Szumiło T, Byra A
Acta Biochim Pol. 1984;31(4):401-8.
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.
在生长培养基中锌受限的条件下，对分枝杆菌属279中的多元醇脱氢酶活性进行了研究。结果发现，在缺锌的细胞中，核糖醇脱氢酶和山梨醇脱氢酶的活性显著降低，而D -阿拉伯糖醇脱氢酶的活性保持不变。所测试的其他离子，即Co2 +、Cu2 +、Ni2 +和Mn2 +，在对酶活性的影响方面未能替代Zn2 +离子。锌响应酶对螯合剂（1,10 -菲咯啉、2,2'-联吡啶）敏感，而D -阿拉伯糖醇脱氢酶不敏感。结果表明，分枝杆菌属279的核糖醇脱氢酶和山梨醇脱氢酶中可能存在锌成分。
