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1 catalyzes the rearrangement of chorismate to prephenate.
2 he pericyclic rearrangement of chorismate to prephenate.
3 nd catalyzes the conversion of chorismate to prephenate.
4 ntramolecular rearrangement of chorismate to prephenate.
6 itated discovery of the tomato gene encoding prephenate aminotransferase, which converts prephenate t
7 We present here the first identification of prephenate aminotransferases (PATs) in seven arogenate-c
8 lly informed biochemical characterization of prephenate aminotransferases (PPA-ATs) that belong to cl
9 easurable catalytic activity, yet bound both prephenate and a competitive inhibitor (S-DNBA) comparab
11 nd ADT homologs indeed efficiently converted prephenate and arogenate into arogenate and Phe, respect
13 indicate that the PDH domain, in which NAD, prephenate and tyrosine binding sites were present, was
15 ic analyses showed an unprecedented role for prephenate as the carboxyl donor and the involvement of
17 ne binding to the regulatory site as well as prephenate binding to the dehydratase domain, both throu
18 al structure of the full-length protein with prephenate bound and the accompanying small angle x-ray
24 contains distinct chorismate mutase (CM) and prephenate dehydratase (PDT) domains as well as a regula
25 two catalytic domains (chorismate mutase and prephenate dehydratase activities) as well as one R-doma
26 n fragment (residues 101-386) containing the prephenate dehydratase and regulatory domains, and (c) R
28 P-protein, a bifunctional chorismate mutase/prephenate dehydratase that is feedback inhibited by Phe
29 the biosynthetic enzymes chorismate mutase, prephenate dehydratase, and prephenate dehydrogenase in
30 inotransferase, a bidomain chorismate mutase/prephenate dehydratase, imidazole acetol-phosphate amino
31 oute in which arogenate dehydratase (ADT) or prephenate dehydratase, respectively, plays a key role.
33 mer that exhibits chorismate mutase (CM) and prephenate dehydrogenase (PDH) activities, both of which
34 orismate mutase, prephenate dehydratase, and prephenate dehydrogenase in cell extracts, so the inhibi
38 r the Claisen rearrangement of chorismate to prephenate has been investigated by application of the c
39 f the Claisen rearrangement of chorismate to prephenate have been examined in water and methanol.
40 r the Claisen rearrangement of chorismate to prephenate in six different environments: water, wild-ty
41 ant PAT enzymes exhibit high activity toward prephenate, indicating that the corresponding genes enco
42 ferase is required for the transamination of prephenate into arogenate, but the identity of the genes
43 with the reactant chorismate or the product prephenate, no water molecule remained near the oxygen o
44 lues of 1140, 490, and 620 M(-1) S(-1), with prephenate not serving as a substrate unless excess reco
45 via the action of either arogenate (ADT) or prephenate (PDT) dehydratases; however, neither enzyme(s
46 that the relative rate of the chorismate --> prephenate reaction is overwhelmingly dependent on the e
47 the important features of the chorismate --> prephenate reaction using molecular dynamics (MD) and th
49 uggest that, along with ADT, a gene encoding prephenate-specific PPA-AT was transferred from a Chloro
51 cilysin antibiotic pathway, BacABGF, convert prephenate to a tetrahydrotyrosine (H(4)Tyr) diastereome
53 rous phenolic compounds, is synthesized from prephenate via an arogenate and/or phenylpyruvate route
54 acid anticapsin from the primary metabolite prephenate, we have overproduced, purified, and characte
55 0), more efficiently utilized arogenate than prephenate, whereas the remaining three, ADT3 (At2g27820
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