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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.
5 H7PS substrates and the allosteric inhibitor prephenate.
6 ere, we show that BigE6 encodes a plastidial prephenate aminotransferase (PPA-AT), a key enzyme in th
8 itated discovery of the tomato gene encoding prephenate aminotransferase, which converts prephenate t
9 We present here the first identification of prephenate aminotransferases (PATs) in seven arogenate-c
10 lly informed biochemical characterization of prephenate aminotransferases (PPA-ATs) that belong to cl
11 easurable catalytic activity, yet bound both prephenate and a competitive inhibitor (S-DNBA) comparab
13 nd ADT homologs indeed efficiently converted prephenate and arogenate into arogenate and Phe, respect
15 indicate that the PDH domain, in which NAD, prephenate and tyrosine binding sites were present, was
17 arogenate pathway at chorismate, instead of prephenate as previously thought, and the complete pathw
18 ic analyses showed an unprecedented role for prephenate as the carboxyl donor and the involvement of
19 ere, we have identified the organic compound prephenate as the oxygen donor for the three hydroxylati
21 ne binding to the regulatory site as well as prephenate binding to the dehydratase domain, both throu
22 al structure of the full-length protein with prephenate bound and the accompanying small angle x-ray
28 contains distinct chorismate mutase (CM) and prephenate dehydratase (PDT) domains as well as a regula
29 two catalytic domains (chorismate mutase and prephenate dehydratase activities) as well as one R-doma
30 n fragment (residues 101-386) containing the prephenate dehydratase and regulatory domains, and (c) R
32 idial enzyme produces a functional cytosolic prephenate dehydratase that catalyzes the conversion of
33 P-protein, a bifunctional chorismate mutase/prephenate dehydratase that is feedback inhibited by Phe
34 the biosynthetic enzymes chorismate mutase, prephenate dehydratase, and prephenate dehydrogenase in
35 inotransferase, a bidomain chorismate mutase/prephenate dehydratase, imidazole acetol-phosphate amino
36 oute in which arogenate dehydratase (ADT) or prephenate dehydratase, respectively, plays a key role.
38 mer that exhibits chorismate mutase (CM) and prephenate dehydrogenase (PDH) activities, both of which
39 orismate mutase, prephenate dehydratase, and prephenate dehydrogenase in cell extracts, so the inhibi
40 ved aspartate kinase-chorismate mutase-tyrA (prephenate dehydrogenase) (ACT) domain upstream of the k
41 riments with (18)O-shikimate, a precursor of prephenate, demonstrated the incorporation of (18)O atom
46 r the Claisen rearrangement of chorismate to prephenate has been investigated by application of the c
47 f the Claisen rearrangement of chorismate to prephenate have been examined in water and methanol.
48 r the Claisen rearrangement of chorismate to prephenate in six different environments: water, wild-ty
49 ant PAT enzymes exhibit high activity toward prephenate, indicating that the corresponding genes enco
50 ferase is required for the transamination of prephenate into arogenate, but the identity of the genes
52 with the reactant chorismate or the product prephenate, no water molecule remained near the oxygen o
53 lues of 1140, 490, and 620 M(-1) S(-1), with prephenate not serving as a substrate unless excess reco
54 via the action of either arogenate (ADT) or prephenate (PDT) dehydratases; however, neither enzyme(s
55 that the relative rate of the chorismate --> prephenate reaction is overwhelmingly dependent on the e
56 the important features of the chorismate --> prephenate reaction using molecular dynamics (MD) and th
58 uggest that, along with ADT, a gene encoding prephenate-specific PPA-AT was transferred from a Chloro
61 d that DAH7PS is allosterically inhibited by prephenate, the product of the CM-catalyzed reaction.
62 cilysin antibiotic pathway, BacABGF, convert prephenate to a tetrahydrotyrosine (H(4)Tyr) diastereome
64 dehydratase that catalyzes the conversion of prephenate to phenylpyruvate, the intermediate step betw
65 rous phenolic compounds, is synthesized from prephenate via an arogenate and/or phenylpyruvate route
66 acid anticapsin from the primary metabolite prephenate, we have overproduced, purified, and characte
67 0), more efficiently utilized arogenate than prephenate, whereas the remaining three, ADT3 (At2g27820