Dual activity of certain HIT-proteins:A. thalianaHint4 andC. elegansDcpS act on adenosine 5′-phosphosulfate as hydrolases (forming AMP) and as phosphorylases (forming ADP)
| Autor: | Jacek Jemielity, Andrzej Guranowski, Jarosław Zimny, Anna Maria Wojdyła, Paweł Bieganowski, Richard E. Davis, Anna Wypijewska, Joanna Kowalska |
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| Rok vydání: | 2009 |
| Předmět: |
Adenosine 5′-phosphosulfate hydrolysis
Hydrolases Stereochemistry Adenosine 5′-phosphosulfate phosphorolysis DCPS Arabidopsis Biophysics Biochemistry Substrate Specificity Hydrolysis Dual catalytic activity Multienzyme Complexes Structural Biology Genetics medicine Animals Phosphorylation Pyrophosphatases Caenorhabditis elegans Caenorhabditis elegans Proteins Molecular Biology Histidine Phosphorolysis chemistry.chemical_classification biology Arabidopsis Proteins Chemistry Histidine triad-family protein Cell Biology Metabolism Hydrogen-Ion Concentration biology.organism_classification Adenosine Adenosine Monophosphate Phosphoric Monoester Hydrolases Adenosine Phosphosulfate Adenosine Diphosphate Enzyme Sulfatases medicine.drug |
| Zdroj: | FEBS Letters. 584:93-98 |
| ISSN: | 0014-5793 |
| DOI: | 10.1016/j.febslet.2009.11.003 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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