The Core of Allosteric Motion in Thermus caldophilus l-Lactate Dehydrogenase

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-lact...

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Shranjeno v:
Bibliografske podrobnosti
izdano v:J Biol Chem
Main Authors: Ikehara, Yoko, Arai, Kazuhito, Furukawa, Nayuta, Ohno, Tadashi, Miyake, Tatsuya, Fushinobu, Shinya, Nakajima, Masahiro, Miyanaga, Akimasa, Taguchi, Hayao
Format: Artigo
Jezik:Inglês
Izdano: American Society for Biochemistry and Molecular Biology 2014
Teme:
Enzymology
Online dostop:https://ncbi.nlm.nih.gov/pmc/articles/PMC4223352/
https://ncbi.nlm.nih.gov/pubmed/25258319
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1074/jbc.M114.599092
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