Dehydrogenases time scale

Most of the information on interdomain motions come from high-resolution crystal structures several reviews are available (Janin and Wodak 1983 Bennett andHuber 1984 Gerstein et al. 1994). Calculations ofhinge bending modes and domain motions in proteins other than lysozyme have been made. They include antibody molecules where the interdomain motions occur on a nanosecond time scale (McCammon and Karplus 1977 Oi et al. 1984), 1-arabinose-binding protein (Mao et al. 1982), liver alcohol dehydrogenase (Colona-Cesari et al. 1986) and the mouse... 

Deng, H., Zhadin, N., Callender, R. (2001) Dynamics of protein ligand binding on multiple time scales NADH binding to lactate dehydrogenase, Biochemistry 40, 3767—3773. 

Formate dehydrogenase has been reported to have a pH optimum of 7.5-8.5 [25], The pH optimum for the reductive amination of (5) by an extract of T. intermedins was found to be about 8.7. Reductive amination reactions were carried out at pH 8.0. A summary of laboratory-scale batches is shown in Table 2. The time course for a representative batch showing conversion of ketoacid (5) to amino acid (4) is presented in Figure 5 using E. coli/C. boidinii heat-dried cells. 

S)-l-[3,5-Bis(trifluoromethyl)phenyl]ethanol (28, Figure 4.5) is an important intermediate for the synthesis of NK-1 receptor antagonists. Pollard and coworkers used alcohol dehydrogenase from Rhodococcus erythropolis and formate dehydrogenase to recycle NADH [57] and obtain this enantiopure alcohol. Under optimized conditions, the process could be scaled-up at 25 kg at 30 °C with a high substrate concentration (100 g/1) affording a space-time yield of 100-110 g/1 per day. 

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