Nakamura T, Naito A, Takahashi Y, Akanuma H
J Biochem. 1986 Mar;99(3):607-13. doi: 10.1093/oxfordjournals.jbchem.a135519.
Bacteria which grow on 1,5-anhydro-D-glucitol (AG) were isolated from soil. One such strain showing the highest AG-assimilating activity was further characterized and identified as a new strain of the Pseudomonas family (named Pseudomonas sp. NK-85001). A subcellular membranous fraction obtained from this strain catalyzed the oxidation of AG to 1,5-anhydro-D-fructose. This oxidation reaction consumed molecular oxygen as the terminal electron acceptor. The AG-oxidizing activity was further purified after solubilization. The AG oxidation catalyzed by this solubilized enzyme utilized molecular oxygen only in the presence of an electron mediator such as 2,6-dichlorophenolindophenol or phenazine methosulfate. Thus, the enzyme was suggested to be a dehydrogenase rather than an oxidase. The solubilized enzyme preparation also showed a strict substrate specificity. The observed specificity indicated that application of the enzyme for AG assay in clinical samples might be possible.
从土壤中分离出能在1,5 - 脱水 - D - 葡萄糖醇（AG）上生长的细菌。其中一株表现出最高AG同化活性的菌株被进一步鉴定并确定为假单胞菌属的一个新菌株（命名为假单胞菌sp. NK - 85001）。从该菌株获得的亚细胞膜部分催化AG氧化为1,5 - 脱水 - D - 果糖。该氧化反应消耗分子氧作为末端电子受体。溶解后，AG氧化活性进一步纯化。这种溶解酶催化的AG氧化仅在存在电子介质如2,6 - 二氯酚靛酚或吩嗪硫酸甲酯时才利用分子氧。因此，该酶被认为是一种脱氢酶而非氧化酶。溶解酶制剂也表现出严格的底物特异性。观察到的特异性表明该酶可能用于临床样本中AG的检测。
