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1 ng this a hemiterpene synthase rather than a monoterpene synthase.
2 at the produced GPP can be used by plastidic monoterpene synthases.
3 d biosynthesis and others with activities as monoterpene synthases.
4 nd of monoterpenes, indicating that they are monoterpene synthases.
5  final cyclization reaction catalyzed by the monoterpene synthases.
6 brary that appeared to encode three distinct monoterpene synthases.
7 prene synthase is a myrcene/ocimene (acyclic monoterpenes) synthase.
8 t has been shown to possess both sesqui- and monoterpene synthase activities resulted in increased le
9 ment with the results of cell-free assays of monoterpene synthase activity, followed by the coordinat
10 mechanism of GES is similar to that of other monoterpene synthases and is different from the action o
11  two that were functionally characterized as monoterpene synthases and three that preferred farnesyl
12 hase falls into the TPS-d1 group (gymnosperm monoterpene synthases) and is most closely related to li
13  residues in length (71.5 kDa); all of these monoterpene synthases appear to be translated as preprot
14                               Genes encoding monoterpene synthases are also prevalent, and they fall
15 owever, closer inspection indicates that the monoterpene synthases arise earlier, as shown by an abbr
16 dization using probes derived from the three monoterpene synthase cDNAs.
17 hat isoprene synthases are either within the monoterpene synthase clade or sister to it.
18 ible for 1,8-cineole biosynthesis, the first monoterpene synthase discovered in fungi.
19     Here we report the characterization of a monoterpene synthase encoded by two identical, closely l
20 imilar biochemical properties to other known monoterpene synthases, except for a relatively low K(m)
21 gene was created by a duplication event of a monoterpene synthase followed by a localized gene conver
22 thases from conifers more closely than other monoterpene synthases from angiosperm species.
23      Sequence comparison revealed that these monoterpene synthases from grand fir resemble sesquiterp
24 solate the cDNAs encoding three multiproduct monoterpene synthases from this species that were functi
25   All previously isolated 'cineole cassette'-monoterpene synthase genes are multi product enzymes tha
26 elopmental, and rhythmic expression of these monoterpene synthase genes in snapdragon flowers reveale
27                                          The monoterpene synthase genes in the cluster likely evolved
28 method would allow the identification of new monoterpene synthase genes using transient expression in
29  to two P450s that were coexpressed with two monoterpene synthases in flowers and were thus predicted
30 ae), thus indicating gene diversification of monoterpene synthases in section Alatae.
31  diphosphate as the "universal" substrate of monoterpene synthases, in tomato glands neryl diphosphat
32 ray structure of the unique "head-to-middle" monoterpene synthase, lavandulyl diphosphate synthase (L
33 specific, methyl jasmonate (MeJA)-responsive monoterpene synthase (Li3CARS) from Lavandula x intermed
34 ion of alternative product profiles of these monoterpene synthases of conifer defense against insects
35 nt enzymes resemble the corresponding native monoterpene synthases of wound-induced grand fir stem.
36                                            A monoterpene synthase producing the set of 'cineole casse
37             Os02g02930 was found to encode a monoterpene synthase producing the single product S-lina
38 gesting that the reaction mechanism of Tps-g monoterpene synthase product formation does not proceed
39  Mg17 aligned more closely to the angiosperm monoterpene synthase subclass TPS-b.
40 haracteristic feature of the Tps-d and Tps-b monoterpene synthases, suggesting that the reaction mech
41 oded by three of these complementary DNAs: a monoterpene synthase that belongs to the TPS-b clade cat
42 dization to map the expression of a putative monoterpene synthase to the epithelium of glands and use
43              These newly isolated snapdragon monoterpene synthases, together with Arabidopsis AtTPS14
44  activated in response to wounding, with the monoterpene synthases up-regulated first (transcripts de
45 ound-induced accumulation of transcripts for monoterpene synthases was demonstrated by RNA blot hybri
46 es (R58R59) which is highly conserved in the monoterpene synthases, was removed.
47  availability of cDNA species encoding these monoterpene synthases will allow an understanding of the

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