Siebert M, Bechthold A, Melzer M, May U, Berger U, Schröder G, Schröder J, Severin K, Heide L
Institut für Pharmazeutische Biologie, Universität Freiburg, Germany.
FEBS Lett. 1992 Aug 3;307(3):347-50. doi: 10.1016/0014-5793(92)80710-x.
Chorismate pyruvate-lyase activity was detected in extracts of Escherichia coli. 4-Hydroxybenzoate was identified as the product of the enzymatic reaction by chemical derivatization and GC-MS analysis. The ubiC gene, coding for the chorismate pyruvate-lyase, was cloned and sequenced. The molecular weight of the gene product was calculated as 18,776 Da and confirmed by expression of the protein in E. coli minicells. The ubiA gene, coding for the 4-hydroxybenzoate octaprenyl transferase, was identified by sequence homology and complementation of a ubiA- strain. It is located directly downstream of ubiC in a typical operon structure.
在大肠杆菌提取物中检测到分支酸丙酮酸裂解酶活性。通过化学衍生化和气相色谱-质谱分析,确定4-羟基苯甲酸为酶促反应的产物。克隆并测序了编码分支酸丙酮酸裂解酶的ubiC基因。计算出该基因产物的分子量为18,776道尔顿,并通过在大肠杆菌微小细胞中表达该蛋白得到证实。通过序列同源性和ubiA-菌株的互补作用,鉴定出编码4-羟基苯甲酸辛二烯基转移酶的ubiA基因。它以典型的操纵子结构直接位于ubiC的下游。