Optimizing the Michaelis Complex of Trimethylamine Dehydrogenase
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چکیده
منابع مشابه
Optimizing the Michaelis complex of trimethylamine dehydrogenase: identification of interactions that perturb the ionization of substrate and facilitate catalysis with trimethylamine base.
Recent evidence from isotope studies supports the view that catalysis by trimethylamine dehydrogenase (TMADH) proceeds from a Michaelis complex involving trimethylamine base and not, as thought previously, trimethylammonium cation. In native TMADH reduction of the flavin by substrate (perdeuterated trimethylamine) is influenced by two ionizations in the Michaelis complex with pK(a) values of 6....
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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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Trimethylamine dehydrogenase contains an unusual covalently bound coenzyme, which has been isolated in the form of a flavin peptide and converted to a novel type of aminoacyl flavin (Steenkamp, D. J., Kenney, W. C., and Singer, T. P. (1978) J. Biol. Chem. 253, 2812-2817). The present paper presents evidence that the aminoacyl coenzyme is a thioether substituted at C-6 of the flavin ring of FMN,...
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متن کاملIdentification of the dimethylamine-trimethylamine complex in the gas phase.
We have identified the dimethylamine-trimethylamine complex (DMA-TMA) at room temperature in the gas phase. The Fourier transform infrared (FTIR) spectrum of DMA-TMA in the NH-stretching fundamental region was obtained by spectral subtraction of spectra of each monomer. Explicitly correlated coupled cluster calculations were used to determine the minimum energy structure and interaction energy ...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 2001
ISSN: 0021-9258
DOI: 10.1074/jbc.m108296200