13100-78-2Relevant academic research and scientific papers
A fungal prenyltransferase catalyzes the regular di-prenylation at positions 20 and 21 of paxilline
Liu, Chengwei,Noike, Motoyoshi,Minami, Atsushi,Oikawa, Hideaki,Dairi, Tohru
, p. 448 - 454 (2014)
A putative indole diterpene biosynthetic gene cluster composed of eight genes was identified in a genome database of Phomopsis amygdali, and from it, biosynthetic genes of fusicoccin A were cloned and characterized. The six genes showed significant similarities to pax genes, which are essential to paxilline biosynthesis in Penicillium paxilli. Recombinants of the three putative prenyltransferase genes in the cluster were overexpressed in Escherichia coli and characterized by means of in vitro experiments. AmyG is perhaps a GGDP synthase. AmyC and AmyD were confirmed to be prenyltransferases catalyzing the transfer of GGDP to IGP and a regular di-prenylation at positions 20 and 21 of paxilline, respectively. AmyD is the first know example of an enzyme with this function. The Km values for AmyD were calculated to be 7.6 ± 0.5 μM for paxilline and 17.9 ± 1.7 μM for DMAPP at a kcat of 0.12 ± 0.003/s.
Specificity of geranylgeranyl diphosphate synthase for homoallylic substrate analogs
Ohya, Norimasa,Ichijo, Takumi,Sato, Hana,Nakamura, Takeshi,Yokota, Saki,Sagami, Hiroshi,Nagaki, Masahiko
, p. 179 - 182 (2015/09/01)
The goal of this study was to determine the substrate specificity of Homo sapiens geranylgeranyl diphosphate synthase (GGPPase) for analogs of isopentenyl diphosphate (IPP) to facilitate the application to organic synthesis techniques to the study of prenyl chain elongation enzymes. For this purpose, we used the IPP analogs 2a-d, which contain different alkyl side-chains at the 3-position, as substrates of the condensation reaction with the allylic substrate geranyl diphosphate (GPP) that is catalyzed by GGPPase. GGPPase catalyzed the reaction of GPP with 3-desmethylisopentenyl diphosphate (but-3-enyl diphosphate) to yield 3-desmethylfarnesyl diphosphate (12.1%), as well as the reaction of GPP with 3-ethylbut-3-enyl diphosphate or 3-propylbut-3-enyl diphosphate to yield 3-ethylfarnesyl diphosphate (46.9%) or 3-propylfarnesyl diphosphate (22.6%), respectively. However, a reaction product was not detected when 3-butylbut-3-enyl diphosphate was used as substrate.
Biosynthetic gene-based secondary metabolite screening: A new diterpene, methyl phomopsenonate, from the fungus Phomopsis amygdali
Toyomasu, Tomonobu,Kaneko, Akane,Tokiwano, Tetsuo,Kanno, Yuya,Kanno, Yuri,Niida, Rie,Miura, Shigeyoshi,Nishioka, Taiki,Ikeda, Chiho,Mitsuhashi, Wataru,Dairi, Tohru,Kawano, Tomikazu,Oikawa, Hideaki,Kato, Nobuo,Sassa, Takeshi
body text, p. 1541 - 1548 (2009/10/02)
The presence of the geranylgeranyl diphosphate synthase (GGS) gene is a common feature of gene clusters for diterpene biosynthesis. We demonstrated identification of a diterpene gene cluster using homology- based PCR of GGS genes and the subsequent genome
