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Role of phosphorolytic cleavage in cellobiose and cellodextrin metabolism by the ruminal bacterium Prevotella ruminicola.

机译:瘤胃细菌细小球藻Prevotella ruminicola在纤维二糖和纤维糊精代谢中的磷酸化裂解作用。

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摘要

In bacteria, cellobiose and cellodextrins are usually degraded by either hydrolytic or phosphorolytic cleavage. Prevotella ruminicola B(1)4 is a noncellulolytic ruminal bacterium which has the ability to utilize the products of cellulose degradation. In this organism, cellobiose hydrolytic cleavage activity was threefold greater than phosphorolytic cleavage activity (113 versus 34 nmol/min/mg of protein), as measured by an enzymatic assay. Cellobiose phosphorylase activity (measured as the release of P(i)) was found in cellobiose-, mannose-, xylose-, lactose-, and cellodextrin-grown cells (> 92 nmol of P(i)/min/mg of protein), but the activity was reduced by more than 74% for cells grown on fructose, L-arabinose, sucrose, maltose, or glucose. A small amount of cellodextrin phosphorylase activity (19 nmol/min/mg of protein) was also detected, and both phosphorylase activities were located in the cytoplasm. Degradation involving phosphorolytic cleavage conserves more metabolic energy than simple hydrolysis, and such degradation is consistent with substrate-limiting conditions such as those often found in the rumen.
机译:在细菌中,纤维二糖和纤维糊精通常通过水解或磷酸化裂解而降解。鲁米尼短螺旋杆菌B(1)4是一种非纤维素瘤胃细菌,具有利用纤维素降解产物的能力。在这种生物中,纤维二糖的水解裂解活性比磷酸裂解活性高三倍(113对34 nmol / min / mg蛋白质),通过酶法测定。在纤维二糖,甘露糖,木糖,乳糖和纤维糊精生长的细胞中发现纤维二糖磷酸化酶活性(以P(i)的释放来衡量)(P(i)/ min / mg蛋白质的> 92 nmol) ,但对于果糖,L-阿拉伯糖,蔗糖,麦芽糖或葡萄糖生长的细胞,活性降低了74%以上。还检测到少量的纤维糊精磷酸化酶活性(19 nmol / min / mg蛋白质),并且两种磷酸化酶活性均位于细胞质中。与简单的水解反应相比,涉及磷酸酶解的降解反应可节省更多的代谢能,且这种降解反应与底物限制条件(如瘤胃中经常发现的条件)一致。

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