Conformational Heterogeneity within the Michaelis Complex of Lactate Dehydrogenase
نویسندگان
چکیده
منابع مشابه
Conformational Heterogeneity in the Michaelis Complex of Lactate Dehydrogenase: An Analysis of Vibrational Spectroscopy Using Markov and Hidden Markov Models.
Lactate dehydrogenase (LDH) catalyzes the interconversion of pyruvate and lactate. Recent isotope-edited IR spectroscopy suggests that conformational heterogeneity exists within the Michaelis complex of LDH, and this heterogeneity affects the propensity toward the on-enzyme chemical step for each Michaelis substate. By combining molecular dynamics simulations with Markov and hidden Markov model...
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Energy Landscape of the Michaelis Complex of Lactate Dehydrogenase: Relationship to Catalytic Mechanism
Lactate dehydrogenase (LDH) catalyzes the interconversion between pyruvate and lactate with nicotinamide adenine dinucleotide (NAD) as a cofactor. Using isotope-edited difference Fourier transform infrared spectroscopy on the "live" reaction mixture (LDH·NADH·pyruvate ⇌ LDH·NAD(+)·lactate) for the wild-type protein and a mutant with an impaired catalytic efficiency, a set of interconverting con...
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Proteins are synthesized and enzymes can function at surprisingly high temperatures in thermophilic micro-organisms. This temperature is about 90°C in the case of Bacillus thermus-aquaticus (A.T.C.C. 25104). Lactate dehydrogenase (EC 1.1.1.27) was isolated from this micro-organism, and the temperature dependence of the rate of pyruvate reduction and thermodynamic parameters of heat inactivation...
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ژورنال
عنوان ژورنال: The Journal of Physical Chemistry B
سال: 2011
ISSN: 1520-6106,1520-5207
DOI: 10.1021/jp2015929