Barengo R, Krisman C R
Acta Physiol Lat Am. 1976;26(5):289-96.
Glycogen biosynthesis was studied in Escherichia coli. An enzyme complex composed of UDP-glucose; protein glucosyltransferase, ADP-glucose: protein glucosyltransferase and ADP-glucose: alpha-1,4 glucan alpha-4-glucosyltransferase was found. Further results revealed that while glycogen concentration remained unchanged, the specific activity of the glucosyltransferase complex increased during the growth phase of the culture. The detergents Lubrol and Brij provoked a decrease of 80% and 20% in the glucose transfer to protein from ADP-glucose and UDP-glucose, respectively. These detergents did not inhibit the glucose incorporation into glycogen by ADP-glucose: alpha-1,4-glucosyltransferase. We postulated that the biosynthesis of glycogen in Escherichia coli could be initiated by two different enzymes which catalyze the transfer of glucose from UDP-glucose or ADP-glucose to an acceptor protien. In a second step, the glucan protein formed is used as primer by the ADP-glucose: alpha-1,4 glucan alpha-1-glucosyltransferase for glycogen formation.
在大肠杆菌中研究了糖原生物合成。发现了一种由UDP-葡萄糖、蛋白质葡糖基转移酶、ADP-葡萄糖：蛋白质葡糖基转移酶和ADP-葡萄糖：α-1,4-葡聚糖α-4-葡糖基转移酶组成的酶复合物。进一步的结果表明，在培养物的生长阶段，虽然糖原浓度保持不变，但葡糖基转移酶复合物的比活性增加。去污剂Lubrol和Brij分别使从ADP-葡萄糖和UDP-葡萄糖向蛋白质的葡萄糖转移减少了80%和20%。这些去污剂不抑制ADP-葡萄糖：α-1,4-葡糖基转移酶将葡萄糖掺入糖原。我们推测大肠杆菌中糖原的生物合成可能由两种不同的酶启动，这两种酶催化葡萄糖从UDP-葡萄糖或ADP-葡萄糖转移到受体蛋白上。在第二步中，形成的葡聚糖蛋白被ADP-葡萄糖：α-1,4-葡聚糖α-1-葡糖基转移酶用作糖原形成的引物。
