Tholl D, Croteau R, Gershenzon J
Max-Planck Institute of Chemical Ecology, Jena, Germany.
Arch Biochem Biophys. 2001 Feb 15;386(2):233-42. doi: 10.1006/abbi.2000.2212.
In the conifer Abies grandis (grand fir), a secreted oleoresin rich in mono-, sesqui-, and diterpenes serves as a constitutive and induced defense against insects and pathogenic fungi. Geranyl diphosphate (GPP) and farnesyl diphosphate (FPP) synthase, two enzymes which form the principal precursors of the oleoresin mono- and sesquiterpenes, were isolated from the stems of 2-year-old grand fir saplings. These enzymes were partially purified by sequential chromatography on DEAE-Sepharose, Mono-Q, and phenyl-Sepharose to remove competing phosphohydrolase and isopentenyl diphosphate (IPP) isomerase activities. GPP and FPP synthase formed GPP and E,E-FPP, respectively, as the sole products of the enzymatic condensation of IPP and dimethylallyl diphosphate (DMAPP). The properties of both enzymes are broadly similar to those of other prenyltransferases. The apparent native molecular masses are 54 +/- 3 kDa for GPP synthase and 110 +/- 6 kDa fo
在针叶树巨冷杉（大冷杉）中，一种富含单萜、倍半萜和二萜的分泌型油性树脂可作为对昆虫和致病真菌的组成型和诱导型防御物质。香叶基二磷酸（GPP）合酶和法尼基二磷酸（FPP）合酶这两种酶构成了油性树脂单萜和倍半萜的主要前体，它们是从2年生大冷杉幼树的茎中分离出来的。这些酶通过在DEAE-琼脂糖、Mono-Q和苯基-琼脂糖上进行连续色谱法进行部分纯化，以去除竞争性磷酸水解酶和异戊烯基二磷酸（IPP）异构酶的活性。GPP合酶和FPP合酶分别形成GPP和E,E-FPP，作为IPP和二甲基烯丙基二磷酸（DMAPP）酶促缩合的唯一产物。这两种酶的特性与其他异戊二烯基转移酶的特性大致相似。GPP合酶的表观天然分子量为54±3 kDa，FPP合酶的表观天然分子量为110±6 kDa 。
