Article
The core of allosteric motion in Thermus caldophilus L-lactate dehydrogenase.
The Journal of biological chemistry - 7 Nov 2014
Ikehara Yoko, Arai Kazuhito, Furukawa Nayuta, Ohno Tadashi, Miyake Tatsuya, Fushinobu Shinya, Nakajima Masahiro, Miyanaga Akimasa, Taguchi Hayao
Abstract excerpt
For Thermus caldophilus L-lactate dehydrogenase (TcLDH), fructose 1,6-bisphosphate (FBP) reduced the pyruvate S(0.5) value 10(3)-fold and increased the V(max) value 4-fold at 30 °C and pH 7.0, indicating that TcLDH has a much more T state-sided allosteric equilibrium than Thermus thermophilus L-lactate dehydrogenase, which has only two amino acid replacements, A154G and H179Y. The inactive (T) and active (R)...
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