cardiovascular Disease Research Group, University of Alberta, Edmonton, 424 Heritage Medical Research Center, T6G 2S2, Edmonton, Alberta, Canada aut NATIONALLICENCE 700 1- Slezák Ján Institute for Heart Research, Slovak Academy of Sciences, DÚbravská cesta 9, 842 33, Bratislava, Slovak Republic aut NATIONALLICENCE 773 0- Molecular and Cellular Biochemistry Kluwer Academic Publishers; http://www.wkap.nl 160-161/1(1996-03-01), 89-93 0300-8177 160-161:1<89 1996 160-161 11010 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer