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Information on EC 4.2.1.20 - tryptophan synthase and Organism(s) Escherichia coli and UniProt Accession P0A877

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EC Tree
     4 Lyases
         4.2 Carbon-oxygen lyases
             4.2.1 Hydro-lyases
                4.2.1.20 tryptophan synthase
IUBMB Comments
A pyridoxal-phosphate protein. The alpha-subunit catalyses the conversion of 1-C-(indol-3-yl)glycerol 3-phosphate to indole and D-glyceraldehyde 3-phosphate (this reaction was included formerly under EC 4.1.2.8). The indole migrates to the beta-subunit where, in the presence of pyridoxal 5'-phosphate, it is combined with L-serine to form L-tryptophan. In some organisms this enzyme is part of a multifunctional protein that also includes one or more of the enzymes EC 2.4.2.18 (anthranilate phosphoribosyltransferase), EC 4.1.1.48 (indole-3-glycerol-phosphate synthase), EC 4.1.3.27 (anthranilate synthase) and EC 5.3.1.24 (phosphoribosylanthranilate isomerase). In thermophilic organisms, where the high temperature enhances diffusion and causes the loss of indole, a protein similar to the beta subunit can be found (EC 4.2.1.122). That enzyme cannot combine with the alpha unit of EC 4.2.1.20 to form a complex.
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Escherichia coli
UNIPROT: P0A877
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The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
trps, tryptophan synthase, tryptophan synthetase, tsase, alphats, trpb2, tryptophan synthase beta, trp synthase, trpb1, beta subunit of tryptophan synthase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
alphaTS
indoleglycerol phosphate aldolase
-
-
-
-
L-tryptophan synthetase
-
-
-
-
synthase, tryptophan
-
-
-
-
tryptophan desmolase
-
-
-
-
tryptophan synthase
tryptophan synthetase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate = L-tryptophan + D-glyceraldehyde 3-phosphate + H2O
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
addition
-
-
-
-
C-O bond cleavage
-
-
SYSTEMATIC NAME
IUBMB Comments
L-serine hydro-lyase [adding 1-C-(indol-3-yl)glycerol 3-phosphate; L-tryptophan and glyceraldehyde-3-phosphate-forming]
A pyridoxal-phosphate protein. The alpha-subunit catalyses the conversion of 1-C-(indol-3-yl)glycerol 3-phosphate to indole and D-glyceraldehyde 3-phosphate (this reaction was included formerly under EC 4.1.2.8). The indole migrates to the beta-subunit where, in the presence of pyridoxal 5'-phosphate, it is combined with L-serine to form L-tryptophan. In some organisms this enzyme is part of a multifunctional protein that also includes one or more of the enzymes EC 2.4.2.18 (anthranilate phosphoribosyltransferase), EC 4.1.1.48 (indole-3-glycerol-phosphate synthase), EC 4.1.3.27 (anthranilate synthase) and EC 5.3.1.24 (phosphoribosylanthranilate isomerase). In thermophilic organisms, where the high temperature enhances diffusion and causes the loss of indole, a protein similar to the beta subunit can be found (EC 4.2.1.122). That enzyme cannot combine with the alpha unit of EC 4.2.1.20 to form a complex.
CAS REGISTRY NUMBER
COMMENTARY hide
9014-52-2
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
D-glyceraldehyde 3-phosphate + indole
1-(indol-3-yl)glycerol 3-phosphate
show the reaction diagram
-
-
-
?
L-serine + indole
L-tryptophan + H2O
show the reaction diagram
-
-
-
?
1-(indol-3-yl)glycerol 3-phosphate
D-glyceraldehyde 3-phosphate + indole
show the reaction diagram
1-(indol-3-yl)glycerol 3-phosphate + L-serine
L-tryptophan + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
?
1-(indol-3-yl)glycerol 3-phosphate + L-serine
L-tryptophan + D-glyceraldehyde 3-phosphate + H2O
show the reaction diagram
2-amino-3-butenoic acid
2-oxobutyric acid + NH3
show the reaction diagram
-
vinylglycine
-
?
2-mercaptoethanol + L-serine + pyridoxal phosphate
S-pyruvylmercaptoethanol + pyridoxamine phosphate + H2O
show the reaction diagram
-
-
-
?
indole + D-glyceraldehyde 3-phosphate
indole-3-glycerol phosphate
show the reaction diagram
-
r
r
?
indole + L-serine
L-tryptophan + H2O
show the reaction diagram
indole-3-glycerol phosphate
indole + D-glyceraldehyde 3-phosphate
show the reaction diagram
L-serine
pyruvate + NH3
show the reaction diagram
L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate
L-tryptophan + D-glyceraldehyde 3-phosphate + H2O
show the reaction diagram
-
the tryptophan synthase alpha2beta2 bi-enzyme complex catalyzes the last two steps in the synthesis of L-tryptophan (L-Trp). The alpha-subunit catalyzes cleavage of 3-indole-D-glycerol 3'-phosphate to give indole and D-glyceraldehyde 3'-phosphate. Indole is then transferred from the alpha-subunit to the beta-subunit where it reacts with L-Ser in a pyridoxal 5'-phosphate-dependent reaction to give L-Trp and a water molecule
-
-
?
L-serine + 2-methylindole
L-2-methyltryptophan + H2O
show the reaction diagram
-
-
-
-
?
L-serine + indole
L-tryptophan + H2O
show the reaction diagram
L-serine + thiophenol
(S)-phenyl-L-cysteine + H2O
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate
L-tryptophan + D-glyceraldehyde 3-phosphate + H2O
show the reaction diagram
-
the tryptophan synthase alpha2beta2 bi-enzyme complex catalyzes the last two steps in the synthesis of L-tryptophan (L-Trp). The alpha-subunit catalyzes cleavage of 3-indole-D-glycerol 3'-phosphate to give indole and D-glyceraldehyde 3'-phosphate. Indole is then transferred from the alpha-subunit to the beta-subunit where it reacts with L-Ser in a pyridoxal 5'-phosphate-dependent reaction to give L-Trp and a water molecule
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
-
pyridoxal 5'-phosphate
additional information
-
the alpha-subunit contains no prosthetic group
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
the enzyme shows high tolerance to ammonium chloride from hair acid hydrolysis industries waste water, and shows no inhibition by ammonium chloride up to 75 mg/ml
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
6-azido-L-tryptophan
-
-
indolebutanol phosphate
-
competitive in the catalysis of indoleglycerol phosphate cleavage, Ki: 0.0011 mM
indoleethanol phosphate
-
competitive in the catalysis of indoleglycerol phosphate cleavage, Ki: 0.05 mM
indolepropanol phosphate
-
competitive in the catalysis of indoleglycerol phosphate cleavage, Ki: 0.004 mM
trans-L-2-amino-4-methoxy-3-butenoic acid
-
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Triton X-100
-
Trion X-100 leads to the emergence of the highest relative activity at 0.02% (v/v)
Tween-80
-
activates at 0.04%
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.78 - 3.35
indole
0.018 - 0.019
indole
additional information
additional information
-
dissociation constants of the beta-subunit combined with the different subunits of wild-type and mutants
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.003 - 0.095
indole
0.16 - 0.34
indole
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00176 - 0.103
indole
8 - 19
indole
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0011
indolebutanol phosphate
-
competitive in the catalysis of indoleglycerol phosphate cleavage
0.05
indoleethanol phosphate
-
competitive in the catalysis of indoleglycerol phosphate cleavage
0.004
indolepropanol phosphate
-
competitive in the catalysis of indoleglycerol phosphate cleavage
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
125
-
indole-3-glycerol phosphate + L-serine
1524
-
wild-type enzyme in presence of alpha-subunit
275
-
indole + L-Ser
85
-
indole + L-Ser
additional information
-
activity of the beta-subunit combined with the different alpha-subunit monomers and dimers of wild-type and mutants
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.8
-
assay at
8
-
recombinant enzyme
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
29000
-
1 * 29000, alpha-subunit, SDS-PAGE
additional information
-
determination of Stoke's radii of native, stable intermediates and unfolded conformers of the purified recombinant alpha-subunit dependent on urea concentrations
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
heterotetramer
-
-
homodimer
crystal structure
monomer
-
1 * 29000, alpha-subunit, SDS-PAGE
tetramer
additional information
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structures of wild-type and mutant P38L/Y173F alpha-subunit, 2.8 A and 1.8 A resolution, hanging-drop vapour diffusion method
hanging drop vapour diffusion method. Crystal structure of the tryptophan synthase alpha-subunit determined at 2.3 A resolution. Structure of tryptophan synthase alpha-subunit from Escherichia coli is compared to structure of alpha2beta2 complex from Salmonella typhimurium
10 mg/ml purified recombinant alpha-subunit, hanging drop vapour diffusion method, 298K, equal volume, 0.001 ml, of protein solution and reservoir solution are mixed and placed over 0.5 ml reservoir solution, precipitant solution: 0.5 M ammonium sulfate, 0.1 M trisodium citrate dihydrate, 1.0 M lithium sulfate monohydrate, pH 5.6, first crystals after 7-10 days, maximal size within 2 weeks, X-ray diffraction structure determination and analysis at 2.8 A resolution
-
crystal structures of apo-beta2 and holo-beta2 from Escherichia coli is determined at 3.0 and 2.9 A resolutions. The apo-type and holo-type molecule retain a dimeric form in solution. The subunit structures of both the apo-beta2 and the holo-beta2 forms consist of two domains, (N domain, C domain). The pyridoxal 5’-phosphate-bound holo-form has multiple interactions between the two domains and a long loop (residues 260-310), which are missing in the apo-form
wild-type and P28L/Y173F double mutant alpha-subunits are crystallized at 25°C by the hanging-drop vapor-diffusion method. X-ray diffraction data are collected to 2.5 A resolution from the wild-type crystals and to 1.8 A from the crystals of the double mutant. The wild-type crystals belonged to the monoclinic space group C2 (a = 155.64 A, b = 44.54 A, c = 71.53 A and beta = 96.39°) and the P28L/Y173F crystals to the monoclinic space group P 2(1) (a = 71.09 A, b = 52.70 A, c = 71.52 A, and beta = 91.49°). The asymmetric unit of both structures contains two molecules of tryptophan synthase alpha-subunit
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A71G
mutation in alpha-subunit, about 10fold decrease in kcat/Km value compared to wild-type alpha subunit
I37A
mutant lacks the hundreds of milliseconds unfolding reaction under strongly refolding conditions
I41A
mutant lacks the hundreds of milliseconds unfolding reaction under strongly refolding conditions
I95A
mutant lacks the hundreds of milliseconds unfolding reaction under strongly refolding conditions
I97A
mutant lacks the hundreds of milliseconds unfolding reaction under strongly refolding conditions
L25A
mutant lacks the hundreds of milliseconds unfolding reaction under strongly refolding conditions
L48A
mutant lacks the hundreds of milliseconds unfolding reaction under strongly refolding conditions
L50A
mutant lacks the hundreds of milliseconds unfolding reaction under strongly refolding conditions
L85A
mutant lacks the hundreds of milliseconds unfolding reaction under strongly refolding conditions
L99A
mutant lacks the hundreds of milliseconds unfolding reaction under strongly refolding conditions
P38L/Y173F
P28L substitution induces the exposure of hydrophobic amino acids and decreases the secondary structure that causes the aggregation. The Y173E mutation suppresses to transfer a signal from the alpha-subunit core to the alpha-subunit surface involved in interactions with the beta-subunit and increases structural stability
T183V
substitution decreases catalytic efficiency of the alpha-subunit in the absence of the beta subunit, leading to local changes in the structural dynamics of the beta2alpha2 and beta6alpha6 loops
T183V/A158G
mutation in alpha-subunit, about 12fold decrease in kcat/Km value compared to wild-type alpha subunit
T183V/A180G
mutation in alpha-subunit, about 20fold decrease in kcat/Km value compared to wild-type alpha subunit
T183V/A185G
mutation in alpha-subunit, about 12fold decrease in kcat/Km value compared to wild-type alpha subunit
T183V/A59G
mutation in alpha-subunit, about 50fold decrease in kcat/Km value compared to wild-type alpha subunit
T183V/A67G
mutation in alpha-subunit, about 30fold decrease in kcat/Km value compared to wild-type alpha subunit
T183V/A71G
mutation in alpha-subunit, about 8fold decrease in kcat/Km value compared to wild-type alpha subunit
V23A
mutant lacks the hundreds of milliseconds unfolding reaction under strongly refolding conditions
C170F
-
beta subunit, indole is channelled from the alpha site to the beta site in the physiologically relevant alphabeta reaction
D305A
-
mutation of a beta-subunit residue, no active site residue, altered subunit interaction
E109D
-
mutation of a beta-subunit active site residue, reduced reach and conformational freedom of the carboxylate functionality, accumulation of indole at the beta-site
E49X
-
effect of amino acid substitution at E49 of alpha-subunit on stability
F139W
F258W
F280A
-
beta-subunit dimers, unaltered activity compared to the wild-type enzyme
F280G
-
beta-subunit dimers, 72% reduced activity compared to the wild-type enzyme
F280P
-
beta-subunit dimers, 94% reduced activity compared to the wild-type enzyme
G281A
-
beta-subunit dimers, 46% reduced activity compared to the wild-type enzyme
G281R
H273A
-
beta-subunit dimers, 2fold increased activity compared to the wild-type enzyme
I278A
-
beta-subunit dimers, 70% reduced activity compared to the wild-type enzyme
I278A/K283A
-
beta-subunit dimers, 92% reduced activity compared to the wild-type enzyme
I278V
-
beta-subunit dimers, 7% reduced activity compared to the wild-type enzyme
I278V/K283A
-
beta-subunit dimers, 35% reduced activity compared to the wild-type enzyme
K283A
-
beta-subunit dimers, 41% reduced activity compared to the wild-type enzyme
K87T
-
mutation of a beta-subunit active site residue, inactive mutant, which can form an external aldimine, but cannot form an alpha-aminoacrylate intermediate
M149T/N171D
2fold increase in catalytic efficiency
M282A
-
beta-subunit dimers, 61% reduced activity compared to the wild-type enzyme
M282P
-
beta-subunit dimers, inactive mutant
P132A
-
increase of activity of the alpha2beta2 complex
P132G
-
increase of activity of the alpha2beta2 complex
P28L/Y173F
-
wild-type crystals belonged to the monoclinic space group C2 (a = 155.64 A, b = 44.54 A, c =71.53 A and beta = 96.39°) and the P28L/Y173F crystals to the monoclinic space group P 2(1) (a = 71.09 A, b = 52.70 A, c = 71.52 A, and beta = 91.49°). The asymmetric unit of both structures contains two molecules of tryptophan synthase alpha-subunit
P57A
-
increase of activity of the alpha2beta2 complex
R275A
-
beta-subunit dimers, 37% reduced activity compared to the wild-type enzyme
T24A/F139W
-
oligonucleotide-directed mutagenesis, recombinant alpha-subunit mutant, forms dimers
T24K/F139W
-
oligonucleotide-directed mutagenesis, recombinant alpha-subunit mutant, forms dimers
T24L/F139W
-
oligonucleotide-directed mutagenesis, recombinant alpha-subunit mutant, forms monomers
T24M/F139W
-
oligonucleotide-directed mutagenesis, recombinant alpha-subunit mutant, forms monomers
T24S/F139W
-
oligonucleotide-directed mutagenesis, recombinant alpha-subunit mutant, forms dimers
V276A
-
beta-subunit dimers, 46% reduced activity compared to the wild-type enzyme
V276A/K283A
-
beta-subunit dimers, 48% reduced activity compared to the wild-type enzyme
Y173F
-
oligonucleotide-directed mutagenesis, gene trpA, alpha-subunit residue exchange, altered fluorescence and folding properties
Y175F
-
oligonucleotide-directed mutagenesis, gene trpA, alpha-subunit residue exchange, altered fluorescence and folding properties
Y279A
-
beta-subunit dimers, 50% reduced activity compared to the wild-type enzyme
Y279F
-
beta-subunit dimers, 33% reduced activity compared to the wild-type enzyme
Y279L
-
beta-subunit dimers, 48% reduced activity compared to the wild-type enzyme
Y279P
-
beta-subunit dimers, 46% reduced activity compared to the wild-type enzyme
additional information
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
30 min, 20% loss of activity
additional information
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
pyridoxal 5'-phosphate strongly stabilizes beta2 subunit
-
urea-induced equilibrium unfolding reaction
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
0°C, in cellulose triacetate, 6 months
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
alpha subunit
-
alpha2beta2 holoenzyme, beta2 holoenzyme, beta2 apoenzyme, alpha subunit
-
beta2 subunit
-
recombinant alpha-subunit
-
recombinant alpha-subunit and N-terminal part of the alpha-subunit of the enzyme, to over 95% purity
-
recombinant alpha-subunits of wild-type and mutant enzymes
-
soluble and refolded, solubilized recombinant alpha-subunit from expression in strain BL21(DE3)
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
alpha-subunit
-
DNA and amino acid sequence determination of the alpha-subunit of the enzyme, overexpression of the alpha-subunit and the larger N-terminal part of the alpha-subunit, amino acid residues 1-188, in inclusion bodies
-
expressed in Escherichia coli BL21(DE3) cells
-
expression in Escherichia coli
-
expression in Escherichia coli strain BL21(DE3)
-
expression of the alpha-subunit in strain BL21(DE3) as soluble and insoluble protein
-
expression of wild-type and mutant F139W, T24M/F139W, and T24L/F139W alpha-subunits as monomers, expression of mutant T24A/F139W, T24S/F139W and T24K/F139W alpha-subunits as soluble dimers in strain RB797
-
overexpression of the alpha-subunit in strain RB797
-
wild-type and P28L/Y173F double mutant alpha-subunits are overexpressed in Escherichia coli
-
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
cooperative unfolding and 2-phase refolding mechanism and kinetics of the alpha-subunit and the N-terminas of the alpha-subunit alone, denaturing by urea at 25°C
-
denaturation of recombinant wild-type and mutant alpha-subunit monomers and dimers with urea, refolding of all forms as monomers
-
effect of ficoll-70 on the alpha subunit of tryptophan synthase. Crowding by ficoll perturbs the native state and the partially folded state of the subunit. Ficoll interacts with the residues that constitute the stable core of the protein
-
insoluble rcombinant alpha-subunit, expressed in strain BL212(DE3), is denatured by 6 M urea, refolding
-
the refolding of urea-denatured alpha-subunit of tryptophan synthase from Escherichia coli is monitored by pulse-quench hydrogen exchange mass spectrometry. An intermediate builds up rapidly and decays slowly over the first 100 seconds of folding, obligatory nature of the intermediate, the latter stages of the folding reaction of alpha-subunit of tryptophan synthase are under thermodynamic control
-
unfolding and refolding of wild-type and mutant alpha-subunits using urea, comparison of the folding process differences, thermodynamic parameters
-
urea-induced equilibrium unfolding reaction
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Crawford, I.P.; Niermann, T.; Kirschner, K.
Prediction of secondary structure by evolutionary comparison: application to the alpha-subunit of tryptophan synthase
Proteins Struct. Funct. Genet.
2
118-129
1987
Klebsiella aerogenes, Bacillus subtilis, Corynebacterium glutamicum, Saccharomyces cerevisiae, Caulobacter vibrioides, Escherichia coli, Lacticaseibacillus casei, Neurospora crassa, Proteus mirabilis, Pseudomonas aeruginosa, Salmonella enterica subsp. enterica serovar Typhimurium, Serratia marcescens, Vibrio parahaemolyticus
Manually annotated by BRENDA team
Miles, E.W.; Bauerle, R.; Ahmed S.A.
Tryptophan synthase from Escherichia coli and Salmonella thyphimurium
Methods Enzymol.
142
398-414
1987
Escherichia coli, Salmonella enterica subsp. enterica serovar Typhimurium
Manually annotated by BRENDA team
Yutani, K.; Ogasahara, K.; Tsujita, T.; Sugino, Y.
Dependence of conformational stability on hydrophobicity of the amino acid residue in a series of variant proteins substituted at a unique position of tryptophan synthase alpha subunit
Proc. Natl. Acad. Sci. USA
84
4441-4444
1987
Escherichia coli
Manually annotated by BRENDA team
Milton, D.L.; Napier, M.L.; Myers, R.M.; Hardman, J.K.
In vitro mutagensis and overexpression of the Escherichia coli trpA gene and the partial characterization of the resultant tryptophan synthase mutant alpha-subunits
J. Biol. Chem.
261
16604-16615
1986
Escherichia coli
Manually annotated by BRENDA team
Drewe, W.F.; Dunn, M.F.
Characterization of the reaction of L-serine and indole with Escherichia coli tryptophan synthase via rapid-scanning ultraviolet-visible spectroscopy
Biochemistry
25
2494-2501
1986
Escherichia coli
Manually annotated by BRENDA team
Shannon, L.M.; Mills, S.E.
Purification and immunoadsorbtion chromatography of the normal and a mutant form of the B2 subunit of Escherichia coli tryptophan synthase
Eur. J. Biochem.
63
563-568
1976
Escherichia coli
Manually annotated by BRENDA team
Kirschner, K.; Wiskocil, R.L.; Foehn, M.; Rezeau, L.
The tryptophan synthase from Escherichia coli. An improved purification procedure for the alpha-subunit and binding studies with substrate analogues
Eur. J. Biochem.
60
513-523
1975
Escherichia coli
Manually annotated by BRENDA team
Zaffaroni, P.; Vitobello, V.; Cecere, F.; Giacomozzi, E.; Morisi, F.
Synthesis of L-tryptophan from indole and DL-serine by tryptophan synthetase entrapped in fibres 1. Preparation and properties of free and entrapped enzyme
Agric. Biol. Chem.
38
1335-1342
1974
Escherichia coli
-
Manually annotated by BRENDA team
Miles, E.W.
Tryptophan synthase, structure, function, and protein engineering
Subcell. Biochem.
24
207-254
1995
Escherichia coli, Salmonella enterica subsp. enterica serovar Typhimurium
Manually annotated by BRENDA team
Lane, A.N.; Paul, C.H.; Kirschner, K.
The mechanism of self-assembly of the multi-enzyme complex tryptophan synthase from Escherichia coli
EMBO J.
3
279-287
1984
Escherichia coli
Manually annotated by BRENDA team
Ahmed, S.A.; McPhie, P.; Miles, E.W.
A thermally induced reversible conformational transition of the tryptophan synthase beta2 subunit probed by the spectroscopic properties of pyridoxal phosphate and by enzymatic activity
J. Biol. Chem.
271
8612-8617
1996
Escherichia coli
Manually annotated by BRENDA team
Choi, S.G.; O'Donnell, S.E.; Sarken, K.D.; Hardmann, J.K.
Tryptophan-containing alpha-subunits of the Escherichia coli tryptophan synthase. Enzymatic and urea stability properties
J. Biol. Chem.
270
17712-17715
1995
Escherichia coli
Manually annotated by BRENDA team
Choi, S.G.; Hardmann, J.K.
Unfolding properties of tryptophan-containing alpha-subunits of the Escherichia coli tryptophan synthase
J. Biol. Chem.
270
28177-28182
1995
Escherichia coli
Manually annotated by BRENDA team
Anderson, K.S.; Kim, A.Y.; Quillen, J.M.; Sayers, E.; Yang, X.J.; Miles, E.W.
Kinetic characterization of channel impaired mutants of tryptophan synthase
J. Biol. Chem.
270
29936-29944
1995
Escherichia coli
Manually annotated by BRENDA team
Zhao, G.P.; Somerville, R.L.
Genetic and biochemical characterization of the trpB8 mutation of Escherichia coli tryptophan synthase. An amino acid switch at the sharp turn of the trypsin-sensitive hinge region diminishes substrate binding and alters solubility
J. Biol. Chem.
267
526-541
1992
Escherichia coli
Manually annotated by BRENDA team
Ki Lim, W.; Sarkar, S.K.; Hardman, J.K.
Enzymatic properties of mutant Escherichia coli tryptophan synthase alpha-subunits
J. Biol. Chem.
266
20205-20212
1991
Escherichia coli
Manually annotated by BRENDA team
Blond-Elguindi, S.; Goldberg, M.E.
Kinetic characterization of early immunoreactive intermediates during the refolding of guanidine-unfolded Escherichia coli tryptophan synthase beta2 subunits
Biochemistry
29
2409-2417
1990
Escherichia coli
Manually annotated by BRENDA team
Jeong, M.S.; Jeong, J.K.; Park, K.S.; Kim, H.T.; Lee, K.M.; Lim, W.K.; Jang, S.B.
Crystallization and preliminary X-ray analysis of tryptophan synthase alpha-subunits from Escherichia coli
Acta Crystallogr. Sect. D
60
132-134
2004
Escherichia coli
Manually annotated by BRENDA team
Kim, J.W.; Kim, E.Y.; Park, H.H.; Jung, J.E.; Kim, H.D.; Shin, H.J.; Lim, W.K.
Homodimers of mutant tryptophan synthase alpha-subunits in Escherichia coli
Biochem. Biophys. Res. Commun.
289
568-572
2001
Escherichia coli
Manually annotated by BRENDA team
Jeong, J.K.; Shin, H.J.; Kim, J.W.; Lee, C.H.; Kim, H.D.; Lim, W.K.
Fluorescence and folding properties of Tyr mutant tryptophan synthase alpha-subunits from Escherichia coli
Biochem. Biophys. Res. Commun.
300
29-35
2003
Escherichia coli
Manually annotated by BRENDA team
Zitzewitz, J.A.; Matthews, C.R.
Molecular dissection of the folding mechanism of the alpha subunit of tryptophan synthase: an amino-terminal autonomous folding unit controls several rate-limiting steps in the folding of a single domain protein
Biochemistry
38
10205-10214
1999
Escherichia coli
Manually annotated by BRENDA team
Gualfetti, P.J.; Iwakura, M.; Lee, J.C.; Kihara, H.; Bilsel, O.; Zitzewitz, J.A.; Matthews, C.R.
Apparent radii of the native, stable intermediates and unfolded conformers of the alpha-subunit of tryptophan synthase from E. coli, a TIM barrel protein
Biochemistry
38
13367-13378
1999
Escherichia coli
Manually annotated by BRENDA team
Rondard, P.; Bedouelle, H.
Mutational scanning of a hairpin loop in the tryptophan synthase beta-subunit implicated in allostery and substrate channeling
Biol. Chem.
381
1185-1193
2000
Escherichia coli, Salmonella enterica subsp. enterica serovar Typhimurium
Manually annotated by BRENDA team
Osborne, A.; Teng, Q.; Miles, E.W.; Phillips, R.S.
Detection of Open and Closed Conformations of Tryptophan Synthase by 15N-Heteronuclear Single-Quantum Coherence Nuclear Magnetic Resonance of Bound 1-15N-L-Tryptophan
J. Biol. Chem.
278
44083-44090
2003
Escherichia coli
Manually annotated by BRENDA team
Vadrevu, R.; Falzone, C.J.; Matthews, C.R.
Partial NMR assignments and secondary structure mapping of the isolated alpha subunit of Escherichia coli tryptophan synthase, a 29-kD TIM barrel protein
Protein Sci.
12
185-191
2003
Escherichia coli
Manually annotated by BRENDA team
Bang, W.; Lang, S.; Sahm, H.; Wagner, F.
Production of L-tryptophan by Escherichia coli cells
Biotechnol. Bioeng.
25
999-1011
1983
Escherichia coli
Manually annotated by BRENDA team
Jeong, M.S.; Jeong, J.K.; Lim, W.K.; Jang, S.B.
Structures of wild-type and P28L/Y173F tryptophan synthase alpha-subunits from Escherichia coli
Biochem. Biophys. Res. Commun.
323
1257-1264
2004
Escherichia coli (P0A877), Escherichia coli
Manually annotated by BRENDA team
Nishio, K.; Morimoto, Y.; Ishizuka, M.; Ogasahara, K.; Tsukihara, T.; Yutani, K.
Conformational changes in the alpha-subunit coupled to binding of the beta 2-subunit of tryptophan synthase from Escherichia coli: crystal structure of the tryptophan synthase alpha-subunit alone
Biochemistry
44
1184-1192
2005
Escherichia coli (P0A877), Escherichia coli
Manually annotated by BRENDA team
Wintrode, P.L.; Rojsajjakul, T.; Vadrevu, R.; Matthews, C.R.; Smith, D.L.
An obligatory intermediate controls the folding of the alpha-subunit of tryptophan synthase, a TIM barrel protein
J. Mol. Biol.
347
911-919
2005
Escherichia coli
Manually annotated by BRENDA team
Wu, Y.; Vadrevu, R.; Yang, X.; Matthews, C.R.
Specific structure appears at the N terminus in the sub-millisecond folding intermediate of the alpha subunit of tryptophan synthase, a TIM barrel protein
J. Mol. Biol.
351
445-452
2005
Escherichia coli
Manually annotated by BRENDA team
Jeong, M.S.; Jang, S.B.
Crystallization and X-ray crystallographic studies of wild-type and mutant tryptophan synthase alpha-subunits from Escherichia coli
Mol. Cells
19
219-222
2005
Escherichia coli
Manually annotated by BRENDA team
Wu, Y.; Vadrevu, R.; Kathuria, S.; Yang, X.; Matthews, C.R.
A tightly packed hydrophobic cluster directs the formation of an off-pathway sub-millisecond folding intermediate in the alpha subunit of tryptophan synthase, a TIM barrel protein
J. Mol. Biol.
366
1624-1638
2007
Escherichia coli (P0A877)
Manually annotated by BRENDA team
Vadrevu, R.; Wu, Y.; Matthews, C.R.
NMR analysis of partially folded states and persistent structure in the alpha subunit of tryptophan synthase: implications for the equilibrium folding mechanism of a 29-kDa TIM barrel protein
J. Mol. Biol.
377
294-306
2008
Escherichia coli
Manually annotated by BRENDA team
Nishio, K.; Ogasahara, K.; Morimoto, Y.; Tsukihara, T.; Lee, S.J.; Yutani, K.
Large conformational changes in the Escherichia coli tryptophan synthase beta(2) subunit upon pyridoxal 5-phosphate binding
FEBS J.
277
2157-2170
2010
Escherichia coli (P0A879), Escherichia coli
Manually annotated by BRENDA team
Zhao, G.; Liu, J.; Dong, K.; Zhang, F.; Zhang, H.; Liu, Q.; Jiao, Q.
Enzymatic synthesis of L-tryptophan from hair acid hydrolysis industries wastewater with tryptophan synthase
Biores. Technol.
102
3554-3557
2011
Escherichia coli, Escherichia coli MG1655
Manually annotated by BRENDA team
Dunn, M.F.
Allosteric regulation of substrate channeling and catalysis in the tryptophan synthase bienzyme complex
Arch. Biochem. Biophys.
519
154-166
2012
Escherichia coli
Manually annotated by BRENDA team
Xu, L.; Wang, Z.; Mao, P.; Liu, J.; Zhang, H.; Liu, Q.; Jiao, Q.C.
Enzymatic synthesis of S-phenyl-L-cysteine from keratin hydrolysis industries wastewater with tryptophan synthase
Biores. Technol.
133
635-637
2013
Escherichia coli
Manually annotated by BRENDA team
Murciano-Calles, J.; Romney, D.; Brinkmann-Chen, S.; Buller, A.; Arnold, F.
A Panel of TrpB biocatalysts derived from tryptophan synthase through the transfer of mutations that mimic allosteric activation
Angew. Chem. Int. Ed. Engl.
55
11577-11581
2016
Archaeoglobus fulgidus (O28672), Escherichia coli (P0A879), Thermotoga maritima (P50909), Pyrococcus furiosus (Q8U093), Pyrococcus furiosus
Manually annotated by BRENDA team
Kadumuri, R.; Gullipalli, J.; Subramanian, S.; Jaipuria, G.; Atreya, H.; Vadrevu, R.
Crowding interactions perturb structure and stability by destabilizing the stable core of the alpha-subunit of tryptophan synthase
FEBS Lett.
590
2096-2105
2016
Escherichia coli
Manually annotated by BRENDA team
Xu, L.; Gao, G.; Cao, W.; Zhao, L.; Zhang, X.; Jiao, Q.; Chen, J.; Song, M.
Enzymatic synthesis of l-2-methyltryptophan catalyzed by tryptophan synthase in a water/organic solvent biphase system
J. Food Sci. Biotechnol.
36
547-552
2017
Escherichia coli
-
Manually annotated by BRENDA team
Axe, J.; ORourke, K.; Kerstetter, N.; Yezdimer, E.; Chan, Y.; Chasin, A.; Boehr, D.
Severing of a hydrogen bond disrupts amino acid networks in the catalytically active state of the alpha subunit of tryptophan synthase
Protein Sci.
24
484-494
2015
Escherichia coli (P0A877), Escherichia coli
Manually annotated by BRENDA team