Glycerol dehydrase

FIGURE 4. The eleven adenosylcobalamin-dependent rearrangements so far described. Notes D-a-lysine [L-p-lysine] 5,6-aminomutase catalyzes similar rearrangements on two substrates diol dehydrase and glycerol dehydrase have over-lapping substrate specificity. 

Toraya, T., 1994, Diol dehydrase and glycerol dehydrase, coenzyme B12 dependent isozymes. In Metal ions in biological systems (H. Sigel and A. Sigel, eds.), Vol. 30, Marcel Dekker, New York, pp. 217n254. 

The enzymatic reactions in which adenosylcobalamin was known to serve as coenzyme by 1964 were those of glutamate mutase, methylmalonyl-CoA mutase (MCM), " propane-1,2-diol hydro-lyase (dioldehydrase, DDH), and glycerol hydro-lyase (glycerol dehydrase), shown in Equations (1)—(4). 

Observations of paramagnetic species in the reactions of ethanolamine ammonia-lyase (EAL), an adenosylcobalamin-dependent deamination, and glycerol dehydrase inspired searches for free radical intermediates. Such intermediates would be compatible with the observation of cob(II)alamin in the reaction of DDH. 

Sass C, Walter J, Bennett GN (1993) Isolation of mutants of Clostridium acetobutylicum ATCC 824. Curr Microbiol 26 151-154 Sauer U, Diirre P (1995) Differential induction of genes related to solvent formation during the shift from acidogenesis to solventogenesis in continuous culture of Clostridium acetobutylicum. FEMS Microbiol Lett 125 115-120 Schneider Z, Larsen EG, Jacobson G, Johnson BC, Pawelkiewicz J (1970) Purification and properties of glycerol dehydrase. J Biol Chem 245 3388-3396 Schoutens GH, Groot WJ (1985) Economic feasibility of the production of isopropanol-butanol-ethanol fuels from whey permeate. Process Biochem 20 117-121... 

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