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1 ernate sesquiterpene products in addition to trichodiene.
2 diphosphate to the sesquiterpene hydrocarbon trichodiene.
3 l diphosphate for the exclusive formation of trichodiene.
4 total of 153 genes were upregulated by added trichodiene and were significantly enriched for genes li
6 ray of sesquiterpenes (iso-gamma-bisabolene, trichodiene, cuprenene, laurene, isochamigrene, chamigre
7 results strongly suggest that the release of trichodiene from the enzyme active site is the rate-limi
8 .2 s-1) corresponding to the accumulation of trichodiene on the surface of the enzyme was followed by
12 resolution X-ray crystal structure of D100E trichodiene synthase and the 2.6 A resolution structure
13 bation buffer, the kcat/Km of both wild type trichodiene synthase and the D104E dropped significantly
15 attenuation of active site closure in D100E trichodiene synthase compromises enzyme-substrate packin
16 The x-ray crystal structure of recombinant trichodiene synthase from Fusarium sporotrichioides has
23 nover reactions of [1,2-14C]FPP catalyzed by trichodiene synthase were carried out at 4, 15, or 30 de
24 segregated with the TRI5 gene (which encodes trichodiene synthase) and probably maps in the trichothe
26 y-state catalytic rate (kcat = 0.09 s-1) for trichodiene synthase-catalyzed conversion of farnesyl di
28 ations of R-azabisabolene to Y305F and D100E trichodiene synthases do not correspond to binding confo
29 pyrophosphate (PP(i)) and of Y305F and D100E trichodiene synthases in ternary complexes with PP(i) an
30 is the conversion of farnesyl diphosphate to trichodiene (TD), a volatile organic compound (VOC), cat
31 gene expression, cultures were treated with trichodiene, the first metabolic intermediate specific t
32 malous sesquiterpene products in addition to trichodiene when incubated with farnesyl diphosphate.
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