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Enzyme Nomenclature
Information on EC 4.2.1.20 - tryptophan synthase
for references in articles please use BRENDA:EC4.2.1.20
Word Map on EC 4.2.1.20
- 4.2.1.20
- pain
- pyridoxal
-
alpha-subunits
- typhimurium
-
myofascial
-
sensory
-
beta-subunits
- 5'-phosphate
-
aldimine
-
indole-3-glycerol
-
trapezius
-
nociceptive
-
vanilloid
-
nose
-
ankyrin
-
quinonoid
-
bienzyme
-
tunable
-
craniofacial
-
epiphyses
-
palpation
-
phalanx
-
beta-site
-
melastatin
-
cone-shaped
-
sternocleidomastoid
-
pear-shaped
-
tryptophanyl-trna
-
metacarpal
-
urea-induced
- assessor
- miles
- tryptophanase
-
bulbous
-
polycystin
-
suboccipital
- l-trp
-
temporalis
- exostoses
-
tension-type
-
dimethylallyl
-
5'-phosphate-dependent
-
taut
-
polymodal
- indoline
- synthesis
- analysis
- biotechnology
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
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EC NUMBER 
COMMENTARY 
4.2.1.20
-
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RECOMMENDED NAME
GeneOntology No.
tryptophan synthase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
overall reaction
-
-
-
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), 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), 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), 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), 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), 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), 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
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), 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), 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)
-
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), 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, 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), 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), 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)
-
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), 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), 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)
-
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
catalyzed reaction and structure of the tryptophan synthase complex, mechanism, overview. Model of the catalytic cycle of the transient enzyme complex, overview
-
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
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
addition
-
-
-
-
condensation
elimination
-
-
of H2O, of NH3, C-O bond cleavage
-
replacement
-
-
beta-position of amino acid
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
L-serine hydro-lyase [adding 1-C-(indol-3-yl)glycerol 3-phosphate; L-tryptophan and glyceraldehyde-3-phosphate-forming]
A pyridoxal-phosphate protein. The alpha-subunit catalyses the conversion of 1-C-(indol-3-yl)glycerol 3-phosphate to indole and D-glyceraldehyde 3-phosphate (this reaction was included formerly under EC 4.1.2.8). The indole migrates to the beta-subunit where, in the presence of pyridoxal 5'-phosphate, it is combined with L-serine to form L-tryptophan. In some organisms this enzyme is part of a multifunctional protein that also includes one or more of the enzymes EC 2.4.2.18 (anthranilate phosphoribosyltransferase), EC 4.1.1.48 (indole-3-glycerol-phosphate synthase), EC 4.1.3.27 (anthranilate synthase) and EC 5.3.1.24 (phosphoribosylanthranilate isomerase). In thermophilic organisms, where the high temperature enhances diffusion and causes the loss of indole, a protein similar to the beta subunit can be found (EC 4.2.1.122). That enzyme cannot combine with the alpha unit of EC 4.2.1.20 to form a complex.
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CAS REGISTRY NUMBER
COMMENTARY
9014-52-2
-
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
hyperthermophile, alpha-subunit TrpA and beta-subunit TrpB1 are encoded by the 2 genes trpA and trpB1 in the trp operon, and by a trpB2 gene outside the operon
-
-
-
5549, 5550, 5551, 5552, 5553, 5558, 5559, 5562, 5567, 5570, 5574, 5575, 5577, 5578, 5579, 5581, 5582, 649237, 649580, 649608, 649852, 649871, 650441, 652475, 658339, 666043, 666051, 666357, 714502, 729099, 729422
-
-
-
5549, 5550, 5567, 5568, 5569, 5576, 5580, 649777, 649865, 649884, 649894, 649898, 649899, 649903, 649979, 650053, 650081, 650181, 650222, 650304, 650441, 650850, 651955, 651967, 652011, 652070, 652086, 652118, 652224, 652550, 652899, 664115, 666055, 677838, 678240, 678297, 678298, 678399, 682732, 692750, 701708, 702257, 715413, 716660, 728850, 729226, 729240, 730007
-
-
gene trpA encodes the alpha-subunit, gene trpB encodes the beta-subunit
-
-
hyperthermophilic archaeon, strain KOD1, alpha- and beta-subunit are encoded by genes Tk-trpA and Tk-trpB
-
-
Q9YGA9: alpha-subunit, Q5JDJ1: beta-subunit TrpB2
SwissProt
Q9YGA9: alpha-subunit, Q9YGB0: beta-subunit TrpB1
SwissProt
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
-
the family of trpB2 genes, identified in the genomes of several microorganisms and plants, can be further divided into the trpB2i, located within the tryptophan operon, and the trpB2o/trpB2a, located outside the operon, subfamilies. The deduced amino acid sequence identities within and between the TrpB1 andTrpB2 families are about 60% and 30%, respectively
malfunction
tryptophan synthase is composed of subunit TrpA and subunit TrpB. Thermococcus kodakarensis possess two paralogs of subunit B, TrpB1 and TrpB2. TrpB1 and TrpB2 both contribute to Trp biosynthesis. TrpB2 catalyzes the TrpB reaction but does not interact with TrpA as in the case of TrpB1. The double-deletion mutant (DELTAtrpB1DELTAtrpB2) displays Trp auxotrophy, whereas individual single mutants (DELTAB1 and DELTAB2 strains) do not; tryptophan synthase is composed of subunit TrpA and subunit TrpB. Thermococcus kodakarensis possess two paralogs of subunit B, TrpB1 and TrpB2. TrpB1 and TrpB2 both contribute to Trp biosynthesis. TrpB2 catalyzes the TrpB reaction but does not interact with TrpA as in the case of TrpB1. The double-deletion mutant (DELTAtrpB1DELTAtrpB2) displays Trp auxotrophy, whereas individual single mutants (DELTAB1 and DELTAB2 strains) do not
metabolism
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. Thermococcus kodakarensis possesses two paralogs of subunit B, TrpB1 and TrpB2. TrpB1 and TrpB2 both contribute to Trp biosynthesis; 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. Thermococcus kodakarensis possesses two paralogs of subunit B, TrpB1 and TrpB2. TrpB1 and TrpB2 both contribute to Trp biosynthesis
physiological function
additional information
physiological function
-
structure analysis indicate that Mycobacterium tuberculosis TrpB exhibits a typical beta/alpha barrel structure
physiological function
-
involved in aromatic amino acid metabolism
physiological function
Vitis vinifera x Vitis vinifera
-
involved in aromatic amino acid metabolism
physiological function
AtTSBtype2 function is not essential under standard growth conditions
physiological function
-
AtTSBtype2 function is not essential under standard growth conditions
-
additional information
-
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. The formation of a transient tryptophan synthase complex, together with the observed low affinity of sTrpB2i for L-serine, couples the rate of tryptophan biosynthesis in Sulfolobus solfataricus to the cytosolic availability of L-serine
additional information
-
molecular dynamics and Brownian dynamics simulations study using PDB entries 2J9X and 3CEP, effects of allostery, oligomerization and intermediate channeling on enhancing the protein function of tryptophan synthase, overview
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(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 + L-serine
L-tryptophan + D-glyceraldehyde 3-phosphate + H2O
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
-
-
-
?
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 + 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-tryptophan + D-glyceraldehyde 3-phosphate + H2O
indole-3-glycerol phosphate + L-serine
-
r
r
-
serine + indole
tryptophan + H2O
-
-
-
?
(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-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 + 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
-
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
-
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-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
-
catalyzed by alpha-subunit
-
-
indole-3-glycerol phosphate
indole + D-glyceraldehyde 3-phosphate
-
-
-
-
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
-
OH of Ser can be replaced by SCH3, OCH3 and Cl, but not by indole
-
-
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
-
-
-
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
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 + 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
-
-
-
-
?
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
-
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
-
beta-subunit of the bienzyme complex, beta-reaction
-
?
L-serine + indole
tryptophan + H2O
-
-
-
-
?
L-serine + indole
tryptophan + H2O
-
beta-subunit of the bienzyme complex, beta-reaction
-
?
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
?
-
-
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
?
-
-
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
?
-
-
catalyzed reaction and structure of the tryptophan synthase complex, overview
-
-
-
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
-
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(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 + 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
-
-
-
-
?
indoleglycerol phosphate
indole + D-glyceraldehyde 3-phosphate
Q9YGA9 and Q5JDJ1, Q9YGA9 and Q9YGB0
the reaction is catalyzed by the tryptophan synthase alpha-subunit TrpA
-
-
r
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 + indole
tryptophan + H2O
-
beta-subunit of the bienzyme complex, beta-reaction
-
?
(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine
L-tryptophan + D-glyceraldehyde 3-phosphate + H2O
Q659I8
-
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(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine
L-tryptophan + D-glyceraldehyde 3-phosphate + H2O
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-
-
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?
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
-
?
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
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?
L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate
L-tryptophan + D-glyceraldehyde 3-phosphate + H2O
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-
-
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?
L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate
L-tryptophan + D-glyceraldehyde 3-phosphate + H2O
P00929
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-
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?
L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate
L-tryptophan + D-glyceraldehyde 3-phosphate + H2O
P00929
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-
-
r
L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate
L-tryptophan + D-glyceraldehyde 3-phosphate + H2O
-
overall reaction
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-
?
L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate
L-tryptophan + D-glyceraldehyde 3-phosphate + H2O
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-
-
-
?
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
Q9YGA9 and Q5JDJ1, Q9YGA9 and Q9YGB0
overall reaction
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-
ir
L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate
L-tryptophan + D-glyceraldehyde 3-phosphate + H2O
Q9YGA9 and Q5JDJ1, Q9YGA9 and Q9YGB0
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
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?
L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate
L-tryptophan + glyceraldehyde 3-phosphate + H2O
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Trp is a precursor of several important signalling molecules in Pseudomonas spp., overview
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?
L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate
L-tryptophan + glyceraldehyde 3-phosphate + H2O
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-
-
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?
L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate
L-tryptophan + glyceraldehyde 3-phosphate + H2O
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-
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?
L-serine + indole
L-tryptophan + H2O
-
beta-subunit of the bienzyme complex, beta-reaction
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?
L-serine + indole
L-tryptophan + H2O
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beta-subunit of the bienzyme complex, beta-reaction
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?
L-serine + indole
L-tryptophan + H2O
Q9YGA9 and Q5JDJ1, Q9YGA9 and Q9YGB0
the reaction is catalyzed by the tryptophan synthase beta-subunit paralogs TrpB1 and TrpB2
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ir
additional information
?
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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
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additional information
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last 2 steps of the tryptophan biosynthesis
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?
additional information
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catalyzed reaction and structure of the tryptophan synthase complex, overview
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pyridoxal 5'-phosphate
-
2 mol bound per mol of beta2 subunit
pyridoxal 5'-phosphate
-
forms a Schiff base with the epsilon amino-group of Lys87
pyridoxal 5'-phosphate
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forms an alpha-aminoacrylate Schiffbase intermediate with L-serine
pyridoxal 5'-phosphate
-
dependent on
pyridoxal 5'-phosphate
-
dependent on, His86 is necessary for binding and stabilization in a correct orientation in the active site of the beta-subunit
pyridoxal 5'-phosphate
-
dependent on, bound via Schiff base to beta-subunit residue Lys87
pyridoxal 5'-phosphate
-
dependent on, bound to the enzyme
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
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
pyridoxal 5'-phosphate
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the coenzyme for reactions catalyzed at the active site of the beta-subunit
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Cd2+
enzyme is up-regulated in plants treated with Cd2+. Overexpression in Arabidopsis and Solanum lycopersicum confers tolerance to cadmium stress
Cs+
DL-glycerol 3-phosphate
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enhances beta-reaction activity of mutant D305N and K167T
K+
Li+
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has an effect on the conformational equilibrium
Na+
NaCl
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ligand binding sites, effector on the action of activators or inhibitors, overview
NH4+
Rb+
-
has an effect on the conformational equilibrium
additional information
Cs+
-
involved in the thermal stability and activity equilibrium of the enzyme complex, overview
Cs+
-
activates the wild-type enzyme and mutant D305A
Cs+
-
activation of mutants D56A and K167T
Cs+
-
affects kinetic properties of the enzyme complex and stabilizes the quinoid intermediates formed
Cs+
-
has an effect on the conformational equilibrium
Cs+
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the enzyme contains three Cs+ ions
K+
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monovalent cations are effectors of the 2-step beta-reaction, role in reaction equilibrium and rate-limitation, overview
K+
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enhances beta-reaction activity of wild-type and mutants, except for mutant D56A
K+
-
has an effect on the conformational equilibrium
Na+
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monovalent cations are effectors of the 2-step beta-reaction, role in reaction equilibrium and rate-limitation, overview
Na+
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involved in the thermal stability and activity equilibrium of the enzyme complex, overview
Na+
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enhances beta-reaction activity of wild-type
Na+
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affects kinetic properties of the enzyme complex and stabilizes the quinoid intermediates formed
Na+
-
has an effect on the conformational equilibrium
Na+
-
in the presence of 100 mM NaCl the enzyme keeps in the Na+ activated form
NH4+
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enhances beta-reaction activity of all wild-type and mutants
NH4+
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activates the wild-type enzyme and mutant D305A
NH4+
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has little effect on the conformational equilibrium
additional information
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the enzyme shows high tolerance to ammonium chloride from hair acid hydrolysis industries waste water, and shows no inhibition by ammonium chloride up to 75 mg/ml
additional information
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effects of Na+ and Cs+ in the intermediate formation between L-serine and aniline
additional information
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monovalent cations are involved in the thermal stability and activity equilibrium of the enzyme complex, overview
additional information
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the beta-reaction is influenced by protons, monovalent cations, and alpha-subunit ligands, that modulate the distribution between open and closed conformation
additional information
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without a bound monovalent cation both the reaction of indoline with alpha-aminoacrylate Schiff base species E(A-A) and the reaction with L-His with internal aldimine Schiff base species are strongly impaired. Monovalent cation binding ensures the structural integrity needed by the beta-active site during stage II of the beta-reaction
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2,3-dihydro-L-tryptophan
-
very good competitive inhibitor
4-(2-hydroxyphenylthio)-1-butenylphosphoric acid
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phosphonate inhibitor
alpha-glycerol 3-phosphate
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alpha-site substrate analogue, reduces the inducing effect caused by monovalent cation effectors
aniline
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nucleophilic analogue used in place of indole leads to formation of intermediate, but no amino acid formation
benzimidazole
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wild-type and mutant D305A enzymes
Indole-3-acetamide
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allosteric effector, binds to the alpha-subunit, inhibitory on the alpha-reaction
indole-3-acetyl-L-alanine
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allosteric effector, binds to the beta-subunit
indole-3-acetyl-L-aspartate
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allosteric effector, binds to the alpha-subunit, slightly inhibitory effect on the enzyme complex, stabilization of the alpha-aminoacrylate Schiff base by perturbing the equilibrium of the catalytic intermediates formed at the beta-active site
indole-3-acetyl-L-aspartic acid
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inhibitor of the alpha-subunit
indole-3-acrylate
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allosteric effector, binds to the beta-subunit, inhibitory on the alpha-reaction due to high concentrations of indole and glyceraldehyde 3-phosphate in the assay mixture
indolebutanol phosphate
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competitive in the catalysis of indoleglycerol phosphate cleavage, Ki: 0.0011 mM
indoleethanol phosphate
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competitive in the catalysis of indoleglycerol phosphate cleavage, Ki: 0.05 mM
indolepropanol phosphate
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competitive in the catalysis of indoleglycerol phosphate cleavage, Ki: 0.004 mM
K+
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inhibits mutant D56A beta-reaction activity, inhibits alpha-reaction of all wild-type and mutants, enhances the overall enzyme complex activity for all wild-type and mutant enzymes, except for mutant D56A
NH4+
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inhibits mutant D56A, D305N and K167T alpha-reaction activity, inhibits alpha-reaction of wild-type and mutant D56A, enhances the overall enzyme complex activity for all wild-type and mutant enzymes
phosphonate inhibitors
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mimic the transition state of the alpha-reaction with higher affinities than the natural substrate indole 3-glycerol phosphate, inhibitor binding changes the conformation of active site residues Glu49 and Phe212, stabilization of the enzyme inhibitor complex by short hydrogen bond between a phosphonate oxygen and Ser235 hydroxyl oxygen, inhibition mechanism
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Urea
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the beta-elimination activity of the enzyme complex decrease less sharply than the beta-replacement activity with increasing concentration in absence of NaCl, 0.1 M NaCl alters the effect of urea concentration
additional information
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inhibition mechanism
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4-(2-aminophenylthio)butylphosphonic acid
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phosphonate inhibitor
4-(2-hydroxy-5-fluorophenylthio)butylphosphonic acid
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phosphonate inhibitor
4-(2-hydroxyphenylsulfinyl)butylphosphonic acid
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phosphonate inhibitor
4-(2-hydroxyphenylthio)butylphosphonic acid
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phosphonate inhibitor
DL-alpha-glycerol 3-phosphate
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alone or in presence of Na+ and Cs+ for wild-type enzyme, for the mutants R141A and D305A the presence of Na+ and NH4+ reverses the inhibitory effect
DL-alpha-glycerol 3-phosphate
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alpha-subunit ligand effects on alpha- and beta-activity wild-type and mutant G181P, on reverse alpha-activity, the rate of beta-reaction, and on the distribution of the catalytic intermediates of the beta-active site, no inhibition of the beta-reaction of mutant G181P
DL-glycerol 3-phosphate
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inhibits beta-reaction activity of wild-type and mutant D56A
DL-glycerol 3-phosphate
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wild-type and mutant enzymes, in presence of monovalent cations
DL-glycerol 3-phosphate
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inhibits the reaction of indole with the enzyme
indole-3-acetyl-L-valine
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allosteric effector, binds to the beta-subunit
indole-3-acetyl-L-valine
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inhibitor of the alpha-subunit
indole-3-acetylglycine
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allosteric effector, binds to the alpha-subunit, slightly inhibitory effect on the enzyme complex, stabilization of the alpha-aminoacrylate Schiff base by perturbing the equilibrium of the catalytic intermediates formed at the beta-active site
indole-3-acetylglycine
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inhibitor of the alpha-subunit
Na+
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inhibits beta-reaction activity of mutant D56A, D305N and K167T, inhibits alpha-reaction of wild-type and mutant D56A, enhances the overall enzyme complex activity for all wild-type and mutant enzymes except for mutant D56A
oxindolyl-L-alanine
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very good competitive inhibitor
trans-L-2-amino-4-methoxy-3-butenoic acid
-
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
betaine
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1 M betaine activates the enzyme 1.8fold in the absence of monovalent cations
Cs+
-
wild-type enzyme alpha-site is activated by the formation of the alpha-aminoacrylate Schiff base at the beta-site
guanidine hydrochloride
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stimulating, dual effector as cation activator and as a modulator of the active site conformation by alteration of the equilibrium distribution of pyridoxal 5'-phosphate intermediates formed in reaction with the beta-subunit, effects on reaction are highly dependent on the substrate, effects are altered by NaCl
guanidinium
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i.e. GuH+, involved in the thermal stability and activity equilibrium of the enzyme complex, overview
Indole-3-acetamide
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allosteric effector, binds to the alpha-subunit, slightly activating effect on the enzyme complex, stabilization of the alpha-aminoacrylate Schiff base by perturbing the equilibrium of the catalytic intermediates formed at the beta-active site
Na+
-
wild-type enzyme alpha-site is activated by the formation of the alpha-aminoacrylate Schiff base at the beta-site
NH4+
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wild-type enzyme alpha-site is activated by the formation of the alpha-aminoacrylate Schiff base at the beta-site
polyethylene glycol 8000
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5% (w/v) activates the enzyme 2.1fold in the absence of monovalent cations
Sucrose
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2 M sucrose activates the enzyme 3.3fold in the absence of monovalent cations
taurine
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0.5 M taurine activates the enzyme 3fold in the absence of monovalent cations
Triton X-100
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Trion X-100 leads to the emergence of the highest relative activity at 0.02% (v/v)
additional information
-
Trp synthase exhibits low-activity (open) and high-activity (closed conformation). The open conformation is favored by high hydrostatic pressure. It is estimated that there are 35-47 more waters in the solvation shell of the open conformation than in that of the closed conformation
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.1
D-glyceraldehyde 3-phosphate
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cosubstrate L-Trp, i.e. reverse reaction
0.02
serine
-
serine deaminase reaction
0.01
1-(indol-3-yl)glycerol 3-phosphate
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reaction of alpha2beta2 complex
0.04
1-(indol-3-yl)glycerol 3-phosphate
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reaction of alpha subunit
0.19
1-(indol-3-yl)glycerol 3-phosphate
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pH 7.5, 80°C, recombinant (TrpA-TrpB1)2 tetrameric complex, alpha-reaction
1.62
1-(indol-3-yl)glycerol 3-phosphate
-
pH 7.5, 80°C, recombinant TrpA, alpha-reaction
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
0.018
indole
-
cosubstrate L-Ser, presence of 20 mM Na+
0.025
indole
-
pH 7.5, 80°C, recombinant (TrpA-TrpB1)2 tetrameric complex, beta-reaction
0.035
indole
pH 7.5, 85°C, reaction catalyzed by TrpB1 in presence of subunit TrpA
0.044
indole
-
cosubstrate L-Ser, presence of 20 mM Li+
0.0629
indole
pH 7.5, 85°C, reaction catalyzed by TrpB2
0.067
indole
-
cosubstrate L-Ser, presence of 20 mM Cs+
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
0.0076
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
0.629
L-serine
subunit TrpB1, at pH 7.5 and 85°C
0.98
L-serine
-
37°C, beta-replacement, enzyme in solution
1.16
L-serine
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37°C, beta-elimination, enzyme in solution
1.17
L-serine
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37°C, beta-replacement, enzyme encapsulated in tetramethylorthosilicate-derived wet silica gels
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; without monovalent cations, at pH 7.8 and 25°C
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
2.7
L-serine
-
without monovalent cations, at pH 8.5 and 25°C
3.7
L-serine
-
pH 7.5, 80°C, recombinant (TrpA-TrpB1)2 tetrameric complex, beta-reaction
4.78
L-serine
-
in the presence of 250 mM NaCl, at pH 6.5 and 25°C
5.6
L-serine
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in the presence of 100 mM CsCl, at pH 7.8 and 25°C
9
L-serine
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in the presence of 100 mM CsCl, at pH 6.5 and 25°C
additional information
additional information
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dissociation constants of the beta-subunit combined with the different subunits of wild-type and mutants
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additional information
additional information
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kinetics of the hydrogen-deuterium exchange reactions
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additional information
additional information
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kinetics
-
additional information
additional information
-
kinetics
-
additional information
additional information
-
kinetics and temperature-dependence
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additional information
additional information
-
kinetics, wild-type and mutants, isotope effects and effector influence
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additional information
additional information
-
kinetic isotope effects with alpha-2H-L-Ser, and thermodynamics, wild-type and mutant
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additional information
additional information
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kinetics of proton release during beta-reaction, thermodynamic cycle of the interconversion of L-serine and alpha-aminoacrylate intermediate structures
-
additional information
additional information
-
dissociation constants, kinetics
-
additional information
additional information
-
kinetics for the wild-type and channel-impaired mutants
-
additional information
additional information
-
kinetics, temperature-, and pH-dependence, and isotope effect at pH 7.0, not at pH 9.0, overview
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additional information
additional information
-
kinetics, wild-type and mutant H86L enzymes
-
additional information
additional information
-
kinetics of wild-type enzyme complex and mutant betaA169L/betaC170W
-
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
-
thermodynamic parameters of subunit association, kinetics
-
additional information
additional information
-
kinetics, beta-reaction
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.4
indoline
-
overall-reaction, mutant D305A enzyme, pH 7.8, 25°C, in presence of 100 mM Cs+
0.06
serine
-
serine deaminase reaction
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
0.033
indole
-
beta-reaction, mutant R141A, pH 7.8, 25°C
0.39
indole
pH 7.5, 85°C, reaction catalyzed by TrpB2; pH 7.5, 85°C, reaction catalyzed by TrpB2 in presence of subunit TrpA
0.88
indole
-
beta-reaction, mutant D305A, pH 7.8, 25°C
1.04
indole
pH 7.5, 85°C, reaction catalyzed by TrpB1
1.6
indole
-
beta-reaction, wild-type, pH 7.8, 25°C
3.3
indole
-
beta-reaction, pH 7.8, 25°C, mutant T183V enzyme; 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
3.41
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
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
5.44
indole
-
cosubstrate L-Ser, presence of 20 mM Cs+
6.08
indole
-
beta-reaction, mutant D305A, pH 7.8, 25°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
0.00017
L-serine
-
overall-reaction, pH 7.8, 25°C, mutant T183V enzyme
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
0.24
L-serine
-
without monovalent cations, at pH 6.5 and 25°C
0.26
L-serine
-
37°C, beta-elimination, enzyme in solution
0.39
L-serine
subunit TrpB2, at pH 7.5 and 85°C; subunit TrpB2 plus subunit TrpA, 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+
0.8
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
1.04
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; in the presence of 250 mM NaCl, at pH 8.5 and 25°C
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; 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
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
7.8
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+
12
L-serine
-
overall-reaction, wild-type enzyme, pH 7.8, 25°C, in presence of K+
14
L-serine
-
overall-reaction, wild-type enzyme, pH 7.8, 25°C, in presence of Cs+
additional information
L-serine
-
in the presence of 100 mM CsCl, at pH 8.5 and 25°C
additional information
additional information
-
turnover of wild-type and mutant D305A in presence of different effectors for alpha-, and beta-reaction
-
additional information
additional information
-
activities of wild-type and mutants in presence of different effectors
-
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
17
indole
pH 7.5, 85°C, reaction catalyzed by TrpB1
48
indole
pH 7.5, 85°C, reaction catalyzed by TrpB2
51
indole
pH 7.5, 85°C, reaction catalyzed by TrpB2 in presence of subunit TrpA
99
indole
pH 7.5, 85°C, reaction catalyzed by TrpB1 in presence of subunit TrpA
17
L-serine
subunit TrpB2, at pH 7.5 and 85°C
48
L-serine
subunit TrpB1, at pH 7.5 and 85°C
51
L-serine
subunit TrpB2 plus subunit TrpA, at pH 7.5 and 85°C
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
12.8
glycerol 3-phosphate
-
pH 7.8, 20°C
0.45
Indole-3-acetamide
-
pH 7.8, 20°C
0.95
indole-3-acetyl-L-alanine
-
pH 7.8, 20°C
1.67
indole-3-acetyl-L-aspartate
-
pH 7.8, 20°C
0.48
indole-3-acetyl-L-valine
-
pH 7.8, 20°C
1.2
indole-3-acetylglycine
-
pH 7.8, 20°C
0.32
indole-3-acrylate
-
pH 7.8, 20°C
0.0011
indolebutanol phosphate
-
competitive in the catalysis of indoleglycerol phosphate cleavage
0.05
indoleethanol phosphate
-
competitive in the catalysis of indoleglycerol phosphate cleavage
0.004
indolepropanol phosphate
-
competitive in the catalysis of indoleglycerol phosphate cleavage
additional information
additional information
-
-
-
additional information
additional information
-
inhibition kinetics
-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
70
-
mutant K167T, in presence of Na+
125
190
-
wild-type enzyme, in presence of guanidinum
288
-
purified wild-type, beta-reaction, in presence of DL-alpha-glycerol 3-phosphate
511
-
purified mutant G181P, reverse alpha-reaction, in presence of DL-alpha-glycerol 3-phosphate
520
-
purified mutant G181P, beta-reaction, in absence or presence of DL-alpha-glycerol 3-phosphate
818
-
purified mutant G181P, reverse alpha-reaction, in absence of DL-alpha-glycerol 3-phosphate
1150
-
purified wild-type, beta-reaction, in absence of DL-alpha-glycerol 3-phosphate
1310
-
wild-type enzyme, in presence of Na+
1375
-
purified wild-type, reverse alpha-reaction, in presence of DL-alpha-glycerol 3-phosphate
1400
-
wild-type enzyme, in presence of Cs+
1524
1605
-
purified wild-type, reverse alpha-reaction, in absence of DL-alpha-glycerol 3-phosphate
1650
-
mutant K167T, in presence of Cs+
2200
-
mutant D56A, in presence of Cs+
additional information
125
-
indole-3-glycerol phosphate + L-serine
1524
-
wild-type enzyme in presence of alpha-subunit
additional information
-
activity of the beta-subunit combined with the different alpha-subunit monomers and dimers of wild-type and mutants
additional information
-
activity of the prified recombinant individually expressed subunits is 10fold lower than the activity of the native enzyme complex
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
7.6
-
optimum for the reactions: 1. indole-3-glycerol phosphate + L-Ser, 2. indole + L-Ser
7.8
8.2
7.8
-
assay at
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
pH-profiling, pH-dependence of the beta-reaction in absence or presence of Na+, Cs+, K+, influence of monovalent cations in combination with alpha-subunit ligand indole-acetylglycine, overview
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
30
37
40
80
25
-
assay at
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 50
-
thermodynamic analysis of the conformational change conditions and the effects of monovalent ions and effector DL-alpha-glycderol 3-phosphate
40 - 85
-
recombinant alpha-subunit shows low activity at all temperatures
70 - 100
-
recombinant beta-subunit, low activity below 70°C, increasing activity from 70°C to 100°C, at 100°C the activity is similar to the native enzyme complex
additional information
-
temperature-dependent changes in equilibrium distribution of enzyme-substrate intermediates and in primary kinetic isotope effect, D56 and K167 are involved
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
activity highest in shoot tips, less activity in young leaves and internodes, activity declines with maturation
additional information
while AtTSB1 is the predominantly expressed isoform in vegetative tissues, AtTSB1 and AtTSBtype2 reach similar transcript levels in seeds, tissue-specific expression pattern, overview
additional information
-
while AtTSB1 is the predominantly expressed isoform in vegetative tissues, AtTSB1 and AtTSBtype2 reach similar transcript levels in seeds, tissue-specific expression pattern, overview
-
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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PDB
SCOP
CATH
UNIPROT
ORGANISM
Q9PIF1
Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168);
Escherichia coli (strain K12);
Q5NE80
Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4);
Q5ZVY3
Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC 33152 / DSM 7513);
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv);
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1);
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720);
Q97P33
Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4);
Q97TX6
Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2);
Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039);
Q9KST7
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961);
P9WFX9
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv);
P9WFX9
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv);
P9WFY1
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv);
P9WFY1
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv);
P9WFY1
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv);
P9WFY1
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv);
P9WFY1
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv);
P9WFY1
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv);
Q8U094
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1);
Q8U093
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1);
Q8U094
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1);
Q8U094
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1);
Q8U094
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1);
Q8U094
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1);
Q8U094
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1);
Q8U094
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1);
Q8U094
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1);
Q8U094
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1);
Q8U094
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1);
Q8U093
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1);
Q8U093
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1);
Q8U093
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1);
Q8U094
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1);
Q8U093
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1);