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首页> 外文期刊>Journal of bacteriology >Phosphoenolpyruvate-dependent maltose:phosphotransferase activity in Fusobacterium mortiferum ATCC 25557: specificity, inducibility, and product analysis.
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Phosphoenolpyruvate-dependent maltose:phosphotransferase activity in Fusobacterium mortiferum ATCC 25557: specificity, inducibility, and product analysis.

机译：磷酸镰刀菌ATCC 25557中依赖于磷酸烯醇丙酮酸的麦芽糖：磷酸转移酶的活性：特异性，诱导性和产物分析

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Phosphoenolypyruvate-dependent maltose:phosphotransferase activity was induced in cells of Fusobacterium mortiferum ATCC 25557 during growth on maltose. The disaccharide was rapidly metabolized by washed cells maintained under anaerobic conditions, but fermentation ceased immediately upon exposure of the cell suspension to air. Coincidentally, high levels of a phosphorylated derivative accumulated within the cells. Chemical and enzymatic analyses, in conjunction with data from 1H, 13C, and 31P nuclear magnetic resonance spectroscopy, established the structure of the purified compound as 6-O-phosphoryl-alpha-D-glucopyranosyl-(1-4)-D-glucose (maltose 6-phosphate). A method for the preparation of substrate amounts of this commercially unavailable disaccharide phosphate is described. Permeabilized cells of F. mortiferum catalyzed the phosphoenolpyruvate-dependent phosphorylation of maltose under aerobic conditions. However, the hydrolysis of maltose 6-phosphate (to glucose 6-phosphate and glucose) by permeabilized cells or cell-free preparations required either an anaerobic environment or addition of dithiothreitol to aerobic reaction mixtures. The first step in dissimilation of the phosphorylated disaccharide appears to be catalyzed by an oxygen-sensitive maltose 6-phosphate hydrolase. Cells of F. mortiferum, grown previously on maltose, fermented a variety of alpha-linked glucosides, including maltose, turanose, palatinose, maltitol, alpha-methylglucoside, trehalose, and isomaltose. Conversely, cells grown on the separate alpha-glucosides also metabolized maltose. For this anaerobic pathogen, we suggest that the maltose:phosphotransferase and maltose 6-phosphate hydrolase catalyze the phosphorylative translocation and cleavage not only of maltose but also of structurally analogous alpha-linked glucosides.
机译：在麦芽糖上生长期间，在腐殖杆菌ATCC 25557的细胞中诱导了依赖磷酸烯丙基丙酮酸的麦芽糖：磷酸转移酶活性。二糖被保持在厌氧条件下的洗涤细胞迅速代谢，但是当细胞悬浮液暴露于空气后，发酵立即停止。巧合的是，高水平的磷酸化衍生物积累在细胞内。化学和酶促分析，结合1H，13C和31P核磁共振波谱数据，确定了纯化化合物的结构为6-O-磷酰基-α-D-吡喃葡萄糖基-（1-4）-D-葡萄糖（麦芽糖6-磷酸）。描述了一种制备底物量的这种商业上不可用的二糖磷酸酯的方法。在有氧条件下，桑蚕的透化细胞催化了麦芽糖的磷酸烯醇丙酮酸依赖性磷酸化。然而，通透的细胞或无细胞制剂将麦芽糖6-磷酸水解（转化为6-磷酸葡萄糖和葡萄糖）需要厌氧环境或将二硫苏糖醇添加到需氧反应混合物中。磷酸二糖异化的第一步似乎是由对氧敏感的麦芽糖6-磷酸水解酶催化的。先前在麦芽糖上生长的F. mortiferum细胞发酵了多种与α连接的葡糖苷，包括麦芽糖，杜拉糖，帕拉金糖，麦芽糖醇，α-甲基葡糖苷，海藻糖和异麦芽糖。相反，在单独的α-葡萄糖苷上生长的细胞也代谢麦芽糖。对于这种厌氧性病原体，我们建议麦芽糖：磷酸转移酶和麦芽糖6-磷酸水解酶不仅催化麦芽糖的磷酸化转运和裂解，而且还催化结构类似的α-连接的糖苷。

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