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1 enases or incorporation of haloindoles using tryptophan synthase.
2 ate enzymatic reaction that does not involve tryptophan synthase.
3 or interpreting the allosteric properties of tryptophan synthase.
4 to the essential alpha- and beta-subunits of tryptophan synthase.
5 unit active site of the PLP-requiring enzyme tryptophan synthase.
6 oenzyme form, the internal aldimine state of tryptophan synthase.
7 is different from the known conformations of tryptophan synthase.
8 bstrate channeling in Salmonella typhimurium tryptophan synthase.
9 and trpA, the genes for the two subunits of tryptophan synthase.
10 f the 15N-indole with L-serine, catalyzed by tryptophan synthase.
11 rine sulfhydrylase, threonine deaminase, and tryptophan synthase.
12 reaction is provided by the alpha-subunit of tryptophan synthase, a (beta/alpha)(8) TIM barrel protei
13 ene identified by Kramer and Koziel as maize tryptophan synthase alpha (TSA) is the site of the genet
14 er substrates, L-Ser reacts rapidly with the tryptophan synthase alpha 2 beta 2 bienzyme from Salmone
15 ve been carried out on a mutant (alpha D60N) tryptophan synthase alpha 2 beta 2 complex which has no
16 regulate the activity and specificity of the tryptophan synthase alpha 2 beta 2 complex, we have dete
18 gene, named trp5-2wvc1, and mutations in the tryptophan synthase alpha and beta 1 genes (trp3-1 and t
19 nclude that the maize enzyme initially named tryptophan synthase alpha in fact is a DIMBOA biosynthet
20 aize enzymes (BX1, benzoxazinoneless 1; TSA, tryptophan synthase alpha subunit; and IGL, indole glyce
21 f temperature on catalytic properties of the tryptophan synthase alpha(2)beta(2) complex and beta(2)
22 activity and allosteric communication in the tryptophan synthase alpha(2)beta(2) complex from Salmone
23 ctional roles of active-site residues in the tryptophan synthase alpha(2)beta(2) complex from Salmone
25 ctions catalyzed by the beta-subunits of the tryptophan synthase alpha(2)beta(2) complex involve mult
27 egrated approach is used to characterize the tryptophan synthase alpha-aminoacrylate intermediate, a
28 um folding mechanism of the alpha subunit of tryptophan synthase (alpha TS) from Escherichia coli, a
29 We report refined crystal structures of the tryptophan synthase alpha2beta2 complex from Salmonella
31 ous x-ray crystallographic structures of the tryptophan synthase alpha2beta2 complex showed an intera
32 uctures are reported for a mutant (betaK87T) tryptophan synthase alpha2beta2 complex with either the
33 t interact in some crystal structures of the tryptophan synthase alpha2beta2 complex, decreases the a
34 that lead to activation of catalysis by the tryptophan synthase alpha2beta2 complex, we have determi
38 quilibrium unfolding of the alpha-subunit of tryptophan synthase (alphaTS) from Escherichia coli can
39 c folding mechanism for the alpha subunit of tryptophan synthase (alphaTS) from Escherichia coli invo
41 ea-induced unfolding of the alpha subunit of tryptophan synthase (alphaTS) from Escherichia coli, an
42 c folding mechanism for the alpha subunit of tryptophan synthase (alphaTS) from Escherichia coli, inv
44 characterized models of the alpha subunit of tryptophan synthase (alphaTS) from Escherichia coli.
45 r during the folding of the alpha-subunit of tryptophan synthase (alphaTS) from Escherichia coli.
46 M barrel model based on the alpha-subunit of tryptophan synthase (alphaTS) from Salmonella typhimuriu
47 ic folding mechanism of the alpha-subunit of tryptophan synthase (alphaTS), a TIM barrel protein, dis
48 rrel protein of low sequence identify, alpha-tryptophan synthase (alphaTS), indicates that the thermo
49 S) and the alpha subunit of Escherichia coli tryptophan synthase (alphaTS), reveal striking similarit
50 C-C coupling using engineered PLP-dependent tryptophan synthases, an enzyme-controlled unusual alpha
51 with the presence or absence of a functional tryptophan synthase and a putative GTPase-inactivating d
52 e pyridoxal phosphate-dependent reactions of tryptophan synthase and affect intersubunit communicatio
54 nt active sites have also been identified in tryptophan synthase and glutamine phosphoribosyl pyropho
55 hase with those of related investigations of tryptophan synthase and O-acetylserine sulfhydrylase.
56 lk assay has also been applied to the enzyme tryptophan synthase and reveals a dramatically different
57 f well-constrained fits to published data on tryptophan synthase and the kinetics of oligonucleotide
58 is that only the former express a functional tryptophan synthase and therefore can synthesize tryptop
59 e evidence that GuHCl exerts dual effects on tryptophan synthase as a cation, stimulating activity, a
62 the pyridoxal phosphate binding site of the tryptophan synthase beta subunit (S377D and S377E) alter
63 of ACS in fold type I is superimposable over tryptophan synthase beta subunit in fold type II and mou
64 selectable RNAi-induced phenotype (encoding tryptophan synthase beta subunit) and another gene of in
65 C-terminal region (residues 378-397) of the tryptophan synthase beta subunit, we have constructed fo
67 p, we rapidly evolve the Thermotoga maritima tryptophan synthase beta-subunit (TmTrpB) through multi-
69 reas the absorption spectra of the wild type tryptophan synthase beta2 subunit and alpha2 beta2 compl
74 te substrate channeling and catalysis in the tryptophan synthase bienzyme complex from Salmonella typ
80 amino acid networks in the alpha subunit of tryptophan synthase both for the resting state (in the a
83 vironment, because in the absence of indole, tryptophan synthase deaminates serine to pyruvate and am
85 nzyme systems including the AROM complex and tryptophan synthase, each of which provides new fundamen
86 supporting the conclusion that a functional tryptophan synthase enzyme and toxin might be the princi
87 rapidly induce expression of C. trachomatis tryptophan synthase, even under conditions of tryptophan
88 dominate the folding of the alpha subunit of tryptophan synthase from Escherichia coli (alphaTS).
91 atalytic potential using the beta-subunit of tryptophan synthase from Pyrococcus furiosus (PfTrpB).
92 itution reaction of an engineered subunit of tryptophan synthase from Pyrococcus furiosus, yielding (
93 rmational transition of the beta2 subunit of tryptophan synthase from Salmonella typhimurium has been
95 sferases FgaPT2 and 7-DMATS (7-dimethylallyl tryptophan synthase) from Aspergillus fumigatus catalyze
96 the utility of this approach by isolating a tryptophan synthase gene (trpB) null mutant that was oth
99 establishes that the reaction of L-Ser with tryptophan synthase gives an H(+) release when the exter
100 of indole-3-glycerol by the alpha-subunit of tryptophan synthase has been proposed to be catalyzed by
101 of the 143-kDa alpha2beta2 tetrameric enzyme tryptophan synthase have been labeled by L-[ring-4-19F]p
102 scovery of anti-tubercular agents inhibiting tryptophan synthase highlights the therapeutic potential
104 1-15N-L-Trp in the presence of wild-type tryptophan synthase in the absence or presence of 50 mm
105 indole due to inactivating mutations within tryptophan synthase, indicating a selection against main
108 to demonstrate that expression of wild-type tryptophan synthase is required for the bactericidal pro
110 The intense fluorescence emission of the Tryptophan synthase L-Ser external aldimine complex at 4
111 T-jump experiments of the Na(+) form of the tryptophan synthase-L-Ser complex show large changes in
114 ction between the alpha and beta subunits of tryptophan synthase leads to mutual stabilization of the
115 kDa pyridoxal-5'-phosphate-dependent enzyme tryptophan synthase, reactions of the alpha-aminoacrylat
116 scopic properties of the L-Ser reaction with tryptophan synthase reflect a mechanism wherein the kine
117 ntrols cofactor chemistry, we have changed a tryptophan synthase residue that interacts with the pyri
118 n equilibrium studies of dilute solutions of tryptophan synthase reveal dissociation from the holoenz
119 to a low-resolution crystal structure of Mtb tryptophan synthase showed they locate to the interface
120 in, avoid this response by the production of tryptophan synthase that rescues them from tryptophan st
121 irst stage (stage I) in the beta-reaction of tryptophan synthase, the reaction of L-serine with pyrid
123 e reaction of a thermostable beta-subunit of tryptophan synthase (TrpB) in a nonnative environment yi
124 We previously engineered the beta-subunit of tryptophan synthase (TrpB), which catalyzes the condensa
125 ed evolution to engineer the beta-subunit of tryptophan synthase, TrpB, for improved activity with di
126 dia trachomatis expresses the genes encoding tryptophan synthase (trpBA) and the tryptophan repressor
128 vestigated the synergistic regulation of the tryptophan synthase (TRPS) complex, studied for decades
133 the pyridoxal-5'-phosphate-dependent enzyme tryptophan synthase under conditions of active catalysis
134 ted mechanisms are inspired by dimethylallyl tryptophan synthases, which direct biological electrophi
135 is by demonstrating that the beta-subunit of tryptophan synthase-which natively couples indole and L-
136 ides, the crystal structures of complexes of tryptophan synthase with a series of phosphonate enzyme