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1-C-(indol-3-yl)glycerol 3-phosphate = indole + D-glyceraldehyde 3-phosphate
(1a)
-
-
-
L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate = L-tryptophan + D-glyceraldehyde 3-phosphate + H2O
L-serine + indole = L-tryptophan + H2O
(1b)
-
-
-
L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate = L-tryptophan + D-glyceraldehyde 3-phosphate + H2O
mechanism
-
L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate = L-tryptophan + D-glyceraldehyde 3-phosphate + H2O
mechanism
-
L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate = L-tryptophan + D-glyceraldehyde 3-phosphate + H2O
also catalyses the conversion of serine and indole into tryptophan and water, and of indoleglycerol phosphate into indole and glyceraldehyde phosphate (the latter reaction was listed formerly as EC 4.2.1.8)
-
L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate = L-tryptophan + D-glyceraldehyde 3-phosphate + H2O
also catalyses the conversion of serine and indole into tryptophan and water, and of indoleglycerol phosphate into indole and glyceraldehyde phosphate (the latter reaction was listed formerly as EC 4.2.1.8)
-
L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate = L-tryptophan + D-glyceraldehyde 3-phosphate + H2O
also catalyses the conversion of serine and indole into tryptophan and water, and of indoleglycerol phosphate into indole and glyceraldehyde phosphate (the latter reaction was listed formerly as EC 4.2.1.8)
-
L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate = L-tryptophan + D-glyceraldehyde 3-phosphate + H2O
also catalyses the conversion of serine and indole into tryptophan and water, and of indoleglycerol phosphate into indole and glyceraldehyde phosphate (the latter reaction was listed formerly as EC 4.2.1.8)
-
L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate = L-tryptophan + D-glyceraldehyde 3-phosphate + H2O
also catalyses the conversion of serine and indole into tryptophan and water, and of indoleglycerol phosphate into indole and glyceraldehyde phosphate (the latter reaction was listed formerly as EC 4.2.1.8)
-
L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate = L-tryptophan + D-glyceraldehyde 3-phosphate + H2O
also catalyses the conversion of serine and indole into tryptophan and water, and of indoleglycerol phosphate into indole and glyceraldehyde phosphate (the latter reaction was listed formerly as EC 4.2.1.8)
L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate = L-tryptophan + D-glyceraldehyde 3-phosphate + H2O
also catalyses the conversion of serine and indole into tryptophan and water, and of indoleglycerol phosphate into indole and glyceraldehyde phosphate (the latter reaction was listed formerly as EC 4.2.1.8), allostery and substrate channeling
-
L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate = L-tryptophan + D-glyceraldehyde 3-phosphate + H2O
also catalyses the conversion of serine and indole into tryptophan and water, and of indoleglycerol phosphate into indole and glyceraldehyde phosphate (the latter reaction was listed formerly as EC 4.2.1.8), allostery and substrate channeling
-
L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate = L-tryptophan + D-glyceraldehyde 3-phosphate + H2O
also catalyses the conversion of serine and indole into tryptophan and water, and of indoleglycerol phosphate into indole and glyceraldehyde phosphate (the latter reaction was listed formerly as EC 4.2.1.8), catalytic mechanism
-
L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate = L-tryptophan + D-glyceraldehyde 3-phosphate + H2O
also catalyses the conversion of serine and indole into tryptophan and water, and of indoleglycerol phosphate into indole and glyceraldehyde phosphate (the latter reaction was listed formerly as EC 4.2.1.8), catalytic mechanism of beta-reaction
-
L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate = L-tryptophan + D-glyceraldehyde 3-phosphate + H2O
also catalyses the conversion of serine and indole into tryptophan and water, and of indoleglycerol phosphate into indole and glyceraldehyde phosphate (the latter reaction was listed formerly as EC 4.2.1.8), catalytic mechanism, allosteric ligand binding
-
L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate = L-tryptophan + D-glyceraldehyde 3-phosphate + H2O
also catalyses the conversion of serine and indole into tryptophan and water, and of indoleglycerol phosphate into indole and glyceraldehyde phosphate (the latter reaction was listed formerly as EC 4.2.1.8), detailed alpha-subunit catalytic mechanism
-
L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate = L-tryptophan + D-glyceraldehyde 3-phosphate + H2O
also catalyses the conversion of serine and indole into tryptophan and water, and of indoleglycerol phosphate into indole and glyceraldehyde phosphate (the latter reaction was listed formerly as EC 4.2.1.8), detailed mechanism of the beta-reaction, beta-active site structure
-
L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate = L-tryptophan + D-glyceraldehyde 3-phosphate + H2O
also catalyses the conversion of serine and indole into tryptophan and water, and of indoleglycerol phosphate into indole and glyceraldehyde phosphate (the latter reaction was listed formerly as EC 4.2.1.8), interaction of residues G181 and S178 are essential for the quilibrium between active closed and inactive open conformation of the alpha-active site
-
L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate = L-tryptophan + D-glyceraldehyde 3-phosphate + H2O
also catalyses the conversion of serine and indole into tryptophan and water, and of indoleglycerol phosphate into indole and glyceraldehyde phosphate (the latter reaction was listed formerly as EC 4.2.1.8), mechanism
-
L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate = L-tryptophan + D-glyceraldehyde 3-phosphate + H2O
also catalyses the conversion of serine and indole into tryptophan and water, and of indoleglycerol phosphate into indole and glyceraldehyde phosphate (the latter reaction was listed formerly as EC 4.2.1.8), mechanism, intermediate formation, reaction equilibrium, conformational states of the catalytic cycle
-
L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate = L-tryptophan + D-glyceraldehyde 3-phosphate + H2O
also catalyses the conversion of serine and indole into tryptophan and water, and of indoleglycerol phosphate into indole and glyceraldehyde phosphate (the latter reaction was listed formerly as EC 4.2.1.8), mechanism, ligand binding, unique ligand-mediated long-range cooperativity for substrate channeling, allosteric control, coordination of metabolic cycles
-
L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate = L-tryptophan + D-glyceraldehyde 3-phosphate + H2O
also catalyses the conversion of serine and indole into tryptophan and water, and of indoleglycerol phosphate into indole and glyceraldehyde phosphate (the latter reaction was listed formerly as EC 4.2.1.8), mechanisms of alpha-and beta-reaction, active site structures
-
L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate = L-tryptophan + D-glyceraldehyde 3-phosphate + H2O
also catalyses the conversion of serine and indole into tryptophan and water, and of indoleglycerol phosphate into indole and glyceraldehyde phosphate (the latter reaction was listed formerly as EC 4.2.1.8), reaction mechanism and intermediates
-
L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate = L-tryptophan + D-glyceraldehyde 3-phosphate + H2O
also catalyses the conversion of serine and indole into tryptophan and water, and of indoleglycerol phosphate into indole and glyceraldehyde phosphate (the latter reaction was listed formerly as EC 4.2.1.8), reaction mechanism of alpha- and beta-reaction step, T183 and D60 are involved
-
L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate = L-tryptophan + D-glyceraldehyde 3-phosphate + H2O
also catalyses the conversion of serine and indole into tryptophan and water, and of indoleglycerol phosphate into indole and glyceraldehyde phosphate (the latter reaction was listed formerly as EC 4.2.1.8), reaction mechanism, formation of intermediates in the alpha-reaction
-
L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate = L-tryptophan + D-glyceraldehyde 3-phosphate + H2O
also catalyses the conversion of serine and indole into tryptophan and water, and of indoleglycerol phosphate into indole and glyceraldehyde phosphate (the latter reaction was listed formerly as EC 4.2.1.8), reaction mechanism, formation of quinoid reaction intermediates in the beta-active site upon reaction with the substrates
-
L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate = L-tryptophan + D-glyceraldehyde 3-phosphate + H2O
also catalyses the conversion of serine and indole into tryptophan and water, and of indoleglycerol phosphate into indole and glyceraldehyde phosphate (the latter reaction was listed formerly as EC 4.2.1.8), reaction mechanism, pyridoxal 5'-phosphate in beta-reaction, formation of an alpha-aminoacrylate Schiff base intermediate
-
L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate = L-tryptophan + D-glyceraldehyde 3-phosphate + H2O
also catalyses the conversion of serine and indole into tryptophan and water, and of indoleglycerol phosphate into indole and glyceraldehyde phosphate (the latter reaction was listed formerly as EC 4.2.1.8), salt bridge betaAsp305-betaArg141 plays a crucial role in both the formation of the closed conformation of the beta-site and the transmission of allosteric signals between the alpha- and beta-sites that switch the alpha-site on and off, mechanism
-
L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate = L-tryptophan + D-glyceraldehyde 3-phosphate + H2O
overall reaction
-
-
-
L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate = L-tryptophan + D-glyceraldehyde 3-phosphate + H2O
pressure perturbation is used to quantify the effects of monovalent cations, ligands, and mutations on the conformational equilibrium of Trp synthase. P-jump kinetics in the presence of Na+, NH4+, and Na+ together with benzimidazole are also examined. The plots of lnk versus P are nonlinear and require a compressibility (beta0) term to obtain a good fit. Compressibility (beta0) is positive for the Na+ enzyme but negative for NH4+ and Na+ with benzimidazole. These results suggest that there is a large contribution of solvation to the kinetics of the conformational change of Trp synthase
-
L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate = L-tryptophan + D-glyceraldehyde 3-phosphate + H2O
catalytic mechanism via an indoline quinonoid intermediate, with importance of an equilibrium between tautomeric forms of the substrate, with the protonation state of the major isomer directing the next catalytic step, active site structure, and indoline and beta-site reactions by NMR spectroscopy, overview
-
L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate = L-tryptophan + D-glyceraldehyde 3-phosphate + H2O
catalyzed reaction and structure of the tryptophan synthase complex, mechanism, overview. Model of the catalytic cycle of the transient enzyme complex, overview
-
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(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine
L-tryptophan + D-glyceraldehyde 3-phosphate + H2O
(3S)-2,3-dihydro-5-fluoro-L-tryptophan
?
-
isomerization
-
-
?
1-(indol-3-yl)glycerol 3-phosphate
D-glyceraldehyde 3-phosphate + indole
1-(indol-3-yl)glycerol 3-phosphate + L-serine
L-tryptophan + D-glyceraldehyde 3-phosphate
1-(indol-3-yl)glycerol 3-phosphate + L-serine
L-tryptophan + D-glyceraldehyde 3-phosphate + H2O
1-C-(indol-3-yl)glycerol 3-phosphate
D-glyceraldehyde 3-phosphate + indole
2-amino-3-butenoic acid
2-oxobutyric acid + NH3
2-mercaptoethanol + L-serine + pyridoxal phosphate
S-pyruvylmercaptoethanol + pyridoxamine phosphate + H2O
5-fluoro-L-tryptophan
?
-
isomerization
-
-
?
beta-chloro-L-alanine
pyruvate + NH3 + HCl
-
in absence of indole
-
?
beta-chloro-L-alanine + indole
L-tryptophan + HCl
-
-
-
?
D-glyceraldehyde 3-phosphate + indole
1-(indol-3-yl)glycerol 3-phosphate
-
-
-
?
indole + D-glyceraldehyde 3-phosphate
indole-3-glycerol phosphate
indole + L-serine
L-tryptophan + H2O
indole-3-glycerol phosphate
indole + D-glyceraldehyde 3-phosphate
indoleglycerol phosphate
indole + D-glyceraldehyde 3-phosphate
the reaction is catalyzed by the tryptophan synthase alpha-subunit TrpA
-
-
r
indoline + L-serine
dihydroisotryptophan + H2O
-
monovalent cation-bound alpha-aminoacrylate Schiff base species E(A-A) reacts rapidly with indoline to give the indoline quinonoid species, E(Q)indoline, which slowly converts to dihydroiso-L-tryptophan
-
-
?
L-histidine + L-serine
?
-
reaction of L-His with internal aldimine species gives an equilibrating mixture of external aldimine and quinonoid species, E(Aex)his and E(Q)his
-
-
?
L-Ser + indole
L-tryptophan + H2O
-
reaction catalyzed by the beta subunit
-
-
ir
L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate
L-tryptophan + D-glyceraldehyde 3-phosphate + H2O
L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate
L-tryptophan + glyceraldehyde 3-phosphate + H2O
L-serine + 1H-indole-5-carbaldehyde
5-formyl-L-tryptophan + H2O
L-serine + 2-methylindole
2-methyltryptophan + H2O
-
-
-
-
?
L-serine + 2-methylindole
L-2-methyltryptophan + H2O
-
-
-
-
?
L-serine + 4-bromoindole
4-bromotryptophan + H2O
L-serine + 4-hydroxyindole
4-hydroxytryptophan + H2O
-
-
-
?
L-serine + 4-methylindole
4-methyltryptophan + H2O
-
-
-
-
?
L-serine + 5-bromoindole
5-bromo-L-tryptophan + H2O
L-serine + 5-bromoindole
5-bromotryptophan + H2O
-
-
-
-
?
L-serine + 5-chloroindole
5-chloro-L-tryptophan + H2O
L-serine + 5-chloroindole
5-chlorotryptophan + H2O
-
-
-
-
?
L-serine + 5-cyanoindole
5-cyano-L-tryptophan + H2O
substrate of mutant M145T/N167D, 49% yield
-
-
?
L-serine + 5-fluoroindole
5-fluorotryptophan + H2O
L-serine + 5-hydroxyindole
5-hydroxy-L-tryptophan + H2O
L-serine + 5-hydroxyindole
5-hydroxytryptophan + H2O
-
-
-
?
L-serine + 5-methoxyindole
5-methoxy-L-tryptophan + H2O
L-serine + 5-methylindole
5-methyl-L-tryptophan + H2O
L-serine + 5-methylindole
5-methyltryptophan + H2O
-
-
-
-
?
L-serine + 5-nitroindole
5-nitro-L-tryptophan + H2O
L-serine + 6-bromoindole
6-bromotryptophan + H2O
-
-
-
-
?
L-serine + 6-chloroindole
6-chlorotryptophan + H2O
-
-
-
-
?
L-serine + 6-fluoroindole
6-fluorotryptophan + H2O
-
-
-
-
?
L-serine + 6-methylindole
6-methyltryptophan + H2O
-
-
-
-
?
L-serine + 7-bromoindole
7-bromotryptophan + H2O
L-serine + 7-chloroindole
7-chlorotryptophan + H2O
-
-
-
-
?
L-serine + 7-fluoroindole
7-fluorotryptophan + H2O
L-serine + 7-hydroxyindole
7-hydroxytryptophan + H2O
-
-
-
?
L-serine + 7-methylindole
7-methyltryptophan + H2O
-
-
-
-
?
L-serine + indole
L-tryptophan + H2O
L-serine + indole
tryptophan + H2O
L-serine + indoline
dihydro-iso-L-tryptophan + H2O
-
-
i.e. DIT
?
L-serine + indoline
dihydroiso-L-tryptophan
-
wild-type and mutant D305A enzymes
-
?
L-serine + indoline
dihydroiso-L-tryptophan + H2O
-
-
i.e. DIT
?
L-serine + N-(4'-trifluoromethoxybenzenesulfonyl)-2-aminoethyl phosphate
?
-
-
-
-
?
L-serine + N-(4'-trifluoromethoxybenzoyl)-2-aminoethyl phosphate
?
-
-
-
-
?
L-serine + thiophenol
(S)-phenyl-L-cysteine + H2O
-
-
-
-
?
L-threonine + 1-C-(indol-3-yl)glycerol 3-phosphate
(2S,3S)-beta-methyltryptophan + D-glyceraldehyde 3-phosphate + H2O
L-threonine + 2-methylindole
2-methyl-(2S,3S)-beta-methyltryptophan + H2O
L-threonine + 4-fluoroindole
4-fluoro-(2S,3S)-beta-methyltryptophan + H2O
L-threonine + 4-methylindole
4-methyl-(2S,3S)-beta-methyltryptophan + H2O
L-threonine + 5-fluoroindole
5-fluoro-(2S,3S)-beta-methyltryptophan + H2O
reaction of mutant I16V/E17G/I68V/F95L/F274S/T292S/T321A/V384A
-
-
?
L-threonine + 6-methylindole
6-methyl-(2S,3S)-beta-methyltryptophan + H2O
L-threonine + 7-azaindole
7-aza-(2S,3S)-beta-methyltryptophan + H2O
reaction of mutant I16V/E17G/I68V/F95L/F274S/T292S/T321A/V384A
-
-
?
L-threonine + 7-chloroindole
7-chloro-(2S,3S)-beta-methyltryptophan + H2O
-
-
-
-
?
L-threonine + 7-fluoroindole
7-fluoro-(2S,3S)-beta-methyltryptophan + H2O
-
-
-
-
?
L-threonine + 7-methoxyindole
7-methoxy-(2S,3S)-beta-methyltryptophan + H2O
-
-
-
-
?
L-threonine + 7-methylindole
7-methyl-(2S,3S)-beta-methyltryptophan + H2O
-
-
-
-
?
L-threonine + indole
(2S,3S)-beta-methyltryptophan + H2O
L-tryptophan + D-glyceraldehyde 3-phosphate + H2O
indole-3-glycerol phosphate + L-serine
-
r
r
?
O-phospho-L-serine + indole
L-tryptophan + phosphate
serine + indole
tryptophan + H2O
-
-
-
?
additional information
?
-
(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine
L-tryptophan + D-glyceraldehyde 3-phosphate + H2O
-
-
-
?
(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine
L-tryptophan + D-glyceraldehyde 3-phosphate + H2O
-
-
-
-
?
1-(indol-3-yl)glycerol 3-phosphate
D-glyceraldehyde 3-phosphate + indole
-
alpha-subunit of the bienzyme complex, alpha-reaction
-
?
1-(indol-3-yl)glycerol 3-phosphate
D-glyceraldehyde 3-phosphate + indole
-
alpha-subunit of the bienzyme complex, alpha-reaction
-
?
1-(indol-3-yl)glycerol 3-phosphate
D-glyceraldehyde 3-phosphate + indole
-
alpha-subunit of the bienzyme complex, alpha-reaction
-
?
1-(indol-3-yl)glycerol 3-phosphate
D-glyceraldehyde 3-phosphate + indole
-
alpha-subunit of the bienzyme complex, alpha-reaction
-
?
1-(indol-3-yl)glycerol 3-phosphate
D-glyceraldehyde 3-phosphate + indole
-
alpha-subunit of the bienzyme complex, alpha-reaction
-
?
1-(indol-3-yl)glycerol 3-phosphate
D-glyceraldehyde 3-phosphate + indole
-
alpha-subunit of the bienzyme complex, alpha-reaction
-
?
1-(indol-3-yl)glycerol 3-phosphate
D-glyceraldehyde 3-phosphate + indole
-
alpha-subunit of the bienzyme complex, alpha-reaction
channeling of indole to the beta-subunit active site
?
1-(indol-3-yl)glycerol 3-phosphate
D-glyceraldehyde 3-phosphate + indole
-
alpha-subunit of the bienzyme complex, alpha-reaction
-
?
1-(indol-3-yl)glycerol 3-phosphate
D-glyceraldehyde 3-phosphate + indole
alpha-subunit of the bienzyme complex, alpha-reaction
-
?
1-(indol-3-yl)glycerol 3-phosphate
D-glyceraldehyde 3-phosphate + indole
-
alpha-subunit of the bienzyme complex, alpha-reaction
-
?
1-(indol-3-yl)glycerol 3-phosphate
D-glyceraldehyde 3-phosphate + indole
-
alpha-subunit of the bienzyme complex, alpha-reaction
-
?
1-(indol-3-yl)glycerol 3-phosphate
D-glyceraldehyde 3-phosphate + indole
-
alpha-subunit of the bienzyme complex, alpha-reaction
-
?
1-(indol-3-yl)glycerol 3-phosphate
D-glyceraldehyde 3-phosphate + indole
-
alpha-subunit of the bienzyme complex, alpha-reaction
-
?
1-(indol-3-yl)glycerol 3-phosphate
D-glyceraldehyde 3-phosphate + indole
-
alpha-subunit of the bienzyme complex, alpha-reaction
-
?
1-(indol-3-yl)glycerol 3-phosphate
D-glyceraldehyde 3-phosphate + indole
-
alpha-subunit of the bienzyme complex, alpha-reaction
-
?
1-(indol-3-yl)glycerol 3-phosphate
D-glyceraldehyde 3-phosphate + indole
-
alpha-subunit of the bienzyme complex, alpha-reaction
-
?
1-(indol-3-yl)glycerol 3-phosphate
D-glyceraldehyde 3-phosphate + indole
-
alpha-subunit of the bienzyme complex, alpha-reaction
-
?
1-(indol-3-yl)glycerol 3-phosphate
D-glyceraldehyde 3-phosphate + indole
-
alpha-subunit of the bienzyme complex, alpha-reaction
-
?
1-(indol-3-yl)glycerol 3-phosphate
D-glyceraldehyde 3-phosphate + indole
-
alpha-subunit of the bienzyme complex, alpha-reaction
-
?
1-(indol-3-yl)glycerol 3-phosphate
D-glyceraldehyde 3-phosphate + indole
-
alpha-subunit of the bienzyme complex, alpha-reaction
-
?
1-(indol-3-yl)glycerol 3-phosphate
D-glyceraldehyde 3-phosphate + indole
-
alpha-subunit of the bienzyme complex, alpha-reaction
-
?
1-(indol-3-yl)glycerol 3-phosphate
D-glyceraldehyde 3-phosphate + indole
-
alpha-subunit of the bienzyme complex, alpha-reaction
-
?
1-(indol-3-yl)glycerol 3-phosphate
D-glyceraldehyde 3-phosphate + indole
-
alpha-subunit of the bienzyme complex, alpha-reaction
-
?
1-(indol-3-yl)glycerol 3-phosphate
D-glyceraldehyde 3-phosphate + indole
-
alpha-subunit of the bienzyme complex, alpha-reaction
-
?
1-(indol-3-yl)glycerol 3-phosphate
D-glyceraldehyde 3-phosphate + indole
-
alpha-subunit of the bienzyme complex, alpha-reaction
-
?
1-(indol-3-yl)glycerol 3-phosphate
D-glyceraldehyde 3-phosphate + indole
-
alpha-subunit of the bienzyme complex, alpha-reaction
-
?
1-(indol-3-yl)glycerol 3-phosphate
D-glyceraldehyde 3-phosphate + indole
-
alpha-subunit of the bienzyme complex, alpha-reaction
-
?
1-(indol-3-yl)glycerol 3-phosphate
D-glyceraldehyde 3-phosphate + indole
-
alpha-subunit of the bienzyme complex, alpha-reaction
-
?
1-(indol-3-yl)glycerol 3-phosphate
D-glyceraldehyde 3-phosphate + indole
-
alpha-subunit of the bienzyme complex, alpha-reaction
-
?
1-(indol-3-yl)glycerol 3-phosphate
D-glyceraldehyde 3-phosphate + indole
-
alpha-subunit of the bifunctional enzyme complex, alpha-reaction
-
?
1-(indol-3-yl)glycerol 3-phosphate
D-glyceraldehyde 3-phosphate + indole
-
alpha-subunit of the bifunctional enzyme complex, alpha-reaction
-
?
1-(indol-3-yl)glycerol 3-phosphate
D-glyceraldehyde 3-phosphate + indole
-
alpha-subunit of the bienzyme complex, alpha-reaction, the consumption of indole in the beta-reaction is necessary for optimal activity
-
?
1-(indol-3-yl)glycerol 3-phosphate
D-glyceraldehyde 3-phosphate + indole
-
alpha-subunit of the bienzyme complex, alpha-reaction
-
?
1-(indol-3-yl)glycerol 3-phosphate + L-serine
L-tryptophan + D-glyceraldehyde 3-phosphate
-
-
-
?
1-(indol-3-yl)glycerol 3-phosphate + L-serine
L-tryptophan + D-glyceraldehyde 3-phosphate
-
-
-
?
1-(indol-3-yl)glycerol 3-phosphate + L-serine
L-tryptophan + D-glyceraldehyde 3-phosphate
-
-
-
?
1-(indol-3-yl)glycerol 3-phosphate + L-serine
L-tryptophan + D-glyceraldehyde 3-phosphate
-
-
-
?
1-(indol-3-yl)glycerol 3-phosphate + L-serine
L-tryptophan + D-glyceraldehyde 3-phosphate
-
alpha-subunit of the bienzyme complex, alpha-reaction
-
?
1-(indol-3-yl)glycerol 3-phosphate + L-serine
L-tryptophan + D-glyceraldehyde 3-phosphate + H2O
-
-
-
-
?
1-(indol-3-yl)glycerol 3-phosphate + L-serine
L-tryptophan + D-glyceraldehyde 3-phosphate + H2O
-
catalyzed by alpha2beta2 holoenzyme
-
?
1-(indol-3-yl)glycerol 3-phosphate + L-serine
L-tryptophan + D-glyceraldehyde 3-phosphate + H2O
-
-
-
?
1-(indol-3-yl)glycerol 3-phosphate + L-serine
L-tryptophan + D-glyceraldehyde 3-phosphate + H2O
-
-
-
-
?
1-(indol-3-yl)glycerol 3-phosphate + L-serine
L-tryptophan + D-glyceraldehyde 3-phosphate + H2O
-
catalyzed by alpha2beta2 holoenzyme
-
-
?
1-(indol-3-yl)glycerol 3-phosphate + L-serine
L-tryptophan + D-glyceraldehyde 3-phosphate + H2O
-
hybrid enzyme with alpha subunit of E. coli or Salmonella typhimurium active in this reaction
-
-
?
1-(indol-3-yl)glycerol 3-phosphate + L-serine
L-tryptophan + D-glyceraldehyde 3-phosphate + H2O
-
hybrid enzyme with beta2 subunit of E. coli or Salmonella typhimurium active in this reaction
-
-
?
1-(indol-3-yl)glycerol 3-phosphate + L-serine
L-tryptophan + D-glyceraldehyde 3-phosphate + H2O
-
-
-
-
?
1-(indol-3-yl)glycerol 3-phosphate + L-serine
L-tryptophan + D-glyceraldehyde 3-phosphate + H2O
-
r
-
?
1-(indol-3-yl)glycerol 3-phosphate + L-serine
L-tryptophan + D-glyceraldehyde 3-phosphate + H2O
-
-
-
-
?
1-(indol-3-yl)glycerol 3-phosphate + L-serine
L-tryptophan + D-glyceraldehyde 3-phosphate + H2O
-
-
-
-
?
1-(indol-3-yl)glycerol 3-phosphate + L-serine
L-tryptophan + D-glyceraldehyde 3-phosphate + H2O
-
catalyzed by alpha2beta2 holoenzyme
-
?
1-(indol-3-yl)glycerol 3-phosphate + L-serine
L-tryptophan + D-glyceraldehyde 3-phosphate + H2O
-
alpha reaction
-
-
r
1-C-(indol-3-yl)glycerol 3-phosphate
D-glyceraldehyde 3-phosphate + indole
-
-
-
-
?
1-C-(indol-3-yl)glycerol 3-phosphate
D-glyceraldehyde 3-phosphate + indole
-
-
-
-
?
2-amino-3-butenoic acid
2-oxobutyric acid + NH3
-
vinylglycine
-
?
2-amino-3-butenoic acid
2-oxobutyric acid + NH3
-
vinylglycine
-
?
2-mercaptoethanol + L-serine + pyridoxal phosphate
S-pyruvylmercaptoethanol + pyridoxamine phosphate + H2O
-
-
-
?
2-mercaptoethanol + L-serine + pyridoxal phosphate
S-pyruvylmercaptoethanol + pyridoxamine phosphate + H2O
-
-
-
?
indole + D-glyceraldehyde 3-phosphate
indole-3-glycerol phosphate
-
r
r
?
indole + D-glyceraldehyde 3-phosphate
indole-3-glycerol phosphate
-
r
r
?
indole + D-glyceraldehyde 3-phosphate
indole-3-glycerol phosphate
-
r
r
?
indole + D-glyceraldehyde 3-phosphate
indole-3-glycerol phosphate
-
r
r
?
indole + L-serine
L-tryptophan + H2O
-
catalyzed by beta2 subunit
-
?
indole + L-serine
L-tryptophan + H2O
-
-
-
-
?
indole + L-serine
L-tryptophan + H2O
-
-
-
?
indole + L-serine
L-tryptophan + H2O
-
-
-
-
?
indole + L-serine
L-tryptophan + H2O
-
-
-
?
indole + L-serine
L-tryptophan + H2O
-
catalyzed by beta2 subunit
-
-
?
indole + L-serine
L-tryptophan + H2O
-
OH of Ser can be replaced by SCH3, OCH3 and Cl, but not by indole, indole can be replaced by CH3SH, CH2OHCH2SH, thiobenzyl alcohol, 1-propanethiol, 1-butanethiol, selenols, 6-azidoindole
-
-
?
indole + L-serine
L-tryptophan + H2O
-
-
-
-
?
indole + L-serine
L-tryptophan + H2O
-
-
-
?
indole + L-serine
L-tryptophan + H2O
-
-
-
-
?
indole + L-serine
L-tryptophan + H2O
-
-
-
-
?
indole + L-serine
L-tryptophan + H2O
-
hybrid enzyme with alpha subunit of E. coli or Salmonella typhimurium shows low activity in this reaction
-
-
?
indole + L-serine
L-tryptophan + H2O
-
hybrid enzyme with beta2 subunit of E. coli or Salmonella typhimurium inactive in this reaction
-
-
?
indole + L-serine
L-tryptophan + H2O
-
-
-
?
indole + L-serine
L-tryptophan + H2O
-
-
-
-
?
indole + L-serine
L-tryptophan + H2O
-
-
-
-
?
indole + L-serine
L-tryptophan + H2O
-
catalyzed by beta2 subunit
-
-
?
indole + L-serine
L-tryptophan + H2O
-
OH of Ser can be replaced by SCH3, OCH3 and Cl, but not by indole, indole can be replaced by CH3SH, CH2OHCH2SH, thiobenzyl alcohol, 1-propanethiol, 1-butanethiol, selenols, 6-azidoindole
-
-
?
indole + L-serine
L-tryptophan + H2O
-
-
-
?
indole-3-glycerol phosphate
indole + D-glyceraldehyde 3-phosphate
-
catalyzed by alpha-subunit
-
?
indole-3-glycerol phosphate
indole + D-glyceraldehyde 3-phosphate
-
-
-
?
indole-3-glycerol phosphate
indole + D-glyceraldehyde 3-phosphate
-
-
-
-
?
indole-3-glycerol phosphate
indole + D-glyceraldehyde 3-phosphate
-
r
r
?
indole-3-glycerol phosphate
indole + D-glyceraldehyde 3-phosphate
-
catalyzed by alpha-subunit
-
?
indole-3-glycerol phosphate
indole + D-glyceraldehyde 3-phosphate
-
-
-
?
indole-3-glycerol phosphate
indole + D-glyceraldehyde 3-phosphate
-
r
r
?
indole-3-glycerol phosphate
indole + D-glyceraldehyde 3-phosphate
-
hybrid enzyme with beta2 subunit of E. coli or Salmonella typhimurium active in this reaction
-
-
?
indole-3-glycerol phosphate
indole + D-glyceraldehyde 3-phosphate
-
catalyzed by alpha-subunit
-
-
?
indole-3-glycerol phosphate
indole + D-glyceraldehyde 3-phosphate
-
-
-
-
?
indole-3-glycerol phosphate
indole + D-glyceraldehyde 3-phosphate
-
r
r
?
indole-3-glycerol phosphate
indole + D-glyceraldehyde 3-phosphate
-
-
-
-
?
indole-3-glycerol phosphate
indole + D-glyceraldehyde 3-phosphate
-
r
r
?
indole-3-glycerol phosphate
indole + D-glyceraldehyde 3-phosphate
-
mechanism
r
?
indole-3-glycerol phosphate
indole + D-glyceraldehyde 3-phosphate
-
catalyzed by alpha-subunit
-
?
indole-3-glycerol phosphate
indole + D-glyceraldehyde 3-phosphate
-
reaction is catalyzed by alpha-subunit. Structural basis of the catalytic mechanism and regulation of the alpha-subunit
-
-
?
indole-3-glycerol phosphate
indole + D-glyceraldehyde 3-phosphate
-
reaction catalyzed by the alpha subunit
-
-
r
L-serine
pyruvate + NH3
-
-
-
?
L-serine
pyruvate + NH3
-
catalyzed by beta2-subunit
-
?
L-serine
pyruvate + NH3
-
OH of Ser can be replaced by SCH3, OCH3 and Cl, but not by indole
-
?
L-serine
pyruvate + NH3
-
-
-
?
L-serine
pyruvate + NH3
-
-
-
?
L-serine
pyruvate + NH3
-
catalyzed by beta2-subunit
-
?
L-serine
pyruvate + NH3
-
OH of Ser can be replaced by SCH3, OCH3 and Cl, but not by indole
-
?
L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate
L-tryptophan + D-glyceraldehyde 3-phosphate + H2O
-
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 + 1-C-(indol-3-yl)glycerol 3-phosphate
L-tryptophan + D-glyceraldehyde 3-phosphate + H2O
-
-
-
?
L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate
L-tryptophan + D-glyceraldehyde 3-phosphate + H2O
-
-
-
?
L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate
L-tryptophan + D-glyceraldehyde 3-phosphate + H2O
-
-
-
-
?
L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate
L-tryptophan + D-glyceraldehyde 3-phosphate + H2O
-
-
-
?
L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate
L-tryptophan + D-glyceraldehyde 3-phosphate + H2O
-
-
-
r
L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate
L-tryptophan + D-glyceraldehyde 3-phosphate + H2O
-
overall reaction
-
-
?
L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate
L-tryptophan + D-glyceraldehyde 3-phosphate + H2O
-
-
-
-
?
L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate
L-tryptophan + D-glyceraldehyde 3-phosphate + H2O
-
-
-
-
?
L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate
L-tryptophan + D-glyceraldehyde 3-phosphate + H2O
-
-
-
?
L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate
L-tryptophan + D-glyceraldehyde 3-phosphate + H2O
overall reaction
-
-
ir
L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate
L-tryptophan + D-glyceraldehyde 3-phosphate + H2O
the last two steps of L-tryptophan biosynthesis are catalyzed by Trp synthase, a heterotetramer composed of TrpA and TrpB. TrpB catalyzes the condensation of indole, synthesized by TrpA, and serine to Trp
-
-
?
L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate
L-tryptophan + D-glyceraldehyde 3-phosphate + H2O
subunit TrpB catalyzes the condensation of indole, synthesized by subunit TrpA, and serine to Trp
-
-
?
L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate
L-tryptophan + glyceraldehyde 3-phosphate + H2O
-
-
-
-
?
L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate
L-tryptophan + glyceraldehyde 3-phosphate + H2O
-
Trp is a precursor of several important signalling molecules in Pseudomonas spp., overview
-
-
?
L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate
L-tryptophan + glyceraldehyde 3-phosphate + H2O
-
-
-
-
?
L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate
L-tryptophan + glyceraldehyde 3-phosphate + H2O
-
-
-
-
?
L-serine + 1H-indole-5-carbaldehyde
5-formyl-L-tryptophan + H2O
substrate of mutant P12L/E17G/I68V/F274S/T292S/T321A
-
-
?
L-serine + 1H-indole-5-carbaldehyde
5-formyl-L-tryptophan + H2O
substrate of mutant M145T/N167D, 32% yield
-
-
?
L-serine + 4-bromoindole
4-bromotryptophan + H2O
-
-
-
-
?
L-serine + 4-bromoindole
4-bromotryptophan + H2O
-
weak reaction
-
-
?
L-serine + 5-bromoindole
5-bromo-L-tryptophan + H2O
-
-
-
?
L-serine + 5-bromoindole
5-bromo-L-tryptophan + H2O
substrate of mutant P12L/E17G/I68V/F274S/T292S/T321A
-
-
?
L-serine + 5-bromoindole
5-bromo-L-tryptophan + H2O
substrate of mutant M145T/N167D, 25% yield
-
-
?
L-serine + 5-chloroindole
5-chloro-L-tryptophan + H2O
substrate of mutant P12L/E17G/I68V/F274S/T292S/T321A
-
-
?
L-serine + 5-chloroindole
5-chloro-L-tryptophan + H2O
substrate of mutant M145T/N167D, 93% yield
-
-
?
L-serine + 5-fluoroindole
5-fluorotryptophan + H2O
-
-
-
-
?
L-serine + 5-fluoroindole
5-fluorotryptophan + H2O
-
-
-
-
?
L-serine + 5-hydroxyindole
5-hydroxy-L-tryptophan + H2O
substrate of mutant P12L/E17G/I68V/F274S/T292S/T321A
-
-
?
L-serine + 5-hydroxyindole
5-hydroxy-L-tryptophan + H2O
substrate of mutant M145T/N167D, 93% yield
-
-
?
L-serine + 5-methoxyindole
5-methoxy-L-tryptophan + H2O
substrate of mutant P12L/E17G/I68V/F274S/T292S/T321A
-
-
?
L-serine + 5-methoxyindole
5-methoxy-L-tryptophan + H2O
substrate of mutant M145T/N167D, 76% yield
-
-
?
L-serine + 5-methylindole
5-methyl-L-tryptophan + H2O
substrate of mutant P12L/E17G/I68V/F274S/T292S/T321A
-
-
?
L-serine + 5-methylindole
5-methyl-L-tryptophan + H2O
substrate of mutant M145T/N167D, 91% yield
-
-
?
L-serine + 5-nitroindole
5-nitro-L-tryptophan + H2O
substrate of mutant P12L/E17G/I68V/F274S/T292S/T321A
-
-
?
L-serine + 5-nitroindole
5-nitro-L-tryptophan + H2O
substrate of mutant M145T/N167D, 88% yield
-
-
?
L-serine + 7-bromoindole
7-bromotryptophan + H2O
-
-
-
-
?
L-serine + 7-bromoindole
7-bromotryptophan + H2O
-
weak reaction
-
-
?
L-serine + 7-fluoroindole
7-fluorotryptophan + H2O
-
-
-
-
?
L-serine + 7-fluoroindole
7-fluorotryptophan + H2O
-
weak reaction
-
-
?
L-serine + indole
L-tryptophan + H2O
-
-
-
-
?
L-serine + indole
L-tryptophan + H2O
-
-
-
?
L-serine + indole
L-tryptophan + H2O
-
-
-
?
L-serine + indole
L-tryptophan + H2O
-
-
-
?
L-serine + indole
L-tryptophan + H2O
-
-
-
-
?
L-serine + indole
L-tryptophan + H2O
-
-
-
-
?
L-serine + indole
L-tryptophan + H2O
-
-
-
?
L-serine + indole
L-tryptophan + H2O
-
-
-
?
L-serine + indole
L-tryptophan + H2O
-
beta-subunit of the bienzyme complex, beta-reaction
-
?
L-serine + indole
L-tryptophan + H2O
-
beta-subunit of the bienzyme complex, beta-reaction
-
?
L-serine + indole
L-tryptophan + H2O
-
beta-subunit of the bienzyme complex, beta-reaction
-
?
L-serine + indole
L-tryptophan + H2O
-
beta-subunit of the bienzyme complex, beta-reaction
-
?
L-serine + indole
L-tryptophan + H2O
-
beta-subunit of the bienzyme complex, beta-reaction
-
?
L-serine + indole
L-tryptophan + H2O
-
beta-subunit of the bienzyme complex, beta-reaction
-
?
L-serine + indole
L-tryptophan + H2O
-
beta-subunit of the bienzyme complex, beta-reaction
-
?
L-serine + indole
L-tryptophan + H2O
-
-
-
-
?
L-serine + indole
L-tryptophan + H2O
-
-
-
-
?
L-serine + indole
L-tryptophan + H2O
-
-
-
?
L-serine + indole
L-tryptophan + H2O
-
-
-
?
L-serine + indole
L-tryptophan + H2O
-
beta-subunit of the bienzyme complex, beta-reaction
-
?
L-serine + indole
L-tryptophan + H2O
beta-subunit of the bienzyme complex, beta-reaction
-
?
L-serine + indole
L-tryptophan + H2O
-
-
-
-
?
L-serine + indole
L-tryptophan + H2O
-
-
-
?
L-serine + indole
L-tryptophan + H2O
-
-
-
-
?
L-serine + indole
L-tryptophan + H2O
-
-
-
-
?
L-serine + indole
L-tryptophan + H2O
-
beta-subunit of the bienzyme complex, beta-reaction
-
?
L-serine + indole
L-tryptophan + H2O
-
beta-subunit of the bienzyme complex, beta-reaction
-
?
L-serine + indole
L-tryptophan + H2O
-
beta-subunit of the bienzyme complex, beta-reaction
-
?
L-serine + indole
L-tryptophan + H2O
-
beta-subunit of the bienzyme complex, beta-reaction
-
?
L-serine + indole
L-tryptophan + H2O
-
beta-subunit of the bienzyme complex, beta-reaction
-
?
L-serine + indole
L-tryptophan + H2O
-
beta-subunit of the bienzyme complex, beta-reaction
-
?
L-serine + indole
L-tryptophan + H2O
-
beta-subunit of the bienzyme complex, beta-reaction
-
?
L-serine + indole
L-tryptophan + H2O
-
beta-subunit of the bienzyme complex, beta-reaction
-
?
L-serine + indole
L-tryptophan + H2O
-
beta-subunit of the bienzyme complex, beta-reaction
-
?
L-serine + indole
L-tryptophan + H2O
-
beta-subunit of the bienzyme complex, beta-reaction
-
?
L-serine + indole
L-tryptophan + H2O
-
beta-subunit of the bienzyme complex, beta-reaction
-
?
L-serine + indole
L-tryptophan + H2O
-
beta-subunit of the bienzyme complex, beta-reaction
-
?
L-serine + indole
L-tryptophan + H2O
-
beta-subunit of the bienzyme complex, beta-reaction
-
?
L-serine + indole
L-tryptophan + H2O
-
beta-subunit of the bienzyme complex, beta-reaction
-
?
L-serine + indole
L-tryptophan + H2O
-
beta-subunit of the bienzyme complex, beta-reaction
-
?
L-serine + indole
L-tryptophan + H2O
-
beta-subunit of the bienzyme complex, beta-reaction
-
?
L-serine + indole
L-tryptophan + H2O
-
beta-subunit of the bienzyme complex, beta-reaction
-
?
L-serine + indole
L-tryptophan + H2O
-
beta-subunit of the bienzyme complex, beta-reaction, detailed determinaion of quinoid reaction intermediates in the beta-active site upon reaction with the substrates
-
?
L-serine + indole
L-tryptophan + H2O
-
beta-subunit of the bienzyme complex, beta-reaction, first step of the reaction is a beta-elimination taht involves a very fast interconversion of the internal aldimine in a highly fluorescent L-serine external aldimine that decays to the alpha-aminoacrylate Schiff base via the alpha-carbon proton removal and beta-hydroxyl group release
-
?
L-serine + indole
L-tryptophan + H2O
-
beta-subunit of the bienzyme complex, beta-reaction, involves multiple covalent transformations facilitated by proton transfer between the cofactor, the reacting substrates, and acid-base catalytic groups of the enzyme
-
?
L-serine + indole
L-tryptophan + H2O
-
beta-subunit of the bifunctional enzyme complex, beta-reaction
-
?
L-serine + indole
L-tryptophan + H2O
-
beta-subunit of the bifunctional enzyme complex, beta-reaction
-
?
L-serine + indole
L-tryptophan + H2O
-
beta reaction
-
-
ir
L-serine + indole
L-tryptophan + H2O
-
-
-
-
?
L-serine + indole
L-tryptophan + H2O
-
-
-
-
?
L-serine + indole
L-tryptophan + H2O
-
-
-
?
L-serine + indole
L-tryptophan + H2O
-
beta-subunit of the bienzyme complex, beta-reaction
-
?
L-serine + indole
L-tryptophan + H2O
reaction is catalyzed by the beta-subunit, TrpB1 or TRpB2. TrpB1 is activated by the addition of the alpha-subunit TrpA and subsequent complex formation, whereas the activity of TrpB2 is not significantly affected by TrpA
-
-
?
L-serine + indole
L-tryptophan + H2O
the reaction is catalyzed by the tryptophan synthase beta-subunit paralogs TrpB1 and TrpB2
-
-
ir
L-serine + indole
L-tryptophan + H2O
-
-
-
-
?
L-serine + indole
L-tryptophan + H2O
-
-
-
?
L-serine + indole
L-tryptophan + H2O
-
beta-subunit of the bienzyme complex, beta-reaction
-
?
L-serine + indole
L-tryptophan + H2O
-
-
-
-
?
L-serine + indole
L-tryptophan + H2O
-
-
-
-
?
L-serine + indole
tryptophan + H2O
-
-
-
?
L-serine + indole
tryptophan + H2O
-
-
-
-
?
L-serine + indole
tryptophan + H2O
-
beta-subunit of the bienzyme complex, beta-reaction
-
?
L-threonine + 1-C-(indol-3-yl)glycerol 3-phosphate
(2S,3S)-beta-methyltryptophan + D-glyceraldehyde 3-phosphate + H2O
-
-
-
?
L-threonine + 1-C-(indol-3-yl)glycerol 3-phosphate
(2S,3S)-beta-methyltryptophan + D-glyceraldehyde 3-phosphate + H2O
-
-
-
?
L-threonine + 2-methylindole
2-methyl-(2S,3S)-beta-methyltryptophan + H2O
-
-
-
?
L-threonine + 2-methylindole
2-methyl-(2S,3S)-beta-methyltryptophan + H2O
-
-
-
-
?
L-threonine + 2-methylindole
2-methyl-(2S,3S)-beta-methyltryptophan + H2O
-
-
-
-
?
L-threonine + 4-fluoroindole
4-fluoro-(2S,3S)-beta-methyltryptophan + H2O
reaction of mutant I16V/E17G/I68V/F95L/F274S/T292S/T321A/V384A
-
-
?
L-threonine + 4-fluoroindole
4-fluoro-(2S,3S)-beta-methyltryptophan + H2O
-
-
-
-
?
L-threonine + 4-fluoroindole
4-fluoro-(2S,3S)-beta-methyltryptophan + H2O
-
-
-
-
?
L-threonine + 4-methylindole
4-methyl-(2S,3S)-beta-methyltryptophan + H2O
-
-
-
-
?
L-threonine + 4-methylindole
4-methyl-(2S,3S)-beta-methyltryptophan + H2O
-
-
-
-
?
L-threonine + 6-methylindole
6-methyl-(2S,3S)-beta-methyltryptophan + H2O
reaction of mutant I16V/E17G/I68V/F95L/F274S/T292S/T321A/V384A
-
-
?
L-threonine + 6-methylindole
6-methyl-(2S,3S)-beta-methyltryptophan + H2O
-
-
-
-
?
L-threonine + indole
(2S,3S)-beta-methyltryptophan + H2O
-
-
-
?
L-threonine + indole
(2S,3S)-beta-methyltryptophan + H2O
-
-
-
-
?
L-threonine + indole
(2S,3S)-beta-methyltryptophan + H2O
-
-
-
-
?
O-phospho-L-serine + indole
L-tryptophan + phosphate
-
-
-
-
?
O-phospho-L-serine + indole
L-tryptophan + phosphate
-
-
-
?
O-phospho-L-serine + indole
L-tryptophan + phosphate
-
-
-
-
?
additional information
?
-
-
the enzyme contains two functional domains: tryptophan synthase alpha (TRPA) catalyzes the conversion of indole glycerol phosphate to indole and tryptophan synthase beta (TRPB) catalyzes the conversion of indole plus serine to tryptophan
-
-
?
additional information
?
-
-
TrpB2 subunits of tryptophan synthase are O-phospho-L-serine dependent tryptophan synthases, whereas TrpB1 enzymes catalyze the L-serine dependent synthesis of tryptophan
-
-
?
additional information
?
-
-
allostery and substrate channeling
-
?
additional information
?
-
-
enzyme switches between open inactive conformation and closed active conformation, overview
-
?
additional information
?
-
-
the enzyme is involved in regulation/inhibition of Pseudomonas aeruginosa type III secretion system, T3SS, by inhibition of T3SS expression through tryptophan catabolites, overview. The T3SS system consists of 43 coordinately regulated genes encoding type III secretion and translocation machinery, regulatory factors, type III effectors and effector-specific chaperones
-
-
?
additional information
?
-
no substrate: 6-hydroxyindole
-
-
?
additional information
?
-
-
no substrate: 6-hydroxyindole
-
-
?
additional information
?
-
native tryptophan synthase can also catalyze a productive reaction with L-threonine, leading to (2S,3S)-beta-methyltryptophan. Substitution occurs in vitro with a 3.4fold higher catalytic efficiency for Ser over Thr using saturating indole. Threonine binds efficiently but decreases the affinity for indole and disrupts the allosteric signaling that regulates the catalytic cycle
-
-
?
additional information
?
-
native tryptophan synthase can also catalyze a productive reaction with L-threonine, leading to (2S,3S)-beta-methyltryptophan. Substitution occurs in vitro with a 3.4fold higher catalytic efficiency for Ser over Thr using saturating indole. Threonine binds efficiently but decreases the affinity for indole and disrupts the allosteric signaling that regulates the catalytic cycle
-
-
?
additional information
?
-
-
catalyzed reaction and structure of the tryptophan synthase complex, overview
-
-
?
additional information
?
-
TrpB2 subunits of tryptophan synthase are O-phospho-L-serine dependent tryptophan synthases, whereas TrpB1 enzymes catalyze the L-serine dependent synthesis of tryptophan
-
-
?
additional information
?
-
-
one-step synthesis of fluoro, chloro, bromo and methyltryptophans using a readily prepared bacterial cell lysate
-
-
?
additional information
?
-
-
allosteric communication, Ser178 is a critical residue in ligand-triggered signals between alpha and beta active sites
-
?
additional information
?
-
-
allosteric interactions that regulate substrate channeling and catalysis in the bienzyme complex are triggered by covalent ractions at the beta-site and binding of substrate/product to te alpha-site, transmission of the allosteric signals between the alpha- and beta-catalytic sites is modulated by an ensemble of weak bonding interactions consisting of salt bridges, hydrogen bonds, and van der Waals contacts that switch the subunits between open and closed conformations
-
?
additional information
?
-
-
allostery and substrate channeling
-
?
additional information
?
-
-
allostery and substrate channeling, synergism between binding interactions at the monovalent cation binding site, the formation of salt bridges to support allosteric communication between sites, ligand binding to the alpha-site, and the catalytic activities of the alpha- and beta-sites
-
?
additional information
?
-
-
allostery and substrate channeling, wild-type and mutant T183V
-
?
additional information
?
-
-
aniline, phenylhydrazine and methoxylamine react with the wild-type enzyme to form quinoid reaction intermediates, which then decay, enzyme shows conformational changes between the active closed and the inactive open form during substrate recognition and binding, Asp305 of the beta-subunit plays an important role
-
?
additional information
?
-
-
functional properties of one subunit are allosterically regulated by ligands of the other subunit, computer-assisted molecular modeling, alpha-subunit ligands do not bind to beta-subunit
-
?
additional information
?
-
-
reaction intermediates formed in the different reactions, conformational transition states regulate the activity and specificity of the enzyme complex
-
?
additional information
?
-
-
role of allosteric effectors indole-3-acetylglycine and indole-3-acetyl-L-aspartic acid in intersubunit communication, they bind to the alpha-subunit, inhibit it and cause conformational changes that influence the beta-subunit
-
?
additional information
?
-
-
substrate channeling, Thr170 occludes the tunnel connecting the alpha- and beta-active sites, accumulation of the intermediate indole during a single enzyme turnover
-
?
additional information
?
-
-
the alpha-beta subunit interaction plays a critical role both in the reciprocal activation of the individual subunits and in the allosteric regulation
-
?
additional information
?
-
-
the enzyme catalyzes the hydrogen-deuterium exchange of the pro-2R and pro-2S protons of [2-13C]glycine at pH 7.8, as well as the hydrogen-deuterium exchange of the alpha-proton of a range of L- and D-amino acids at pH 7.8, with the exception of tryptophan and norleucine, the stereospecificities of the first-order alpha-proton exchange rates are independent of the size and electronegativity of the mino acid R-group, similar second-order proteon exchnage rates with L-tryptophan and L-serine showing especially high stereospecificity
-
?
additional information
?
-
-
the enzyme possesses an intramolecular hydrophobic tunnel through which the metabolic intermediate indole is channeled from the alpha-subunit active site to the beta-subunit active site, mechanism and structural requirements, signaling by ligand-induced conformational changes
-
?
additional information
?
-
-
the intermediate product indole is transferred from the alpha- to the beta-site through a 25 A long hydrophobic tunnel
-
?
additional information
?
-
-
the intermediate product indole is transferred from the alpha- to the beta-site through a 25 A long hydrophobic tunnel
-
?
additional information
?
-
-
the intermediate product indole is transferred from the alpha- to the beta-site through a 25 A long hydrophobic tunnel
-
?
additional information
?
-
-
last 2 steps of the tryptophan biosynthesis
-
?
additional information
?
-
-
in the case of silica gel-encapsulated enzyme, the altered equilibrium distribution of tertiary conformations can not be totally ascribed to caging and viscosity effects, but might have a strong contribution from protein matrix intercation
-
-
?
additional information
?
-
-
structure-activity relationship dependent on temperature for alpha- and beta-subunit
-
?
additional information
?
-
-
both subunit TrpB1 and TrpB2 show trace levels of serine deaminase activity by converting L-serine to pyruvate and ammonia
-
-
?
additional information
?
-
both subunit TrpB1 and TrpB2 show trace levels of serine deaminase activity by converting L-serine to pyruvate and ammonia
-
-
?
additional information
?
-
both subunit TrpB1 and TrpB2 show trace levels of serine deaminase activity by converting L-serine to pyruvate and ammonia
-
-
?
additional information
?
-
-
indole is channeled to the active site of the beta-subunit, the TrpB2 homodimer has a high catalytic efficiency due to a low Km for indole, it functions as a rescue protein for indole to prevent the escape of the costly hydrophobic metabolite at the hig growing temperatures of the hyperthermophile
-
?
additional information
?
-
-
TrpB2 subunits of tryptophan synthase are O-phospho-L-serine dependent tryptophan synthases, whereas TrpB1 enzymes catalyze the L-serine dependent synthesis of tryptophan
-
-
?
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0.01 - 1.62
1-(indol-3-yl)glycerol 3-phosphate
0.02 - 1.4
1-C-(indol-3-yl)glycerol 3-phosphate
0.016
4-hydroxyindole
pH 7.0, 30°C
1.1
D-glyceraldehyde 3-phosphate
-
cosubstrate L-Trp, i.e. reverse reaction
0.01 - 0.316
O-phospho-L-serine
0.02
serine
-
serine deaminase reaction
additional information
additional information
-
0.01
1-(indol-3-yl)glycerol 3-phosphate
-
reaction of alpha2beta2 complex
0.013
1-(indol-3-yl)glycerol 3-phosphate
-
-
0.032
1-(indol-3-yl)glycerol 3-phosphate
-
cosubstrate L-Ser
0.04
1-(indol-3-yl)glycerol 3-phosphate
-
reaction of alpha subunit
0.07
1-(indol-3-yl)glycerol 3-phosphate
-
cosubstrate L-Ser
0.19
1-(indol-3-yl)glycerol 3-phosphate
-
pH 7.5, 80°C, recombinant (TrpA-TrpB1)2 tetrameric complex, alpha-reaction
0.5
1-(indol-3-yl)glycerol 3-phosphate
-
no cosubstrate
1.62
1-(indol-3-yl)glycerol 3-phosphate
-
pH 7.5, 80°C, recombinant TrpA, alpha-reaction
0.02
1-C-(indol-3-yl)glycerol 3-phosphate
cosubstrate L-serine, pH 8.0, temperature not specified in the publication
1.4
1-C-(indol-3-yl)glycerol 3-phosphate
cosubstrate L-threonine, pH 8.0, temperature not specified in the publication
0.000074
indole
recombinant isozyme AtTSBtype2, pH 8.2, 30°C
0.007
indole
-
recombinant isozyme TSB type 2, pH 8.2, 30°C
0.0076
indole
pH 7.5, 85°C, reaction catalyzed by TrpB2 in presence of subunit TrpA
0.0081
indole
pH 7.5, 85°C, reaction catalyzed by TrpB1
0.009
indole
mutant P12L/E17G/I68V/F274S/T292S/T321A, pH 8.0, 75°C
0.011
indole
-
cosubstrate L-Ser
0.011
indole
mutant M156T/N178D, pH 8.0, 60°C
0.012
indole
wild-type, pH 8.0, 60°C
0.018
indole
-
cosubstrate L-Ser, presence of 20 mM Na+
0.018
indole
mutant M149T/N171D, pH 8.0, 37°C
0.019
indole
wild-type, pH 8.0, 37°C
0.025
indole
-
pH 7.5, 80°C, recombinant (TrpA-TrpB1)2 tetrameric complex, beta-reaction
0.025
indole
mutant T292S, pH 8.0, 75°C
0.026
indole
mutant P19G/I69V/T292S, pH 8.0, 75°C
0.032
indole
mutant M145T/N167D, pH 8.0, 75°C
0.033
indole
wild-type, pH 8.0, 75°C
0.035
indole
pH 7.5, 85°C, reaction catalyzed by TrpB1 in presence of subunit TrpA
0.035
indole
pH 7.5, 85°C, he reaction is catalyzed by TrpB1
0.04
indole
-
pH 7.5, 80°C, recombinant TrpB1, beta-reaction
0.042
indole
mutant M144T/N166D, pH 8.0, 75°C
0.044
indole
-
cosubstrate L-Ser, presence of 20 mM Li+
0.048
indole
mutant P25L/P30G/I80V/L285S/T303S/T321A, pH 8.0, 60°C
0.05
indole
-
cosubstrate L-Ser
0.06
indole
-
cosubstrate L-Ser
0.0629
indole
pH 7.5, 85°C, reaction catalyzed by TrpB2
0.0629
indole
pH 7.5, 85°C, the reaction is catalyzed by the complex of TrpB1 and TrpA
0.067
indole
-
cosubstrate L-Ser, presence of 20 mM Cs+
0.07
indole
-
cosubstrate L-Ser
0.072
indole
mutant P14L/P19G/I69V/L274S/T292S, pH 8.0, 75°C
0.077
indole
wild-type, pH 8.0, 75°C
0.094
indole
-
37°C, beta-replacement, enzyme in solution
0.095
indole
-
cosubstrate L-Ser, presence of 20 mM K+
0.15
indole
-
37°C, beta-replacement, enzyme encapsulated in tetramethylorthosilicate-derived wet silica gels
0.16
indole
-
cosubstrate L-Ser
0.17
indole
-
cosubstrate D-glyceraldehyde 3-phosphate
0.59
indole
-
cosubstrate L-Ser
0.78
indole
alpha-subunit, mutant T183V/A185G, pH 7.6, 25°C
0.8
indole
alpha-subunit, mutant T183V/A158G, pH 7.6, 25°C
0.84
indole
alpha-subunit, mutant T183V/A67G, pH 7.6, 25°C
0.926
indole
wild-type, pH 7.6, 25°C
0.997
indole
-
mutant Q128A
1.013
indole
-
mutant T204A
1.1
indole
alpha-subunit, mutant T183V, pH 7.6, 25°C
1.485
indole
-
mutant S249A
1.5 - 2
indole
alpha-subunit, mutant T183V/A180G, pH 7.6, 25°C
1.7
indole
alpha-subunit, mutant T183V/A71G, pH 7.6, 25°C
1.84
indole
alpha-subunit, mutant A71G, pH 7.6, 25°C
2.083
indole
-
mutant S390A
2.342
indole
-
mutant S99A
2.86
indole
-
mutant N250A
2.906
indole
-
mutant Q364A
3.35
indole
alpha-subunit, mutant T183V/A59G, pH 7.6, 25°C
4.471
indole
-
mutant H100A
8.7
indole
subunit TrpB1, mutant P12L/E17G/I68V/F274S/T292S/T321A, pH 8.0, 75°C
11
indole
subunit TrpB1, mutant E17G/I68V/F274S/T292S/T321A, pH 8.0, 75°C
14
indole
subunit TrpB1, mutant T292S, pH 8.0, 75°C
20
indole
wild-type holoenzyme, pH 8.0, 75°C
77
indole
subunit TrpB1, wild-type, pH 8.0, 75°C
0.6
L-Ser
-
cosubstrate indole
5.3
L-Ser
-
cosubstrate indole
5.7
L-Ser
-
cosubstrate indole
0.0076
L-serine
subunit TrpB2 plus subunit TrpA, at pH 7.5 and 85°C
0.0081
L-serine
subunit TrpB2, at pH 7.5 and 85°C
0.035
L-serine
subunit TrpB1 plus subunit TrpA, at pH 7.5 and 85°C
0.14
L-serine
-
in the presence of 250 mM NaCl, at pH 8.5 and 25°C
0.27
L-serine
-
in the presence of 100 mM KCl, at pH 8.5 and 25°C
0.52
L-serine
-
in the presence of 250 mM NaCl, at pH 7.8 and 25°C
0.58
L-serine
-
in the presence of 100 mM KCl, at pH 7.8 and 25°C
0.6
L-serine
pH 8.0, temperature not specified in the publication
0.6
L-serine
wild-type holoenzyme, pH 8.0, 75°C
0.629
L-serine
subunit TrpB1, at pH 7.5 and 85°C
0.7
L-serine
subunit TrpB1, mutant P12L/E17G/I68V/F274S/T292S/T321A, pH 8.0, 75°C
0.84
L-serine
subunit TrpB1, mutant T292S, pH 8.0, 75°C
0.98
L-serine
-
37°C, beta-replacement, enzyme in solution
0.983
L-serine
-
mutant T204A
1.052
L-serine
-
mutant Q128A
1.16
L-serine
-
37°C, beta-elimination, enzyme in solution
1.17
L-serine
-
37°C, beta-replacement, enzyme encapsulated in tetramethylorthosilicate-derived wet silica gels
1.2
L-serine
subunit TrpB1, mutant E17G/I68V/F274S/T292S/T321A, pH 8.0, 75°C
1.2
L-serine
subunit TrpB1, wild-type, pH 8.0, 75°C
1.235
L-serine
-
mutant S249A
1.4
L-serine
-
mutant L166V, pH not specified in the publication, temperature not specified in the publication
1.41
L-serine
-
37°C, beta-elimination, enzyme encapsulated in tetramethylorthosilicate-derived wet silica gels
1.6
L-serine
-
without monovalent cations, at pH 6.5 and 25°C
1.6
L-serine
-
without monovalent cations, at pH 7.8 and 25°C
1.6
L-serine
-
wild-type, pH not specified in the publication, temperature not specified in the publication
1.683
L-serine
-
mutant S99A
1.85
L-serine
-
mutant N250A
1.89
L-serine
-
in the presence of 100 mM KCl, at pH 6.5 and 25°C
1.9
L-serine
-
in the presence of 100 mM CsCl, at pH 8.5 and 25°C
1.911
L-serine
-
mutant S390A
2.7
L-serine
-
without monovalent cations, at pH 8.5 and 25°C
2.9
L-serine
pH 7.0, 30°C
3.7
L-serine
-
pH 7.5, 80°C, recombinant (TrpA-TrpB1)2 tetrameric complex, beta-reaction
4
L-serine
-
mutant Q364A
4.78
L-serine
-
in the presence of 250 mM NaCl, at pH 6.5 and 25°C
5.6
L-serine
-
in the presence of 100 mM CsCl, at pH 7.8 and 25°C
6.2
L-serine
-
recombinant isozyme TSB type 2, pH 8.2, 30°C
9
L-serine
-
in the presence of 100 mM CsCl, at pH 6.5 and 25°C
15.8
L-serine
-
mutant H100A
35
L-serine
-
pH 7.5, 30°C
35
L-serine
recombinant isozyme AtTSBtype2, pH 8.2, 30°C
35
L-serine
isoform TrpB2i, pH 7.5, 60°C
50.2
L-serine
-
pH 7.5, 80°C
52
L-serine
-
mutant L166A, pH not specified in the publication, temperature not specified in the publication
110
L-serine
-
pH 7.5, 80°C, recombinant TrpB1, beta-reaction
151
L-serine
isoform TrpB2a, pH 7.5, 60°C
1.3
L-threonine
pH 8.0, temperature not specified in the publication
210
L-threonine
-
wild-type, pH not specified in the publication, temperature not specified in the publication
310
L-threonine
-
mutant L166V, pH not specified in the publication, temperature not specified in the publication
340
L-threonine
-
mutant L166A, pH not specified in the publication, temperature not specified in the publication
0.01
O-phospho-L-serine
-
pH 7.5, 30°C
0.014
O-phospho-L-serine
isoform TrpB2a, pH 7.5, 60°C
0.015
O-phospho-L-serine
isoform TrpB2i, pH 7.5, 60°C
0.316
O-phospho-L-serine
-
pH 7.5, 80°C
additional information
additional information
-
kinetics
-
additional information
additional information
-
kinetics
-
additional information
additional information
-
dissociation constants of the beta-subunit combined with the different subunits of wild-type and mutants
-
additional information
additional information
-
dissociation constants, kinetics
-
additional information
additional information
-
kinetic isotope effects with alpha-2H-L-Ser, and thermodynamics, wild-type and mutant
-
additional information
additional information
-
kinetics and temperature-dependence
-
additional information
additional information
-
kinetics for the wild-type and channel-impaired mutants
-
additional information
additional information
-
kinetics of formation of quinoid reaction intermediates in the beta-active site upon reaction with the substrates, pH-dependence
-
additional information
additional information
-
kinetics of proton release during beta-reaction, thermodynamic cycle of the interconversion of L-serine and alpha-aminoacrylate intermediate structures
-
additional information
additional information
-
kinetics of the hydrogen-deuterium exchange reactions
-
additional information
additional information
-
kinetics of wild-type enzyme complex and mutant betaA169L/betaC170W
-
additional information
additional information
-
kinetics, beta-reaction
-
additional information
additional information
-
kinetics, temperature-, and pH-dependence, and isotope effect at pH 7.0, not at pH 9.0, overview
-
additional information
additional information
-
kinetics, wild-type and mutant H86L enzymes
-
additional information
additional information
-
kinetics, wild-type and mutants, isotope effects and effector influence
-
additional information
additional information
-
steady state kinetics
-
additional information
additional information
-
thermodynamic parameters of subunit association, kinetics
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.00017 - 6
1-(indol-3-yl)glycerol 3-phosphate
1.4
indoline
-
overall-reaction, mutant D305A enzyme, pH 7.8, 25°C, in presence of 100 mM Cs+
5.4
L-Ser
-
cosubstrate indole
0.0007 - 0.61
L-threonine
0.015 - 0.414
O-phospho-L-serine
0.06
serine
-
serine deaminase reaction
additional information
L-serine
0.00017
1-(indol-3-yl)glycerol 3-phosphate
-
overall-reaction, pH 7.8, 25°C, mutant T183V enzyme
0.00059
1-(indol-3-yl)glycerol 3-phosphate
-
alpha-reaction, pH 7.8, 25°C, mutant T183V enzyme
0.063
1-(indol-3-yl)glycerol 3-phosphate
-
alpha-reaction, pH 7.8, 25°C, wild-type enzyme
0.16
1-(indol-3-yl)glycerol 3-phosphate
-
overall-reaction, mutant R141A, pH 7.8, 25°C
0.174
1-(indol-3-yl)glycerol 3-phosphate
-
pH 7.5, 80°C, recombinant TrpA, alpha-reaction
0.28
1-(indol-3-yl)glycerol 3-phosphate
-
reaction of alpha subunit
0.3
1-(indol-3-yl)glycerol 3-phosphate
-
alpha-reaction, wild-type enzyme, pH 7.8, 25°C
0.3
1-(indol-3-yl)glycerol 3-phosphate
-
alpha-reaction, wild-type, and overall-reaction, wild-type and mutant D305A, pH 7.8, 25°C
0.36
1-(indol-3-yl)glycerol 3-phosphate
-
alpha-reaction, mutant R141A, pH 7.8, 25°C
0.44
1-(indol-3-yl)glycerol 3-phosphate
-
alpha-reaction, mutant D305A enzyme, pH 7.8, 25°C
0.44
1-(indol-3-yl)glycerol 3-phosphate
-
alpha-reaction, mutant D305A, pH 7.8, 25°C
2.61
1-(indol-3-yl)glycerol 3-phosphate
-
overall-reaction, pH 7.8, 25°C, wild-type enzyme
3 - 6
1-(indol-3-yl)glycerol 3-phosphate
-
overall-reaction, pH 7.8, 25°C, wild-type enzyme
3.7
1-(indol-3-yl)glycerol 3-phosphate
-
reaction of alpha2beta2 complex
5.6
1-(indol-3-yl)glycerol 3-phosphate
-
pH 7.5, 80°C, recombinant (TrpA-TrpB1)2 tetrameric complex, alpha-reaction
0.003
indole
alpha-subunit, mutant T183V/A71G, pH 7.6, 25°C
0.007
indole
recombinant isozyme AtTSBtype2, pH 8.2, 30°C
0.007
indole
alpha-subunit, mutant T183V, pH 7.6, 25°C
0.007
indole
alpha-subunit, mutant T183V/A158G, pH 7.6, 25°C
0.007
indole
alpha-subunit, mutant T183V/A180G, pH 7.6, 25°C
0.007
indole
alpha-subunit, mutant T183V/A185G, pH 7.6, 25°C
0.01
indole
alpha-subunit, mutant T183V/A59G, pH 7.6, 25°C
0.0102
indole
-
recombinant isozyme TSB type 2, pH 8.2, 30°C
0.011
indole
alpha-subunit, mutant T183V/A67G, pH 7.6, 25°C
0.02
indole
alpha-subunit, mutant A71G, pH 7.6, 25°C
0.033
indole
-
beta-reaction, mutant R141A, pH 7.8, 25°C
0.074
indole
wild-type, pH 8.0, 60°C
0.095
indole
alpha-subunit, wild-type, pH 7.6, 25°C
0.11
indole
mutant P14L/P19G/I69V/L274S/T292S, pH 8.0, 75°C
0.16
indole
wild-type, pH 8.0, 37°C
0.31
indole
subunit TrpB1, wild-type, pH 8.0, 75°C
0.31
indole
wild-type, pH 8.0, 75°C
0.34
indole
mutant M149T/N171D, pH 8.0, 37°C
0.34
indole
mutant M156T/N178D, pH 8.0, 60°C
0.39
indole
pH 7.5, 85°C, reaction catalyzed by TrpB2
0.39
indole
pH 7.5, 85°C, reaction catalyzed by TrpB2 in presence of subunit TrpA
0.51
indole
mutant P25L/P30G/I80V/L285S/T303S/T321A, pH 8.0, 60°C
0.83
indole
mutant M144T/N166D, pH 8.0, 75°C
0.88
indole
-
beta-reaction, mutant D305A, pH 7.8, 25°C
1
indole
wild-type holoenzyme, pH 8.0, 75°C
1.04
indole
pH 7.5, 85°C, reaction catalyzed by TrpB1
1.04
indole
pH 7.5, 85°C, the reaction is catalyzed by the complex of TrpB1 and TrpA
1.1
indole
subunit TrpB1, mutant T292S, pH 8.0, 75°C
1.28
indole
wild-type, pH 8.0, 75°C
1.6
indole
-
beta-reaction, wild-type, pH 7.8, 25°C
2.2
indole
subunit TrpB1, mutant E17G/I68V/F274S/T292S/T321A, pH 8.0, 75°C
2.531
indole
-
mutant H100A
2.64
indole
-
cosubstrate L-Ser
2.9
indole
mutant P12L/E17G/I68V/F274S/T292S/T321A, pH 8.0, 75°C
2.9
indole
subunit TrpB1, mutant P12L/E17G/I68V/F274S/T292S/T321A, pH 8.0, 75°C
3.3
indole
-
beta-reaction, pH 7.8, 25°C, mutant T183V enzyme
3.3
indole
-
beta-reaction, pH 7.8, 25°C, wild-type enzyme
3.3
indole
-
37°C, beta-replacement, enzyme encapsulated in tetramethylorthosilicate-derived wet silica gels
3.3
indole
mutant M145T/N167D, pH 8.0, 75°C
3.41
indole
-
cosubstrate L-Ser, presence of 20 mM Na+
3.46
indole
pH 7.5, 85°C, reaction catalyzed by TrpB1 in presence of subunit TrpA
3.46
indole
pH 7.5, 85°C, he reaction is catalyzed by TrpB1
4.2
indole
-
pH 7.5, 80°C, recombinant TrpB1, beta-reaction
4.27
indole
-
cosubstrate L-Ser, presence of 20 mM Li+
4.51
indole
-
beta-reaction, pH 7.8, 25°C, wild-type enzyme
4.85
indole
-
cosubstrate L-Ser, presence of 20 mM K+
5.24
indole
-
beta-reaction, pH 7.8, 25°C, mutant T183V enzyme
5.4
indole
-
cosubstrate L-Ser
5.44
indole
-
cosubstrate L-Ser, presence of 20 mM Cs+
5.8
indole
mutant T292S, pH 8.0, 75°C
6.08
indole
-
beta-reaction, mutant D305A, pH 7.8, 25°C
6.427
indole
-
mutant Q364A
9.8
indole
mutant P19G/I69V/T292S, pH 8.0, 75°C
10
indole
-
pH 7.5, 80°C, recombinant (TrpA-TrpB1)2 tetrameric complex, beta-reaction
10.1
indole
-
37°C, beta-replacement, enzyme in solution
21.14
indole
-
mutant S99A
26.84
indole
-
mutant S249A
34.73
indole
-
mutant S390A
40.18
indole
-
mutant N250A
50.65
indole
-
mutant T204A
68.43
indole
-
mutant Q128A
0.00017
L-serine
-
overall-reaction, pH 7.8, 25°C, mutant T183V enzyme
0.0155
L-serine
recombinant isozyme AtTSBtype2, pH 8.2, 30°C
0.016
L-serine
-
pH 7.5, 30°C
0.0223
L-serine
-
recombinant isozyme TSB type 2, pH 8.2, 30°C
0.032
L-serine
isoform TrpB2a, pH 7.5, 60°C
0.0817
L-serine
-
mutant L166V, pH not specified in the publication, temperature not specified in the publication
0.15
L-serine
-
37°C, beta-elimination, enzyme encapsulated in tetramethylorthosilicate-derived wet silica gels
0.16
L-serine
-
37°C, beta-replacement, enzyme encapsulated in tetramethylorthosilicate-derived wet silica gels
0.183
L-serine
-
mutant L166A, pH not specified in the publication, temperature not specified in the publication
0.2
L-serine
isoform TrpB2i, pH 7.5, 60°C
0.24
L-serine
-
without monovalent cations, at pH 6.5 and 25°C
0.26
L-serine
-
37°C, beta-elimination, enzyme in solution
0.35
L-serine
-
wild-type, pH not specified in the publication, temperature not specified in the publication
0.39
L-serine
subunit TrpB2 plus subunit TrpA, at pH 7.5 and 85°C
0.39
L-serine
subunit TrpB2, at pH 7.5 and 85°C
0.4
L-serine
-
overall-reaction, mutant D305A enzyme, pH 7.8, 25°C, in presence of Na+
0.44
L-serine
-
pH 7.5, 80°C
0.8
L-serine
-
overall-reaction, mutant D305A enzyme, pH 7.8, 25°C, in presence of K+
0.88
L-serine
-
beta-reaction and overall-reaction, mutant D305A enzyme, pH 7.8, 25°C
0.91
L-serine
-
without monovalent cations, at pH 7.8 and 25°C
1
L-serine
pH 8.0, temperature not specified in the publication
1.04
L-serine
subunit TrpB1, at pH 7.5 and 85°C
1.37
L-serine
-
without monovalent cations, at pH 8.5 and 25°C
1.6
L-serine
-
beta-reaction, wild-type enzyme, pH 7.8, 25°C
1.9
L-serine
-
in the presence of 250 mM NaCl, at pH 6.5 and 25°C
1.9
L-serine
-
in the presence of 250 mM NaCl, at pH 8.5 and 25°C
1.987
L-serine
-
mutant H100A
2
L-serine
-
overall-reaction, wild-type enzyme, pH 7.8, 25°C
2.08
L-serine
-
in the presence of 100 mM KCl, at pH 6.5 and 25°C
2.61
L-serine
-
overall-reaction, pH 7.8, 25°C, wild-type enzyme
2.8
L-serine
-
in the presence of 250 mM NaCl, at pH 7.8 and 25°C
3 - 6
L-serine
-
overall-reaction, pH 7.8, 25°C, wild-type enzyme
3.3
L-serine
-
beta-reaction, pH 7.8, 25°C, mutant T183V enzyme
3.3
L-serine
-
beta-reaction, pH 7.8, 25°C, wild-type enzyme
3.46
L-serine
subunit TrpB1 plus subunit TrpA, at pH 7.5 and 85°C
3.462
L-serine
-
mutant Q364A
3.8
L-serine
-
pH 7.5, 80°C, recombinant TrpB1, beta-reaction
4
L-serine
-
in the presence of 100 mM KCl, at pH 8.5 and 25°C
4.51
L-serine
-
beta-reaction, pH 7.8, 25°C, wild-type enzyme
4.8
L-serine
-
in the presence of 100 mM KCl, at pH 7.8 and 25°C
5
L-serine
-
overall-reaction, mutant D305A enzyme, pH 7.8, 25°C, in presence of NH4+
5.24
L-serine
-
beta-reaction, pH 7.8, 25°C, mutant T183V enzyme
6
L-serine
-
in the presence of 100 mM CsCl, at pH 6.5 and 25°C
6.08
L-serine
-
beta-reaction and overall-reaction, mutant D305A enzyme, pH 7.8, 25°C
6.15
L-serine
-
in the presence of 100 mM CsCl, at pH 8.5 and 25°C
7.106
L-serine
-
mutant N250A
7.8
L-serine
-
overall-reaction, mutant D305A enzyme, pH 7.8, 25°C, in presence of Cs+
8
L-serine
-
overall-reaction, wild-type enzyme, pH 7.8, 25°C, in presence of Na+
8
L-serine
-
pH 7.5, 80°C, recombinant (TrpA-TrpB1)2 tetrameric complex, beta-reaction
8.2
L-serine
-
37°C, beta-replacement, enzyme in solution
8.7
L-serine
-
in the presence of 100 mM CsCl, at pH 7.8 and 25°C
10.3
L-serine
-
overall-reaction, wild-type enzyme, pH 7.8, 25°C, in presence of NH4+
10.69
L-serine
-
mutant S249A
12
L-serine
-
overall-reaction, wild-type enzyme, pH 7.8, 25°C, in presence of K+
13.22
L-serine
-
mutant S99A
14
L-serine
-
overall-reaction, wild-type enzyme, pH 7.8, 25°C, in presence of Cs+
16.35
L-serine
-
mutant T204A
20.48
L-serine
-
mutant S390A
21.47
L-serine
-
mutant Q128A
0.0007
L-threonine
-
wild-type, pH not specified in the publication, temperature not specified in the publication
0.0035
L-threonine
-
mutant L166A, pH not specified in the publication, temperature not specified in the publication
0.007
L-threonine
-
mutant L166V, pH not specified in the publication, temperature not specified in the publication
0.61
L-threonine
pH 8.0, temperature not specified in the publication
0.015
O-phospho-L-serine
-
pH 7.5, 30°C
0.015
O-phospho-L-serine
isoform TrpB2a, pH 7.5, 60°C
0.3
O-phospho-L-serine
isoform TrpB2i, pH 7.5, 60°C
0.414
O-phospho-L-serine
-
pH 7.5, 80°C
additional information
L-serine
-
in the presence of 100 mM CsCl, at pH 8.5 and 25°C
additional information
additional information
-
activities of wild-type and mutants in presence of different effectors
-
additional information
additional information
-
turnover of wild-type and mutant D305A in presence of different effectors for alpha-, and beta-reaction
-
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heterodimer
-
x-ray crystallography
homodimer
crystal structure
?
-
x * 33000 (alpha) + x * 51000 (beta), SDS-PAGE
?
-
alpha subunit, x * 28800, calculation from amino acid sequence, x * 31000, SDS-PAGE
?
-
2 * 39700-41000, beta subunit, 1 * 82000, beta2 subunit, ultracentrifugation, SDS-PAGE
?
-
x * 25600-26300, alpha subunit, ultracentrifugation, SDS-PAGE
?
x * 75500, calculated from sequence
?
-
89000, B2 subunit, polyacrylamide gel electrophoresis, 2 * 43000, B subunit, SDS-PAGE
dimer
-
2 * 50000, SDS-PAGE
dimer
-
2 * 42500, recombinant beta-subunit, SDS-PAGE
dimer
-
2 * 74000, SDS-PAGE
dimer
-
2 * 77000, sedimentation equilibrium in 6 M guanidine hydrochloride
dimer
-
recombinant beta-subunit, SDS-PAGE and gel filtration
dimer
-
TrpB2 does not bind to the alpha-subunit and forms homodimers, TrpB1 alone forms homodimers
heterotetramer
-
-
heterotetramer
-
2 * 25500 + 2 * 41750, gel filtration
heterotetramer
2 * 27700 (subunit TrpA) + 2 * 42600 (subunit TrpB1), calculated from sequence, tryptophan synthase is composed of subunit TrpA and subunit TrpB. Thermococcus kodakarensis possess two paralogs of subunit B, TrpB1 and TrpB2. TrpB2 catalyzes the TrpB reaction but does not interact with TrpA as in the case of TrpB1
heterotetramer
2 * 27700 (subunit TrpA) + 2 * 49300 (subunit TrpB2), calculated from sequence, tryptophan synthase is composed of subunit TrpA and subunit TrpB. Thermococcus kodakarensis possess two paralogs of subunit B, TrpB1 and TrpB2. TrpB2 catalyzes the TrpB reaction but does not interact with TrpA as in the case of TrpB1
heterotetramer
2 * 20800 + 2 * 67400, heterotetramer from subunits TrpA and TrpB1, SDS-PAGE
heterotetramer
2 * 27700 + 2 * 42600, heterotetramer from subunits TrpA and TrpB1, calculated from amino acid sequence
heterotetramer
alpha,beta,beta,alpha heterotetramer
monomer
-
1 * 29000, alpha-subunit, SDS-PAGE
monomer
-
1 * 27500, recombinant alpha-subunit, SDS-PAGE
monomer
-
recombinant alpha-subunit, SDS-PAGE and gel filtration
monomer
-
TrpA alone forms monomers
tetramer
-
alpha2beta2 complex
tetramer
-
alpha2beta2 enzyme complex
tetramer
-
2 * 275000 + 2 * 42500, recombinant alpha2beta2 enzyme complex, SDS-PAGE
tetramer
-
alpha2beta2 complex
tetramer
-
alpha2beta2 complex, structural organization
tetramer
-
alpha2beta2 complex, structure model
tetramer
-
alpha2beta2 complex, structure-function relationship
tetramer
-
alpha2beta2 enzyme complex
tetramer
-
X-ray crystallography, consists of an alpha2beta2 bienzyme complex with alphabeta dimeric units assembled as the tetrameric species via the beta-beta subunit interface, each alpha-subunit catalyzes the cleavage of 3-indole-D-glycerol 3'-phosphate to indole and D-glyceraldehyde 3-phosphate, the pyridoxal phosphate requiring beta-subunit catalyzes a beta-replacement reaction in which indole replaces the hydroxyl of L-Ser, giving L-Trp
tetramer
-
alpha2beta2 enzyme complex, SDS-PAGE and gel filtration
tetramer
-
alphabetabetaalpha complex of TRpA and TrpB1, sedimentation equilibrium
additional information
-
sequence alignment of alpha-subunit
additional information
-
sequence alignment of alpha-subunit
additional information
-
sequence alignment of alpha-subunit
additional information
-
activities of alpha and beta subunits are coordinated by allosteric interactions
additional information
-
sequence alignment of alpha-subunit
additional information
-
kinetics of assembly of subunits
additional information
-
determination of secondary structure of the isolated alpha-subunit by NMR measurements, the alpha-subunit is a 29 kDa TIM barrel protein, tertiary interactions, overview
additional information
-
dimer formation seems to be associated with the formation of protein aggregates in vivo
additional information
-
molecular dissection of the alpha-subunit
additional information
-
NMR measurement and determination of wild-type and mutant enzyme structures, complexed with L-tryptophane, in presence or absence of allosteric ligands, such as Na+, NH4+, Cs+, and DL_alpha-glycerol 3-phosphate, overview
additional information
-
structural analysis, wild-type and mutant beta-subunit dimers, hairpin loop in the beta-subunit, overview
additional information
-
the alpha-subunit contains no disulfide bond, conformational stabilization mechanism
additional information
-
the alpha-subunit is a TIM barrel protein, structure analysis
additional information
-
(betaalpha)8 TIM barrel protein
additional information
-
sequence alignment of alpha-subunit
additional information
-
sequence alignment of alpha-subunit
additional information
-
sequence alignment of alpha-subunit
additional information
-
high association constant for the hyperthermophile enzyme subunits, pH-dependence of the molecular weights
additional information
-
the hyperthermophilic archaeon Sulfolobus solfataricus does not contain a TrpB1 protein, as other prototypical tryptophan synthases, but instead two members of the phylogenetically distinct family of TrpB2 proteins, which are encoded within, sTrpB2i, and outside, sTrpB2a, the tryptophan operon. sTrpB2a does not functionally or structurally interact with sTrpA, whereas sTrpB2i substantially activates sTrpA in a unidirectional manner. In the absence of catalysis, no physical complex between sTrpB2i and sTrpA is detected. Stoichiometry of the complex is 1 subunit of sTrpA per 2 subunits of sTrpB2i, which corresponds to a alphabetabeta quaternary structure and testifies to a strong negative cooperativity for the binding of the alpha-monomers to the betabeta-dimer. The alphabetabeta complex remains stable during the whole catalytic cycle and disintegrates into alpha- and betabeta-subunits upon the release of the reaction product tryptophan, structure-function relationship, overview
additional information
-
sequence alignment of alpha-subunit
additional information
-
activities of alpha and beta subunits are coordinated by allosteric interactions
additional information
-
sequence alignment of alpha-subunit
additional information
-
conformational states, overview, subunit dissociation in presence of guanidinium hydrochloride
additional information
-
crystal structure analysis, structure-function relationship, overview
additional information
-
salt-bridges extending between the subunits involve alphaAsp56, betaLys167, beta-Asp305, and betaR141
additional information
-
structural analysis, wild-type and mutant beta-subunit dimers, hairpin loop in the beta-subunit, overview
additional information
-
structure and conformation regulating the activity and allosteric communication in the enzyme complex, modeling of the high activity closed form and the low activity open form
additional information
-
structure and conformation regulating the activity and allosteric communication in the enzyme complex, modeling of the high activity closed form and the low activity open form dependent on temperature, conversion from the open to the closed form at high temperature
additional information
-
structure models
additional information
-
three-dimensional structure of the alphaloop6 in the closed conformation with hydrogen bond between Gly181 ans Ser178
additional information
-
structure and conformation of the alpha/beta-complex, the isolated monomers show structural flexibility versus the alpha/beta-dimeric unit, H-bond formations in different states, overview
additional information
-
recombinantly expressed alpha-subunit forms monomers of 26.7 kDa, while the recombinant beta-subunits B1 and B2 both form dimers of 49.4 and 61.7 kDa, respectively
additional information
-
sequence alignment of alpha-subunit
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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
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
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
-
crystal structure of tryptophan synthase beta2 subunit determined at 2.2 A resolution, hanging drop vapour diffusion method. Crystals belong to the orthorhombic space group P2(1)2(1)2(1) with unit cell dimensions of a = 84.8 A, b = 110.5 A, c = 160.0 A
hanging drop vapour diffusion method, crystal structure of the alpha2beta2 complex, crystals belong to the orthorhombic space group of P2(1)2(1)2(1) with unit cell dimensions of a = 89.1 A, b = 220.3 A, c = 292.6 A
-
purified recombinant alpha-subunit, hanging drop vapour diffusion method, 10°C, reservoir solution: 0.1 M MES-NaOH, pH 6.5, 12% PEG 20000, X-ray diffraction structure determination and analysis at 2.0 A resolution
wild-type in complex with L-threonine, to 1.54 A. L-threonine binds non-covalently, no formation of an electrophilic amino-acrylate intermediate. With mutant I16V/E17G/I68V/F95L/F274S/T292S/T321A/V384A, the species is formed
crystal structures of the alpha-subunit of tryptophan synthase alone and in the alpha2beta2 complex
-
crystallization of wild-type and mutant S178P in presence or absence of alpha-subunit ligands, structure comparison
-
crystallization of wild-type enzyme alone and complexed with L-serine and 3-indolylpropanol 3'-phosphate, and of mutant T183V complexed with L-serine, 1-(indol-3-yl)glycerol 3-phosphate, and 3-indolylpropanol 3'-phosphate, hanging drop method in the dark at room temperature, equal volumes of protein solution, containing 10 mg/ml protein, 50 mM Na-bicine, pH 7.8, 10 mM Na-EDTA, 1 mM dithioerythritol, 0.02 mM pyridoxal 5'-phosphate, and of reservoir solution, containing 50 mM Na-bicine, pH 7.8, 5 mM dithioerythritol, 5 mM Na-EDTA, 0.1 mM pyridoxal 5'-phosphate, 2 mM spermine, 8-12% w/v PEG 8000, X-ray diffraction structure determination and analysis at different resolutions 1.45-2.3 A, comparison of crystal structures of the different complexes
-
hanging drop method, 10 mg/ml purified recombinant mutant S178P enzyme in 50 mM bicine, pH 7.8, with equal volume of reservoir solution: 50 mM bicine, 1 mM EDTA, 12% w/v PEG 8000, 1.4 mM spermine, pH 7.8, 21°C, structure determination and functional investigation by polarized absorption microspectrophotometry
-
hanging drop vapour diffusion method
-
in complex with inhibitor N-(4'-trifluoro-methoxybenzenesulfonyl)-2-amino-ethyl phosphate
molecular dynamics simulations. The unprotonated pyridine nitrogen can form an H-bond with Ser377, which stabilizes the PLP ring structure. When the pyridoxyl phenolic oxygen is unprotonated, the polar side chain of Gln114 moves toward the negatively charged oxygen, which affects the movements of the water molecules around the active site and induces the switch to the open conformation of the beta subunit. The carboxylate oxygens typically form stable H-bonds with Thr110, Gly111, and His115
purified enzyme complexed with allosteric effectors indole-3-acetylglycine and indole-3-acetyl-L-aspartic acid, hanging drop method, in the dark at room temperature, equal volumes of protein and reservoir solution, the latter containing 9-12% PEG 8000, 1.5 mM spermine, 1 mM EDTA, 50 mM bicine, pH 7.8, X-ray diffraction structure determination and analysis at 2.5 A resolution, modeling
-
purified mutant A169L/C170W complexed with the alpha-active site substrate analogue 5-fluoro-indole-propanol-phosphate, X-ray diffraction structure determination and analysis at 2.25 A resolution
-
purified recombinant enzyme complex, structure determination and analysis
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purified recombinant enzyme in complex with potential alpha-reaction phosphonate inhibitors, 5-10 mg/ml protein mixed with 1 mM inhibitor, in 50 mM bicine, 1 mM Na-EDTA, 0.8-1.5 mM spermine, 12% PEG 4000, to pH 7.8 with NaOH, X-ray diffraction structure determination and analysis at 2.3 A resolution or higher
-
purified recombinant wild-type enzyme alone or in complex with alpha-subunit substrate analogue indole propanol phosphate, 10 mg/ml in 50 mM bicine, pH 7.8, 10 mM Na-EDTA, 0.02 mM pyridoxal 5'-phosphate, 1 mM dithioerythritol, in the dark at room temperature, hanging drop method, equal volumes of protein and reservoir solution, the latter containing 50 mM bicine, pH 7.8, 5 mM dithioerytritol, 5 mM Na-EDTA, 0.1 mM pyridoxal 5'-phosphate, 2 mM spermine, 2 mM NaN3, and 8-12% w/v PEG 8000, with or without 7 mM indole propanol phosphate, X-ray diffraction structure determination and analysis at 1.4 A resolution, structure modeling
-
single-molecule stochastic model of the enzyme, with the transition state constants deduced from the experimental data available. The model yields direct theoretical evidence for intramolecular synchronization phenomena
soaking native crystals for 10 min in a solution containing 90 mM Bis-Tris-propane (pH 7.8), 150 mM NaCl, 15% (w/v) PEG 8000, and 20% glycerol
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structure and function of alpha subunit, beta subunit, alpha2beta2 complex
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structures of tryptophan synthase crystallized with varying numbers of amphipathic N-(4'-trifluoromethoxybenzoyl)-2-aminoethyl phosphate. One of the ligands threads into the tunnel from the beta-site and reveals a distinct hydrophobic region. The N-(4'-trifluoromethoxybenzoyl)-2-aminoethyl phosphate phosphoryl group fits into a polar pocket of the beta-subunit active site. One portion of the tunnel binds clusters of water molecules, whereas waters are not observed in the nonpolar N-(4'-trifluoromethoxybenzoyl)-2-aminoethyl phosphate binding region of the tunnel. Hydrophobic molecules can freely diffuse between the alpha- and beta-sites via the tunnel, while water does not. Exclusion of water may serve to inhibit reaction of water with the alpha-aminoacrylate intermediate to form ammonium ion and pyruvate
vapor diffusion method, using 1 mM dithiothreitol, 0.04% (w/v) NaN3, and 12% (w/v) polyethylene glycol 8000
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sitting drop vapor diffusion method, using 0.1M HEPES-Na, pH 7.5, 2% (v/v) polyethylene glycol 400 and 2 M ammonium sulfate, at 4°C
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crystal structure of alpha-subunit of tryptophan synthase, oil batch method, discussion of the thermostabilization mechanism of the tryptophan synthase alpha-subunit on the basis of crystal structures and DSC data of the alpha-subunit orthologs from mesophilic, extreme thermophilic, and hyperthermophilic organisms
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M156T/N178D
5fold increase in catalytic efficiency
P25L/P30G/I80V/L285S/T303S/T321A
18fold increase in catalytic efficiency
A71G
mutation in alpha-subunit, about 10fold decrease in kcat/Km value compared to wild-type alpha subunit
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
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
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
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
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
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
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
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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
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
P57A
-
increase of activity of the alpha2beta2 complex
R275A
-
beta-subunit dimers, 37% reduced activity compared to the wild-type enzyme
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
T24A/F139W
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oligonucleotide-directed mutagenesis, recombinant alpha-subunit mutant, forms dimers
T24K/F139W
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oligonucleotide-directed mutagenesis, recombinant alpha-subunit mutant, forms dimers
T24L/F139W
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oligonucleotide-directed mutagenesis, recombinant alpha-subunit mutant, forms monomers
T24M/F139W
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oligonucleotide-directed mutagenesis, recombinant alpha-subunit mutant, forms monomers
T24S/F139W
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oligonucleotide-directed mutagenesis, recombinant alpha-subunit mutant, forms dimers
V23A
mutant lacks the hundreds of milliseconds unfolding reaction under strongly refolding conditions
V276A
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beta-subunit dimers, 46% reduced activity compared to the wild-type enzyme
V276A/K283A
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beta-subunit dimers, 48% reduced activity compared to the wild-type enzyme
Y173F
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oligonucleotide-directed mutagenesis, gene trpA, alpha-subunit residue exchange, altered fluorescence and folding properties
Y175F
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oligonucleotide-directed mutagenesis, gene trpA, alpha-subunit residue exchange, altered fluorescence and folding properties
Y279A
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beta-subunit dimers, 50% reduced activity compared to the wild-type enzyme
Y279F
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beta-subunit dimers, 33% reduced activity compared to the wild-type enzyme
Y279L
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beta-subunit dimers, 48% reduced activity compared to the wild-type enzyme
Y279P
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beta-subunit dimers, 46% reduced activity compared to the wild-type enzyme
H100A
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Km (indole), (L-serine) higher than wild-type, kcat (indole), (L-serine) significantly decreased compared to wild-type
N250A
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Km (indole), (L-serine) higher than wild-type, kcat (indole), (L-serine) lower compared to wild-type
Q128A
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Km (indole), (L-serine) higher than wild-type, kcat (indole) slightly lower than wild-type, kcat (L-serine) lower compared to wild-type
Q364A
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Km (indole), (L-serine) higher than wild-type, kcat (indole), (L-serine) significantly decreased compared to wild-type
S249A
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Km (indole), (L-serine) higher than wild-type, kcat (indole), (L-serine) lower compared to wild-type
S390A
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Km (indole), (L-serine) higher than wild-type, kcat (indole), (L-serine) lower compared to wild-type
S99A
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Km (indole), (L-serine) higher than wild-type, kcat (indole), (L-serine) lower compared to wild-type
T204A
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Km (indole), (L-serine) higher than wild-type, kcat (indole), (L-serine) lower compared to wild-type
up
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PtINS has about two to fivefold higher transcript level than that of PtTSA (tryptophan synthase alpha-subunit). After treatment with 2,1,3-benzothiadiazole the relative transcript level of PtINS (indole synthase) over PtTSA (tryptophan synthase alpha-subunit) is significantly enhanced in the plant
E17G/I68V/F274S/T292S/T321A
mutation in subunit TrpB1, 50fold increase of catalytic efficiency of isolated beta subunit
I16V/E17G/I68V/F95L/F274S/T292S/T321A/V384A
significant increase in activity with L-threonine
M144T/N166D
5fold increase in catalytic efficiency
P12L/E17G/I68V/F274S/T292S/T321A
T292S
mutation in subunit TrpB1, 20fold increase of catalytic efficiency of isolated beta subunit
S206C
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site-directed mutagenesis of subunit sTrpA, complex formation with subunit TrpB2i compared to wild-type TrpA
S229C
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site-directed mutagenesis of subunit sTrpA, complex formation with subunit TrpB2i compared to wild-type TrpA
W65F
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site-directed mutagenesis of subunit sTrpA, complex formation with subunit TrpB2i compared to wild-type TrpA
W88F
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site-directed mutagenesis of subunit sTrpA, complex formation with subunit TrpB2i compared to wild-type TrpA
A169L/C170W
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mutants of beta-subunit residues, altered kinetic properties and conformation
D124A
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mutation significantly perturbs the secondary and tertiary structure
D130A
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mutation significantly perturbs the secondary and tertiary structure
D13N/F22C/T24A/K35E/D46N/D56N/P62S/E90K/G98C/L177D/Q210L/A222T
the mutant shows phosphoribosylanthranilate isomerase activity
D13N/F22C/T24A/K35E/D56N/P62S/E90K/G98C/L144I/L177D/Q210L/I240V
the mutant shows phosphoribosylanthranilate isomerase activity
D13N/F22C/T24A/K35E/D56N/P62S/G98C/L177D/Q210L
the mutant shows phosphoribosylanthranilate isomerase activity
D13N/F22C/T24A/T39A/D60N/G61S/P62S/N66S/E90K/G98C/L177D/Q210L/A222T/I240V
the mutant shows phosphoribosylanthranilate isomerase activity
D305N
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site-directed mutagenesis, residue is involved in formation of salt bridges between the different subunits, kinetic and structural, conformational alterations, altered signaling by ligand binding, overview
D46A
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mutation significantly perturbs the secondary and tertiary structure
D60Y
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mutation inhibits the ligand-induced transition of the alpha subunit from an open to a closed conformation that serves to block the tunnel for the metabolite chanelling
E109A
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catalytic activity with beta-chloro-L-Ala, but negligible activity with L-Ser, beta subunit
E49F
-
mutation inhibits the ligand-induced transition of the alpha subunit from an open to a closed conformation that serves to block the tunnel for the metabolite chanelling
F22C/T24A/K35E/D56N/P62S/E90K/G98C
the mutant shows phosphoribosylanthranilate isomerase activity
F22C/T24A/K35E/D56N/P62S/E90K/L144I/L177D/I240V
the mutant shows phosphoribosylanthranilate isomerase activity
F22C/T24A/K35E/T39A/D56N/G61S/E90K/G98C/L177D/Q210L/I240V
the mutant shows phosphoribosylanthranilate isomerase activity
F22Y/T39A/G61S/G98C/D161V/Y203N/A222T
the mutant shows phosphoribosylanthranilate isomerase activity
F280A
-
beta-subunit dimers, unaltered activity compared to the wild-type enzyme
F280G
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beta-subunit dimers, 72% reduced activity compared to the wild-type enzyme
F280P
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beta-subunit dimers, 94% reduced activity compared to the wild-type enzyme
G181A
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2fold decrease of activity compared to the wild type enzyme
G181F
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mutant shows a significant change in the alphaloop6 structure
G181V
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mutant shows a significant change in the alphaloop6 structure
G281A
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beta-subunit dimers, 46% reduced activity compared to the wild-type enzyme
G51L
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mutation inhibits the ligand-induced transition of the alpha subunit from an open to a closed conformation that serves to block the tunnel for the metabolite chanelling
H273A
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beta-subunit dimers, 2fold increased activity compared to the wild-type enzyme
H86L
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site-directed mutagenesis, exchange of His86, located adjacent to beta subunit Lys87, which forms an intermediate with the pyridoxal 5'-phosphate, leads to 20fold reduced binding of the cofactor and reduced formation the reaction intermediate, altered pH-profile
I278A
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beta-subunit dimers, 70% reduced activity compared to the wild-type enzyme
I278A/K283A
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beta-subunit dimers, 92% reduced activity compared to the wild-type enzyme
I278V
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beta-subunit dimers, 7% reduced activity compared to the wild-type enzyme
I278V/K283A
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beta-subunit dimers, 35% reduced activity compared to the wild-type enzyme
K283A
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beta-subunit dimers, 41% reduced activity compared to the wild-type enzyme
K87T
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Lys87 represents an essential catalytic residue as acceptor of the alpha-proton of L-Ser, alpha subunit
L166A
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mutation in beta-subunit, 3fold increase in catalytic efficiency with L-threonine as substrate, decrease in efficiency with L-serine
L166V
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mutation in beta-subunit, 7fold increase in catalytic efficiency with L-threonine as substrate, decrease in efficiency with L-serine
M282A
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beta-subunit dimers, 61% reduced activity compared to the wild-type enzyme
M282P
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beta-subunit dimers, inactive mutant
R141A
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forms a bienzyme complex with impaired allosteric communication, impaired beta-site catalytic acitivity, the Na+ form of the alpha-site of the mutant is no longer activated by the formation of the alpha-aminoacrylate Schiff base at the beta-site, no restoration by NH4+ or Cs+
R179L
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mutation inhibits the ligand-induced transition of the alpha subunit from an open to a closed conformation that serves to block the tunnel for the metabolite chanelling
R275A
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beta-subunit dimers, 37% reduced activity compared to the wild-type enzyme
T183V
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site-directed mutagenesis, isosteric alpha-subunit mutant, exchange of a highly conserved residue, strongly impaired allosteric alpha-beta communication, 100fold reduced alpha-reaction activity, beta-reaction activity is not affected, effects are due to a missing hydrogen bind between alphaT183 and the catalytic residue alphaAsp60
V276A
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beta-subunit dimers, 46% reduced activity compared to the wild-type enzyme
V276A/K283A
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beta-subunit dimers, 48% reduced activity compared to the wild-type enzyme
Y279A
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beta-subunit dimers, 50% reduced activity compared to the wild-type enzyme
Y279F
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beta-subunit dimers, 33% reduced activity compared to the wild-type enzyme
Y279L
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beta-subunit dimers, 48% reduced activity compared to the wild-type enzyme
Y279P
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beta-subunit dimers, 46% reduced activity compared to the wild-type enzyme
L166A
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mutation in beta-subunit, 3fold increase in catalytic efficiency with L-threonine as substrate, decrease in efficiency with L-serine
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L166V
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mutation in beta-subunit, 7fold increase in catalytic efficiency with L-threonine as substrate, decrease in efficiency with L-serine
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M145T/N167D
mutant accepts various substrates with substitutions in position 5 of indole
P14L/P19G/I69V/L274S/T292S
2fold decrease in catalytic efficiency
P19G/I69V/T292S
10fold increase in catalytic efficiency
T292S
7fold increase in catalytic efficiency
F139W
-
replacement of Phe with Trp does not alter the stability to urea
F139W
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kinetics of unfolding of alpha subunit
F139W
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oligonucleotide-directed mutagenesis, recombinant alpha-subunit mutant, forms monomers
F258W
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replacement of Phe with Trp does not alter the stability to urea
F258W
-
kinetics of unfolding of alpha subunit
G281R
-
reduced activity and weak association with alpha subunit
G281R
-
beta2 subunit, shift of pH-optimum from 7.5 to 9.8, mutant stimulated by NH4+
P12L/E17G/I68V/F274S/T292S/T321A
9fold increase in kcat with an equivalent decrease in KM
P12L/E17G/I68V/F274S/T292S/T321A
mutation in subunit TrpB1, 80fold increase of catalytic efficiency of isolated beta subunit
D305A
-
forms a bienzyme complex with impaired allosteric communication, altered beta-site substrate reaction specificity, the Na+ form of the alpha-site of the mutant is no longer activated by the formation of the alpha-aminoacrylate Schiff base at the beta-site, but this can be restored by replacing Na+ with NH4+ or Cs+
D305A
-
mutation of a salt-bridging residue of the beta-subunit, substitution decreases the affinity of the beta-site for the substrate L-serine, destabilizes the enzyme-bound alpha-aminoacrylate, and quinoid species, and changes the nucleophile specificity of the beta-reaction, increased rate of pyruvate formation compared to the wild-type enzyme
D305A
-
much broader substrate specificity for nucleophiles than the wild type enzyme
D305A
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mutations that affects the allosteric equilibrium also has a dramatic effect on the reaction volume (DELTA V0)
D56A
-
site-directed mutagenesis, mutation in the alpha-subunit, replacement of the residue, which builds a salt bridge to the alpha-subunit, has deleterious effects, which can be repaired by increased temperature in combination with CsCl or NaCl plus alpha-glycerol 3-phosphate, an alpha-ligand, alteration of temperature dependence of the enzyme complex
D56A
-
site-directed mutagenesis, residue is involved in formation of salt bridges between the different subunits, kinetic and structural, conformational alterations, altered signaling by ligand binding, overview
E109D
-
catalytic activity with beta-chloro-L-Ala, but reduced activity with L-Ser, beta subunit
E109D
-
modest but significant effects of 40 to 2000fold on the conformational equilibrium
E109D
-
mutations that affects the allosteric equilibrium also has a dramatic effect on the reaction volume (DELTA V0)
G181P
-
site-directed mutagenesis, replacement of an alphaloop6 residue, loss of the hydrogen bond between residues alphaG181 and betaS178 does not influence the intersubunit catalytic activity, but completely abolishes ligand-induced intersubunit signaling, stabilization of the inactive open conformation of the alpha-active site
G181P
-
mutant shows a significant change in the alphaloop6 structure
K167T
-
site-directed mutagenesis, mutation in the beta-subunit, replacement of the residue, which builds a salt bridge to the alpha-subunit, has deleterious effects, which can be repaired by increased temperature in combination with CsCl or NaCl plus alpha-glycerol 3-phosphate, an alpha-ligand, alteration of temperature dependence of the enzyme complex
K167T
-
site-directed mutagenesis, residue is involved in formation of salt bridges between the different subunits, kinetic and structural, conformational alterations, altered signaling by ligand binding, overview
S178P
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site-directed mutagenesis, molecular modeling of the structural effects caused by the mutation, hydrogen bond with alphaGlu181 is interrupted, 2fold decreased activity of the beta-subunit, not affected, in contrast to the wild-type, by allosteric effectors indole-3-acetylglycine and DL-alpha-glycerol-3-phosphate in the beta-reaction, weaker binding of Na+
S178P
-
site-directed mutagenesis, replacement of an betahelix6 residue, loss of the hydrogen bond between residues alphaG181 and betaS178 does not influence the intersubunit catalytic activity, but completely abolishes ligand-induced intersubunit signaling, stabilization of the inactive open conformation of the alpha-active site
additional information
Trp-overproducing mutant trp5-1 is associated with high chlorophyll levels and low lipid peroxidation. The Trp-auxotroph mutant trp2-1 is sensitive to Cd2+
additional information
-
Trp-overproducing mutant trp5-1 is associated with high chlorophyll levels and low lipid peroxidation. The Trp-auxotroph mutant trp2-1 is sensitive to Cd2+
additional information
construction of Attsbtype2 T-DNA insertion mutants,SALK lines 011904, 124293, 082810, and 162268, that show no obvious deviation from the wild-type
additional information
-
construction of Attsbtype2 T-DNA insertion mutants,SALK lines 011904, 124293, 082810, and 162268, that show no obvious deviation from the wild-type
additional information
-
the trp2-8 and trp2-5 mutants have the most dramatically reduced accumulation of TSB mRNA (7% and 34% of wild type, respectively). In contrast, trp2-9 and trp2-10 plants have modest, but reproducible, enhancement of TSB RNA (28% and 40% higher than the wild type, respectively). TSB protein levels in the trp2 mutants vary from very low (13% of wild type for trp2-5 and 15% for trp2-8) to significantly greater than that of wild type (50-60% higher for trp2-10, trp2-100and trp2-102)
additional information
-
construction of Attsbtype2 T-DNA insertion mutants,SALK lines 011904, 124293, 082810, and 162268, that show no obvious deviation from the wild-type
-
additional information
-
enzymatic properties of 93 mutants of the alpha subunit
additional information
-
hydrogen-to-deuterium exchange in alpha-tryptophan synthase
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