The possible occurrence of zinc in ribitol and sorbitol dehydrogenases from Mycobacterium sp. 279.
The activity of polyhydric alcohol dehydrogenases in Mycobacterium sp. 279 was studied under limitation of zinc in the growth medium. It was found that the activity of ribitol and sorbitol dehydrogenases were markedly lowered and that of D-arabinitol dehydrogenase remained unchanged in the Zn2+-deficient cells. Other ions tested i.e., Co2+, Cu2+, Ni2+ and Mn2+ failed to substitute Zn2+ ions in their effect on the enzyme activities. The Zn2+-responsive enzymes were sensitive to the chelating agents (1,10-phenanthroline, 2,2'-dipyridyl), whereas D-arabinitol dehydrogenase was insensitive. The results indicate possible existence of a zinc component in the ribitol and sorbitol dehydrogenases from Mycobacterium sp. 279.
D002413:Cations, Divalent; D007064:L-Iditol 2-Dehydrogenase / Q000302:isolation & purification / Q000378:metabolism*; D009161:Mycobacterium / Q000201:enzymology*; D013401:Sugar Alcohol Dehydrogenases / Q000302:isolation & purification / Q000378:metabolism*; D015032:Zinc / Q000494:pharmacology*
D002413:Cations, Divalent; D013401:Sugar Alcohol Dehydrogenases; C022751:D-arabinitol dehydrogenase; D007064:L-Iditol 2-Dehydrogenase; C022529:ribitol 2-dehydrogenase; D015032:Zinc