Journal
FEBS LETTERS
Volume 584, Issue 1, Pages 93-98Publisher
WILEY
DOI: 10.1016/j.febslet.2009.11.003
Keywords
Histidine triad-family protein; Dual catalytic activity; Adenosine 5 '-phosphosulfate hydrolysis; Adenosine 5 '-phosphosulfate; phosphorolysis
Funding
- Polish Ministry of Sciences and Higher Education [PBZ- MNiSW-07/1/2007]
- NIH [AI049558]
Ask authors/readers for more resources
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. (C) 2009 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available