PMID: 8597571Feb 8, 1996Paper

Spectroscopic studies of myo-inositol monophosphatase with a novel fluorescent substrate

Biochimica Et Biophysica Acta
T PinedaJ E Churchich

Abstract

myo-Inositol monophosphatase catalyzes dephosphorylation of the synthetic substrate anthraniloyl-2'-AMP. Binding of this fluorescent substrate to Tb(III)-monophosphatase was monitored by luminescence spectroscopy. The anthraniloyl chromophore excited at 330 nm sensitizes the long lived luminescence of enzyme bound Tb(III) at 490, 545, 585 and 620 nm. Assuming a mechanism of radiationless energy transfer, the actual distance of separation between the donor anthraniloyl moiety and the acceptor Tb(III) was calculated to be R = 10 angstroms. The binding studies support the earlier observation of Bone et al. (Proc. Natl. Acad. Sci. USA 89 (1992) 10031-10035) that the substrate and the lanthanide Gd(III) interact with a common binding domain of the protein. The catalytic activity of the monophosphatase is completely dependent upon Mg(II) ions which elicit changes in the secondary structure of the protein as revealed by circular dichroism measurements. Binding of Mg(II) ions tend to stabilize the secondary structure of the phosphatase against guanidinium-HCl denaturation.

References

Nov 15, 1979·Analytical Biochemistry·P A LanzettaO A Candia
Nov 1, 1992·Proceedings of the National Academy of Sciences of the United States of America·R BoneJ R Atack
Nov 1, 1991·Analytical Biochemistry·J E Churchich, F Kwok
Jun 26, 1990·Biochemistry·A J Ganzhorn, M C Chanal
Oct 14, 1988·Biochemical and Biophysical Research Communications·J L MeekE Anton
Aug 1, 1985·Journal of Biochemistry·K TakimotoH Nakagawa
Jun 1, 1984·The Biochemical Journal·M J Berridge
Jun 1, 1994·European Journal of Biochemistry·P J GreasleyM G Gore

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Citations

Sep 1, 1996·European Journal of Biochemistry·F MorenoJ E Churchich

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