Hölscher Tina, Weinert-Sepalage Dinusha, Görisch Helmut
Fachgebiet Technische Biochemie, Institut für Biotechnologie, Technische Universität Berlin, D-13353 Berlin, Germany.
Microbiology (Reading). 2007 Feb;153(Pt 2):499-506. doi: 10.1099/mic.0.2006/002196-0.
The GOX1857 gene, which encodes a putative membrane-bound pyrroloquinoline quinone (PQQ)-dependent dehydrogenase in Gluconobacter oxydans ATCC 621H, was characterized. GOX1857 was disrupted and the oxidizing potential of the resulting mutant strain was compared to that of the wild-type. In contrast to the wild-type, the mutant was unable to grow with myo-inositol as the sole energy source and did not show any myo-inositol dehydrogenase activity in vitro, indicating that GOX1857 encodes an inositol dehydrogenase. The association of inositol dehydrogenase with the membrane and the requirement for the cofactor PQQ were confirmed. Inositol dehydrogenase exhibited optimal activity at pH 8.75. As indicated by cultivation on different substrates, inositol dehydrogenase was repressed by d-glucose.
对氧化葡萄糖酸杆菌ATCC 621H中编码一种假定的膜结合吡咯喹啉醌(PQQ)依赖性脱氢酶的GOX1857基因进行了表征。破坏了GOX1857,并将所得突变菌株的氧化电位与野生型进行了比较。与野生型相比,该突变体不能以肌醇作为唯一能量源生长,并且在体外未显示任何肌醇脱氢酶活性,这表明GOX1857编码一种肌醇脱氢酶。证实了肌醇脱氢酶与膜的关联以及对辅因子PQQ的需求。肌醇脱氢酶在pH 8.75时表现出最佳活性。如在不同底物上培养所示,肌醇脱氢酶受到d-葡萄糖的抑制。