Muth J D, Allen C M
Arch Biochem Biophys. 1984 Apr;230(1):49-60. doi: 10.1016/0003-9861(84)90085-7.
a++Undecaprenyl pyrophosphate synthetase has been purified from Lactobacillus plantarum. It catalyzes the formation of a C55 polyprenyl pyrophosphate having isoprene residues with cis stereochemistry. The enzyme was shown to be an acidic protein (pI = 5.1), which can be partially purified by preparative gel electrophoresis and Blue-agarose column chromatography. The Km's of the enzyme for its substrates t,t-farnesyl pyrophosphate and isopentenyl pyrophosphate were determined to be 0.13 and 1.92 microM, respectively. The molecular weight of the enzyme was estimated by molecular sieve chromatography and gradient centrifugation to be 56,000 +/- 4000. Analysis by sodium dodecyl sulfate-polyacrylamide gel electrophoresis indicated that the protein was composed of a dimer of 30,000-Da subunits. The enzyme was inactivated by the arginine-specific reagents phenylglyoxal, butanedione and, cyclohexanedione, but this inactivation was not prevented by either of the substrates.
已从植物乳杆菌中纯化出十一异戊烯基焦磷酸合成酶。它催化形成具有顺式立体化学的异戊二烯残基的C55聚异戊二烯焦磷酸。该酶是一种酸性蛋白质（pI = 5.1），可通过制备性凝胶电泳和蓝琼脂糖柱色谱进行部分纯化。该酶对其底物反，反-法呢基焦磷酸和异戊烯基焦磷酸的Km值分别测定为0.13和1.92 microM。通过分子筛色谱和梯度离心估计该酶的分子量为56,000±4000。十二烷基硫酸钠-聚丙烯酰胺凝胶电泳分析表明该蛋白质由30,000道尔顿亚基的二聚体组成。该酶被精氨酸特异性试剂苯乙二醛、丁二酮和环己二酮灭活，但这种灭活不受任何一种底物的阻止。
