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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)
FEBS Letters (2010)
  • Andrzej Guranowski
  • Anna M. Wojdyła
  • Jaroslaw Zimny
  • Anna Wypijewska
  • Joanna Kowalska
  • Jacek Jemielity
  • Richard E. Davis
  • Pawel Bieganowski
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
  • Histidine triad-family protein,
  • Dual catalytic activity,
  • Adenosine 5′-phosphosulfate hydrolysis,
  • Adenosine 5′-phosphosulfate phosphorolysis
Publication Date
January, 2010
Citation Information
Andrzej Guranowski, Anna M. Wojdyła, Jaroslaw Zimny, Anna Wypijewska, et al.. "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)" FEBS Letters Vol. 584 Iss. 1 (2010)
Available at: http://works.bepress.com/joanna_kowalska/7/