10527-48-7Relevant academic research and scientific papers
Engineering human FHIT, a diadenosine triphosphate hydrolase, into an efficient dinucleoside polyphosphate synthase
Huang, Kaisheng,Frey, Perry A.
, p. 9548 - 9549 (2004)
The putative human tumor suppressor gene FHIT encodes Fhit, the fragile histidine triad protein. Fhit is thought to participate in a signal transduction pathway involving dinucleoside polyphosphates. Fhit catalyzes the Mg2+-dependent hydrolysis of P1-5′-O-adenosine-P3-5′-O-adenosine triphosphate (Ap3A) to AMP and MgADP. Mutation of His96 to glycine disables Fhit as a catalyst for the hydrolysis of phosphoanhydrides such as Ap3A. However, the mutated enzyme H96G-Fhit efficiently catalyzes the synthesis of phosphoanhydride bonds in reactions of nucleoside-5′-phosphimidazolides with nucleoside di- and triphosphates. H96G-Fhit can be employed in the synthesis of a wide range of dinucleoside tri- and tetraphosphates. We here describe the use of H96G-Fhit to catalyze the synthesis of Ap3A, Ap3C, Ap3G, Ap3T, Ap3U, Cp3U, Tp3U, dAp3U, Ap4A, Ap4U, and the fluorescent Ap4etheno-C. Copyright
Characterisation of stress protein LysU. Enzymic synthesis of diadenosine 5′,5?-P1,P4-tetraphosphate (Ap4A) analogues by LysU
Theoclitou, Maria-Elena,Wittung, E. Pernilla L.,Hindley, Alison D.,El-Thaher, Talal S. H.,Miller, Andrew D.
, p. 2009 - 2019 (2007/10/03)
The stress protein LysU (lysyl tRNA synthetase) has been purified from a recombinant strain of Escherichia coli expressing the plasmid pXLys5, and kinetically characterised. Preparative syntheses of analogues of the biologically important molecule diadenosine 5′,5?-P1,P4-tetraphosphate (Ap4A) are then achieved in good yield by enzyme catalysis, using purified LysU.
