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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
-
-
-
-
?
L-serine + indole
L-tryptophan + D-glyceraldehyde 3-phosphate + 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 + D-glyceraldehyde 3-phosphate + H2O
-
-
-
?
L-serine + indole
L-tryptophan + D-glyceraldehyde 3-phosphate + H2O
-
-
-
?
L-serine + indole
L-tryptophan + D-glyceraldehyde 3-phosphate + 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
-
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/inhibtion 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 7.0, 30°C
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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