ライフサイエンスコーパス: tryptophan synthase

1 to the essential alpha- and beta-subunits of tryptophan synthase.

2 or interpreting the allosteric properties of tryptophan synthase.

3 oenzyme form, the internal aldimine state of tryptophan synthase.

4 is different from the known conformations of tryptophan synthase.

5 bstrate channeling in Salmonella typhimurium tryptophan synthase.

6 and trpA, the genes for the two subunits of tryptophan synthase.

7 unit active site of the PLP-requiring enzyme tryptophan synthase.

8 f the 15N-indole with L-serine, catalyzed by tryptophan synthase.

9 rine sulfhydrylase, threonine deaminase, and tryptophan synthase.

10 ate enzymatic reaction that does not involve tryptophan synthase.

11 reaction is provided by the alpha-subunit of tryptophan synthase, a (beta/alpha)(8) TIM barrel protei

12 ene identified by Kramer and Koziel as maize tryptophan synthase alpha (TSA) is the site of the genet

13 er substrates, L-Ser reacts rapidly with the tryptophan synthase alpha 2 beta 2 bienzyme from Salmone

14 ve been carried out on a mutant (alpha D60N) tryptophan synthase alpha 2 beta 2 complex which has no

15 regulate the activity and specificity of the tryptophan synthase alpha 2 beta 2 complex, we have dete

16 s (0.02-0.08 M) is a cation activator of the tryptophan synthase alpha 2 beta 2 complex.

17 gene, named trp5-2wvc1, and mutations in the tryptophan synthase alpha and beta 1 genes (trp3-1 and t

18 nclude that the maize enzyme initially named tryptophan synthase alpha in fact is a DIMBOA biosynthet

19 f temperature on catalytic properties of the tryptophan synthase alpha(2)beta(2) complex and beta(2)

20 activity and allosteric communication in the tryptophan synthase alpha(2)beta(2) complex from Salmone

21 ctional roles of active-site residues in the tryptophan synthase alpha(2)beta(2) complex from Salmone

22 The mechanism of the tryptophan synthase alpha(2)beta(2) complex from Salmone

23 ctions catalyzed by the beta-subunits of the tryptophan synthase alpha(2)beta(2) complex involve mult

24 unit in allosteric communication between the tryptophan synthase alpha- and beta-subunits.

25 um folding mechanism of the alpha subunit of tryptophan synthase (alpha TS) from Escherichia coli, a

26 We report refined crystal structures of the tryptophan synthase alpha2beta2 complex from Salmonella

27 Our crystallization of the tryptophan synthase alpha2beta2 complex from Salmonella

28 ous x-ray crystallographic structures of the tryptophan synthase alpha2beta2 complex showed an intera

29 uctures are reported for a mutant (betaK87T) tryptophan synthase alpha2beta2 complex with either the

30 t interact in some crystal structures of the tryptophan synthase alpha2beta2 complex, decreases the a

31 that lead to activation of catalysis by the tryptophan synthase alpha2beta2 complex, we have determi

32 NIH) since 1966 has focused on the bacterial tryptophan synthase alpha2beta2 complex.

33 nneling, and allosteric communication in the tryptophan synthase alpha2beta2 complex.

34 The alpha-subunit of tryptophan synthase (alphaTS) catalyzes the conversion o

35 quilibrium unfolding of the alpha-subunit of tryptophan synthase (alphaTS) from Escherichia coli can

36 c folding mechanism for the alpha subunit of tryptophan synthase (alphaTS) from Escherichia coli invo

37 The alpha subunit of tryptophan synthase (alphaTS) from Escherichia coli is a

38 ea-induced unfolding of the alpha subunit of tryptophan synthase (alphaTS) from Escherichia coli, an

39 c folding mechanism for the alpha subunit of tryptophan synthase (alphaTS) from Escherichia coli, inv

40 isoleucine residues in the alpha subunit of tryptophan synthase (alphaTS) from Escherichia coli.

41 characterized models of the alpha subunit of tryptophan synthase (alphaTS) from Escherichia coli.

42 r during the folding of the alpha-subunit of tryptophan synthase (alphaTS) from Escherichia coli.

43 M barrel model based on the alpha-subunit of tryptophan synthase (alphaTS) from Salmonella typhimuriu

44 ic folding mechanism of the alpha-subunit of tryptophan synthase (alphaTS), a TIM barrel protein, dis

45 rrel protein of low sequence identify, alpha-tryptophan synthase (alphaTS), indicates that the thermo

46 S) and the alpha subunit of Escherichia coli tryptophan synthase (alphaTS), reveal striking similarit

47 with the presence or absence of a functional tryptophan synthase and a putative GTPase-inactivating d

48 e pyridoxal phosphate-dependent reactions of tryptophan synthase and affect intersubunit communicatio

49 1-15N-L-Trp was complexed with wild-type tryptophan synthase and beta-subunit mutants, betaK87T,

50 nt active sites have also been identified in tryptophan synthase and glutamine phosphoribosyl pyropho

51 hase with those of related investigations of tryptophan synthase and O-acetylserine sulfhydrylase.

52 f well-constrained fits to published data on tryptophan synthase and the kinetics of oligonucleotide

53 e evidence that GuHCl exerts dual effects on tryptophan synthase as a cation, stimulating activity, a

54 Over-expression studies confirmed tryptophan synthase as the biological target.

55 y different from the expression of the maize tryptophan synthase beta (TSB) genes.

56 the pyridoxal phosphate binding site of the tryptophan synthase beta subunit (S377D and S377E) alter

57 of ACS in fold type I is superimposable over tryptophan synthase beta subunit in fold type II and mou

58 selectable RNAi-induced phenotype (encoding tryptophan synthase beta subunit) and another gene of in

59 C-terminal region (residues 378-397) of the tryptophan synthase beta subunit, we have constructed fo

60 iously identified cation binding site in the tryptophan synthase beta subunit.

61 A small set of mutations of the tryptophan synthase beta-subunit (TrpB) from Pyrococcus

62 reas the absorption spectra of the wild type tryptophan synthase beta2 subunit and alpha2 beta2 compl

63 The tryptophan synthase bienzyme complex (alpha2beta2) from

64 The alpha-subunit of the tryptophan synthase bienzyme complex catalyzes the forma

65 The tryptophan synthase bienzyme complex channels substrate

66 Substrate channeling in the tryptophan synthase bienzyme complex from Salmonella typ

67 te substrate channeling and catalysis in the tryptophan synthase bienzyme complex from Salmonella typ

68 The tryptophan synthase bienzyme complex is activated and re

69 Substrate channeling in the tryptophan synthase bienzyme complex is regulated by all

70 The tryptophan synthase bienzyme complex is the most extensi

71 In the tryptophan synthase bienzyme complex, indole produced by

72 Substrate channeling in the tryptophan synthase bienzyme is regulated by allosteric

73 amino acid networks in the alpha subunit of tryptophan synthase both for the resting state (in the a

74 The three-dimensional structures of tryptophan synthase, carbamoyl phosphate synthetase, glu

75 To further investigate this unusual tryptophan synthase E(A-A) species, these studies examin

76 nzyme systems including the AROM complex and tryptophan synthase, each of which provides new fundamen

77 supporting the conclusion that a functional tryptophan synthase enzyme and toxin might be the princi

78 dominate the folding of the alpha subunit of tryptophan synthase from Escherichia coli (alphaTS).

79 The alpha subunit of tryptophan synthase from Escherichia coli has been previ

80 ic folding mechanism of the alpha-subunit of tryptophan synthase from Escherichia coli.

81 atalytic potential using the beta-subunit of tryptophan synthase from Pyrococcus furiosus (PfTrpB).

82 itution reaction of an engineered subunit of tryptophan synthase from Pyrococcus furiosus, yielding (

83 rmational transition of the beta2 subunit of tryptophan synthase from Salmonella typhimurium has been

84 The monovalent cation (MVC) site of the tryptophan synthase from Salmonella typhimurium plays es

85 sferases FgaPT2 and 7-DMATS (7-dimethylallyl tryptophan synthase) from Aspergillus fumigatus catalyze

86 the utility of this approach by isolating a tryptophan synthase gene (trpB) null mutant that was oth

87 hese genes included three ATPase genes and a tryptophan synthase gene.

88 homatis strains is shown to be linked to the tryptophan synthase genotype.

89 establishes that the reaction of L-Ser with tryptophan synthase gives an H(+) release when the exter

90 of indole-3-glycerol by the alpha-subunit of tryptophan synthase has been proposed to be catalyzed by

91 of the 143-kDa alpha2beta2 tetrameric enzyme tryptophan synthase have been labeled by L-[ring-4-19F]p

92 scovery of anti-tubercular agents inhibiting tryptophan synthase highlights the therapeutic potential

93 One mutant had a missense mutation in tryptophan synthase; however, this mutant behaved differ

94 1-15N-L-Trp in the presence of wild-type tryptophan synthase in the absence or presence of 50 mm

95 Tryptophan synthase is an alpha2beta2 multienzyme comple

96 The tunnel in tryptophan synthase is approximately 25 A in length, whe

97 Tryptophan synthase is the only enzyme that has been con

98 The intense fluorescence emission of the Tryptophan synthase L-Ser external aldimine complex at 4

99 T-jump experiments of the Na(+) form of the tryptophan synthase-L-Ser complex show large changes in

100 imine and aminoacrylate intermediates in the Tryptophan synthase-L-Ser complex.

101 imine and aminoacrylate intermediates in the Tryptophan synthase-L-Ser complex.

102 ction between the alpha and beta subunits of tryptophan synthase leads to mutual stabilization of the

103 kDa pyridoxal-5'-phosphate-dependent enzyme tryptophan synthase, reactions of the alpha-aminoacrylat

104 scopic properties of the L-Ser reaction with tryptophan synthase reflect a mechanism wherein the kine

105 ntrols cofactor chemistry, we have changed a tryptophan synthase residue that interacts with the pyri

106 n equilibrium studies of dilute solutions of tryptophan synthase reveal dissociation from the holoenz

107 to a low-resolution crystal structure of Mtb tryptophan synthase showed they locate to the interface

108 in, avoid this response by the production of tryptophan synthase that rescues them from tryptophan st

109 irst stage (stage I) in the beta-reaction of tryptophan synthase, the reaction of L-serine with pyrid

110 dia trachomatis expresses the genes encoding tryptophan synthase (trpBA) and the tryptophan repressor

111 ith inactivating mutations in the pathogen's tryptophan synthase (trpBA) genes.

112 vestigated the synergistic regulation of the tryptophan synthase (TRPS) complex, studied for decades

113 Tryptophan synthase (TRPS), with linearly arrayed subuni

114 ardtii cDNA that encodes the beta-subunit of tryptophan synthase (TSB).

115 the pyridoxal-5'-phosphate-dependent enzyme tryptophan synthase under conditions of active catalysis

116 ted mechanisms are inspired by dimethylallyl tryptophan synthases, which direct biological electrophi

117 ides, the crystal structures of complexes of tryptophan synthase with a series of phosphonate enzyme