Purification and properties of an unusual UDP-glucose dehydrogenase, NADPH-dependent, from Xanthomonas albilineans
Purification and properties of an unusual UDP-glucose dehydrogenase, NADPH-dependent, from Xanthomonas albilineans
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DOI：
10.1016/j.micres.2006.07.011
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发表时间：
2008-01-01
影响因子：
6.7
通讯作者：
Vicente, C.
中科院分区：
文献类型：
--
作者：
Blanch, Maria;Legaz, Maria-Estrella;Vicente, C.
黄单胞菌产生UDP-葡萄糖脱氢酶生长在蔗糖上。该酶通过使用分子氧和NADPH将UDP-葡萄糖氧化为UDP-葡萄糖醛酸。NADPH的酶促氧化动力学与供氧量呈线性关系。该酶已被纯化为均一的。纯化酶的pI值为8.98，分子量估计为14 kDa。该酶对UDP-葡萄糖浓度表现出Michaelian动力学。UDP-葡萄糖的K（m）值为0.87 mM，NADPH的K（m）值为0.26 mM，尽管该酶有三个不同的位点与NADPH相互作用。该酶被UDP-葡萄糖浓度高于1.3 mM抑制。N-末端序列已确定为IQPYNH。(c)2006年Elsevier GmbH。All rights reserved.
Xanthomonas albilineans produces a UDP-glucose dehydrogenase growing on sucrose. The enzyme oxidizes UDP-glucose to UDP-glucuronic acid by using molecular oxygen and NADPH. Kinetics of enzymatic oxydation of NADPH is linearly dependent on the amount of oxygen supplied. The enzyme has been purified at homogeneity. The value of pl of the purified enzyme is 8.98 and its molecular mass has been estimated as about 14 kDa. The enzyme shows a michaelian kinetics for UDP-glucose concentrations. The value of K(m) for UDP-glucose is 0.87 mM and 0.26 mM for NADPH, although the enzyme has three different sites to interact with NADPH. The enzyme is inhibited by UDP-glucose concentrations higher than 1.3 mM. N-Terminal sequence has been determined as IQPYNH. (c) 2006 Elsevier GmbH. All rights reserved.