ライフサイエンスコーパス: chorismate mutase

1 o structural homology to the Escherchia coli chorismate mutase.

2 talytic contributions of various residues in chorismate mutase.

3 ld, as first identified in Bacillus subtilis chorismate mutase.

4 the catalysis of chorismate to prephenate by chorismate mutase.

5 pericyclic reaction catalysed by the enzyme chorismate mutase.

6 nce; hence, it belongs to the *AroQ class of chorismate mutases.

7 ochorismate-pyruvate lyase with adventitious chorismate mutase activity from Pseudomonas aerugionsa (

8 s reduced by approximately 60-70%, and total chorismate mutase activity in corolla tissue is reduced

9 developed a novel complementation system for chorismate mutase activity in Escherichia coli by reengi

10 n the absence of Mg2+ MbtI has a promiscuous chorismate mutase activity similar to that of the isocho

11 distinct physiological role in coordinating chorismate mutase activity with developmental and enviro

12 s of this family, combined with the observed chorismate mutase activity, suggests that MbtI may explo

13 emonstrating the eponymous activity and also chorismate mutase activity.

14 e-chain version of a catalytic antibody with chorismate mutase activity.

15 f first generation catalytic antibodies with chorismate mutase activity.

16 Chorismate mutase acts at the first branch-point of arom

17 all three structures are similar to that of chorismate mutase, although there is little sequence hom

18 analogue inhibitor binding to the wild-type chorismate mutase and its Q88E mutant using isothermal t

19 iosynthesis, contains two catalytic domains (chorismate mutase and prephenate dehydratase activities)

20 his finding for the mechanism of all natural chorismate mutases and for the design of artificial cata

21 -binding domain forms an ACT (aspartokinase, chorismate mutase, and TyrA) fold and contains the tetra

22 strate in solution and in the active site of chorismate mutase are reported.

23 In the present study, the DAHPS (aroA) and chorismate mutase (aroQ) activities of B. subtilis DAHPS

24 Three independent Arabidopsis chorismate mutase cDNAs were isolated by functional comp

25 nzyme complex formed by two pathway enzymes: chorismate mutase (CM) and 3-deoxy-d-arabino-heptulosona

26 lanine (Phe) biosynthesis, contains distinct chorismate mutase (CM) and prephenate dehydratase (PDT)

27 acid T-protein is a homodimer that exhibits chorismate mutase (CM) and prephenate dehydrogenase (PDH

28 on of chalcone to flavanone, whereas E. coli chorismate mutase (CM) catalyzes the pericyclic rearrang

29 The rate enhancement provided by the chorismate mutase (CM) enzyme for the Claisen rearrangem

30 RR and in vivo selection to the evolution of chorismate mutase (CM) enzymes.

31 tulosonate-7-phosphate synthase (DAH7PS) and chorismate mutase (CM) from Geobacillus sp.

32 The gene for chorismate mutase (CM) from the archaeon Methanococcus j

33 The catalytic reaction of chorismate mutase (CM) has been the subject of major cur

34 This paradigm has been challenged for chorismate mutase (CM), a well-characterized metabolic e

35 Chorismate mutase converts chorismate into prephenate fo

36 talysis as expected from previously reported chorismate mutase data.

37 d subjected to a growth based selection in a chorismate mutase deficient strain.

38 for its ability to complement an auxotrophic chorismate mutase deletion strain.

39 estigated in six positions of the engineered chorismate mutase domain of the Escherichia coli chorism

40 Chorismate mutase (EC 5.4.99.5) catalyzes the intramolec

41 ) in water and at the active site of E. coli chorismate mutase (EcCM) have been compared.

42 he protein interface of the Escherichia coli chorismate mutase (EcCM) homodimer to be dependent on in

43 lar dynamics studies of the Escherichia coli chorismate mutase (EcCM), containing at the active site

44 A definitive mechanism for the chorismate mutase enzymes is provided.

45 recent finding that an engineered monomeric chorismate mutase exhibits catalytic efficiency similar

46 al of the R-domain decreased the affinity of chorismate mutase for chorismate.

47 of Gln88 to glutamate in the monofunctional chorismate mutase from Escherichia coli results in an en

48 The structure of the complex of the chorismate mutase from the yeast Saccharomyces cerevisia

49 ations catalyzed by evolutionarily unrelated chorismate mutases from Escherichia coli and Bacillus su

50 Comparisons of chorismate mutases from multiple plants suggest that sub

51 isomerization of chorismate to prephenate by chorismate mutase in the biosynthetic pathway that forms

52 that the enzyme is a structural homologue of chorismate mutases in the AroQalpha class despite low se

53 to transform an intimately entwined, dimeric chorismate mutase into a monomeric, four-helix-bundle pr

54 , we analyzed the three Arabidopsis thaliana chorismate mutase isoforms (AtCM1-3) and determined the

55 variants of the AroH class Bacillus subtilis chorismate mutase lacking the otherwise highly conserved

56 H37Rv encodes a monofunctional and secreted chorismate mutase (*MtCM) with a 33-amino-acid cleavable

57 te synthase on the branch leading to Trp and chorismate mutase on the branch leading to Phe and Tyr.

58 system, we have cloned and characterized two CHORISMATE MUTASE (PhCM1 and PhCM2) cDNAs from petunia.

59 bit the activity of the biosynthetic enzymes chorismate mutase, prephenate dehydratase, and prephenat

60 ismate mutase domain of the Escherichia coli chorismate mutase-prephenate dehydratase.

61 e Escherichia coli P-protein, a bifunctional chorismate mutase/prephenate dehydratase that is feedbac

62 3-phosphoserine aminotransferase, a bidomain chorismate mutase/prephenate dehydratase, imidazole acet

63 ate that AS, ADCS, IS, and SS do not possess chorismate mutase promiscuous activity, contrary to seve

64 ese results show that PhCM1 is the principal CHORISMATE MUTASE responsible for the coupling of metabo

65 ilic and mesophilic enzyme Bacillus subtilis chorismate mutase substrate complex (BsCM x S): (i) elec

66 ics (MD) simulations of Thermus thermophilus chorismate mutase substrate complex (TtCM x S) have been

67 range of effector control in the Arabidopsis chorismate mutases than previously reported.

68 nzymatic mechanism suggested for a bacterial chorismate mutase, that the active site is by design cap

69 ssion of Arabidopsis thaliana genes encoding chorismate mutase, the enzyme catalyzing the first commi

70 A study of the Thermus thermophilus chorismate mutase (TtCM) is described by using quantum m

71 of allosteric yeast Saccharomyces cerevisiae chorismate mutase was solved by molecular replacement at

72 basis of allosteric regulation in the plant chorismate mutases, we analyzed the three Arabidopsis th

73 organizing the ground state is compared with chorismate mutase whose catalytic prowess, when compared

74 ctor-regulated allosteric mechanism of yeast chorismate mutase (YCM) was studied by normal mode analy