Salusjärvi Tuomas, Hvorslev Niels, Miasnikov Andrei N
Danisco Innovation, Sokeritehtaantie 20, Kantvik, 02460, Finland.
Appl Microbiol Biotechnol. 2005 Mar;66(6):664-7. doi: 10.1007/s00253-004-1775-3. Epub 2004 Nov 24.
The chromosomal locus NP_636946 of Xanthomonas campestris DSM 3586 (ATCC 33913) which was earlier presumed to encode a quinoprotein glucose dehydrogenase has been cloned, expressed in Escherichia coli and the recombinant enzyme has been characterised. It was found to have no glucose dehydrogenase activity but to be active on many different polyols and diols, aliphatic alcohols, certain aldonic acids and amino-sugars. The product of D: -gluconic acid oxidation was 5-keto-D: -gluconic acid. The enzyme differs from polyol/gluconate dehydrogenases found in Gluconobacter by its single-chain architecture, different substrate specificity and much higher (20- to 30-fold) expression level in E.coli.
野油菜黄单胞菌DSM 3586（ATCC 33913）的染色体位点NP_636946，此前被推测编码一种醌蛋白葡萄糖脱氢酶，现已被克隆，在大肠杆菌中表达，并对重组酶进行了表征。结果发现它没有葡萄糖脱氢酶活性，但对许多不同的多元醇和二醇、脂肪醇、某些醛糖酸和氨基糖具有活性。D-葡萄糖酸氧化的产物是5-酮-D-葡萄糖酸。该酶与葡糖杆菌中发现的多元醇/葡萄糖酸脱氢酶不同，其具有单链结构、不同的底物特异性，并且在大肠杆菌中的表达水平要高得多（20至30倍）。
