Mannitol oxidation in two Micromonospora isolates and in representative species of other actinomycetes.
Mannitol kinase and mannitol-1-phosphate dehydrogenase activities were detected in two Micromonospora isolates. The presence of these enzyme activities indicates that mannitol is catabolized first to mannitol-1-phosphate and then to fructose-6-phosphate. Mannitol-oxidizing enzymes were also surveyed in representative species of four other genera of actinomycetes. Mannitol-1-phosphate dehydrogenase was detected in cell-free extracts of Streptomyces lactamdurans. In contrast, cell-free extracts of Mycobacterium smegmatis, Nocardia erythrophila, Streptomyces lavendulae, and Actinoplanes missouriensis contained mannitol dehydrogenase activity but no detectable mannitol-1-phosphate dehydrogenase activity. The mannitol dehydrogenase activities in the latter species support the operation of a pathway for catabolism of mannitol that involves the oxidation of mannitol to fructose, followed by phosphorylation to fructose-6-phosphate.
D000192:Actinomycetales / Q000201:enzymology / Q000378:metabolism*; D000429:Alcohol Oxidoreductases / Q000378:metabolism; D002474:Cell-Free System; D008353:Mannitol / Q000378:metabolism*; D008847:Micromonospora / Q000201:enzymology / Q000378:metabolism*; D010084:Oxidation-Reduction; D010770:Phosphotransferases / Q000378:metabolism
D008353:Mannitol; D000429:Alcohol Oxidoreductases; D010770:Phosphotransferases