On the effect on specificity of Thr246----Gly mutation in L-lactate dehydrogenase of Bacillus sterothermophilus

Biochemical and Biophysical Research Communications
D BurH M Wilks

Abstract

The function of the amino acid Thr246 in L-lactate dehydrogenase from Bacillus stearothermophilus has been investigated by site-directed replacement with glycine. Kinetic experiments with a number of 2-oxo acids showed strongly reduced activity for the mutated enzyme. However, the mutant enzyme shows a relative preference for the large hydrophobic sidechains of alpha-keto acids and an even higher specific activity than the wild-type lactate dehydrogenase for the polar oxaloacetate substrate. Graphic analyses indicate that the loss of one hydrogen bond, or intrusion of water into the active site, might be responsible for the reduced activity. The kinetic results suggest that the binding modes of bulky hydrophobic or polar substrates compensate to some degree for the partially disrupted active site.

References

Dec 5, 1987·Journal of Molecular Biology·C Abad-ZapateroM G Rossmann
Jul 15, 1987·Biochemical and Biophysical Research Communications·K W HartJ J Holbrook

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Citations

May 29, 1991·Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences·C R DunnJ J Holbrook
Sep 27, 2014·The Journal of Biological Chemistry·Yoko IkeharaHayao Taguchi
Mar 4, 1994·Journal of Molecular Biology·J D GoldbergP Brick
Feb 14, 1992·Biochemical and Biophysical Research Communications·R SakowiczJ B Jones

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