Formate dehydrogenase NADP-dependent

Yamamoto I, T Saiki, S-M Liu, LG Ljungdahl (1983) Purification and properties of NADP-dependent formate dehydrogenase from Clostridium thermoaceticum, a tungsten-selenium-iron protein. J Biol Chem 258 1826-1832. 

Klyushnichenko, V., Tishkov, V. andKula, M.R. (1997) Rapid SDS-Gel capillary electrophoresis for the analysis of recombinant NADP(+)-dependent formate dehydrogenase during expression in Escherichia coli cells and its purification. J... 

Cytosolic alcohol dehydrogenases only act on free retinol, not retinol bound to CRBP, so they are unlikely to he involved in formation of retinaldehyde and retinoic acid. Furthermore, inhihition of cytosolic alcohol dehydrogenases does not inhibit the oxidation of retinol to retinoic acid (Boerman and Napoli, 1996). CRBP-bound retinol is a substrate for atleast three microsomal NADP+-dependent dehydrogenases hut, given the intracellular NADP+ NADPH ratio (0.01, compared with an NAD+ NADH ratio of the order of 10 ), it is likely that these microsomal enzymes wiU act mainly to reduce retinaldehyde to retinol and not to oxidize retinol. 

Acetogenesis and the primary structure of the NADP-dependent formate dehydrogenase of Clostridium thermoaceticum, a tungsten-selenium-iron protein. 

C. thermoaceticum contains a NADP-dependent formate dehydrogenase that catalyzes the reversible reduction of COj with NADPH (Reaction 4). It was found in 1966 [17], and subsequently its formation was shown to be dependent on several metals present in the growth medium [18]. It was purified by Yamamoto et al. [19]. 

Tishkov, V.I., Yasnyi, I.E., Sadykhov, E.G., Matorin, A.D., and Serov, A.E. (2006) Study of thermal stability of mutant NADP -dependent formate dehydrogenases from Pseudomonas sp. 101. Dold. Biochem. Biophys., 409,... 

Hatrongjit, R. and Packdibamrung, K. (2010) A novel NADP -dependent formate dehydrogenase from Burkholderia stabilis 15516 screening, purification and characterization. Enzyme Microb. Technol, 46, 557-561. 

Two types of enzymes have been identified, one in the membrane and the other in the cytoplasm (Asai, 1968). The D- and L-lactate oxydases are membranal enzymes which do not reqnire a cofactor bnt fnnction with the cytochrome chain. The membranes also contain the pymvate decarboxylase, catalyzing the transformation into ethanal. In the cytoplasm, D- and L-lactate dehydrogenases ensure the oxidation of lactate into pyrnvate. The pyruvate decarboxylase ensures ethanal prodnc-tion. Finally, the NADP-dependent ALDH leads to the formation of acetic acid. This metabolism does not seem to be particnlarly active in wine it has never been proven that it is the sonrce of wine spoilage. 

Weckbecker, A. and Hummel, W. (2004) Improved synthesis of chiral alcohols with Escherichia coli cells co-expressing pyridine nucleotide transhydrogenase, NADP+-dependent alcohol dehydrogenase and NAD+-dependent formate dehydrogenase. Biotechnol. Lett., 26, 1739-1744. 

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