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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) |
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| Authors: | Andrzej Guranowski Anna Maria Wojdy?a Anna Wypijewska Jacek Jemielity Pawe? Bieganowski |
| Affiliation: | a Department of Biochemistry and Biotechnology, The University of Life Sciences, 35 Wo?yńska Street, 60-637 Poznań, Poland b Division of Biophysics, Institute of Experimental Physics, Faculty of Physics, Warsaw University, 02-089 Warsaw, Poland c Department of Biochemistry and Molecular Genetics, School of Medicine University of Colorado Denver, Aurora, CO 80010, USA d Department of Pediatrics, School of Medicine University of Colorado Denver, Aurora, CO 80010, USA e Department of Pharmacology, Mossakowski Medical Research Centre, 5 Pawińskiego Street, 02-106 Warsaw, Poland |
| Abstract: | Histidine triad (HIT)-family proteins interact with different mono- and dinucleotides and catalyze their hydrolysis. During a study of the substrate specificity of seven HIT-family proteins, we have shown that each can act as a sulfohydrolase, catalyzing the liberation of AMP from adenosine 5′-phosphosulfate (APS or SO4-pA). However, in the presence of orthophosphate, Arabidopsis thaliana Hint4 and Caenorhabditis elegans DcpS also behaved as APS phosphorylases, forming ADP. Low pH promoted the phosphorolytic and high pH the hydrolytic activities. These proteins, and in particular Hint4, also catalyzed hydrolysis or phosphorolysis of some other adenylyl-derivatives but at lower rates than those for APS cleavage. A mechanism for these activities is proposed and the possible role of some HIT-proteins in APS metabolism is discussed. |
| Keywords: | APS or SO4-pA, adenosine 5&prime -phosphosulfate IPS or SO4-pI, inosine 5&prime -phosphosulfate HIT, histidine triad HPLC, high performance liquid chromatography TLC, thin layer chromatography |
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