Information on EC 4.2.1.20 - tryptophan synthase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea

EC NUMBER
COMMENTARY
4.2.1.20
-
RECOMMENDED NAME
GeneOntology No.
tryptophan synthase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
1-C-(indol-3-yl)glycerol 3-phosphate = indole + D-glyceraldehyde 3-phosphate
show the reaction diagram
(1a)
-
-
-
L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate = L-tryptophan + D-glyceraldehyde 3-phosphate + H2O
show the reaction diagram
overall reaction
-
-
-
L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate = L-tryptophan + D-glyceraldehyde 3-phosphate + H2O
show the reaction diagram
mechanism
-
L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate = L-tryptophan + D-glyceraldehyde 3-phosphate + H2O
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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 + indole = L-tryptophan + H2O
show the reaction diagram
(1b)
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
addition
-
-
-
-
C-O bond cleavage
-
-
elimination
-
-
of H2O, of NH3, C-O bond cleavage
-
replacement
-
-
beta-position of amino acid
-
PATHWAY
KEGG Link
MetaCyc Link
Biosynthesis of secondary metabolites
-
Glycine, serine and threonine metabolism
-
Metabolic pathways
-
Phenylalanine, tyrosine and tryptophan biosynthesis
-
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.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
alpha2beta2 tryptophan synthase
-
consists of an alpha2beta2 bienzyme complex with alphabeta dimeric units assembled as the tetrameric species via the beta-beta subunit interface, each alpha-subunit catalyzes the cleavage of 3-indole-D-glycerol 3'-phosphate to indole and D-glyceraldehyde 3-phosphate, the pyridoxal phosphate requiring beta-subunit catalyzes a beta-replacement reaction in which indole replaces the hydroxyl of L-Ser, giving L-Trp
alphaTS
-
alpha-subunit
alphaTS
-
alpha subunit of tryptophan synthase
AtTSB1
P14671
-
beta subunit of tryptophan synthase
-
-
indoleglycerol phosphate aldolase
-
-
-
-
It-TSA
Q659I8
-
L-serine hydro-lyase (adding indoleglycerol-phosphate)
-
-
L-tryptophan synthetase
-
-
-
-
Rv1612
-
gene name
synthase, tryptophan
-
-
-
-
Trp synthase beta
-
-
trpB
Vitis vinifera x Vitis riparia, Vitis vinifera x Vitis vinifera
-
-
tryptophan desmolase
-
-
-
-
tryptophan synthase
-
-
tryptophan synthase
-
-
tryptophan synthase
-
subunit TrpA catalyzes the reversible cleavage of indole-3-glycerol phosphate (IGP1) into glyceraldehyde-3-phosphate and indole, the indole migrates through a hydrophobic channel to an active site of an attached TrpB1 subunit, where it condenses with L-serine in a pyridoxal phosphate dependent irreversible reaction to form L-tryptophan
tryptophan synthase alpha2beta2 complex
-
-
tryptophan synthase beta
-
-
tryptophan synthase beta
Q9FFW8
-
tryptophan synthase beta
Arabidopsis thaliana Col-0
Q9FFW8
-
-
tryptophan synthase beta
-
-
tryptophan synthase beta
Zea mays B73
-
-
-
tryptophan synthase beta 1
-
-
tryptophan synthase beta 1
P14671
-
tryptophan synthase beta subunit
-
-
tryptophan synthase beta subunit
Q60142
-
tryptophan synthase beta subunit
Bacillus subtilis K
Q60142
-
-
tryptophan synthase beta subunit
-
-
tryptophan synthase beta subunit
Vitis vinifera x Vitis riparia, Vitis vinifera x Vitis vinifera
-
-
tryptophan synthetase
-
-
-
-
TSase
Escherichia coli MG1655
-
-
-
TSB
Arabidopsis thaliana Col-0
Q9FFW8
-
-
TSB
-
-
TSB
Zea mays B73
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9014-52-2
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
ecotype Columbia
UniProt
Manually annotated by BRENDA team
isozymes AtTSB1 and AtTSBtype2
UniProt
Manually annotated by BRENDA team
Arabidopsis thaliana Col-0
isozymes AtTSB1 and AtTSBtype2
UniProt
Manually annotated by BRENDA team
Bacillus subtilis K
-
UniProt
Manually annotated by BRENDA team
serovar L2/LGV-434
-
-
Manually annotated by BRENDA team
alph-subunit alphaTS
-
-
Manually annotated by BRENDA team
BL21(DE3)
-
-
Manually annotated by BRENDA team
strain CB149
Uniprot
Manually annotated by BRENDA team
Escherichia coli CB149
strain CB149
Uniprot
Manually annotated by BRENDA team
Escherichia coli MG1655
-
-
-
Manually annotated by BRENDA team
-
Q659I8
UniProt
Manually annotated by BRENDA team
strains CHA or PAO1
-
-
Manually annotated by BRENDA team
gene trpA encodes the alpha-subunit, gene trpB encodes the beta-subunit
-
-
Manually annotated by BRENDA team
hyperthermophilic archaeon, strain KOD1, alpha- and beta-subunit are encoded by genes Tk-trpA and Tk-trpB
-
-
Manually annotated by BRENDA team
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
-
-
Manually annotated by BRENDA team
Vitis vinifera x Vitis riparia
-
-
-
Manually annotated by BRENDA team
Vitis vinifera x Vitis vinifera
-
-
-
Manually annotated by BRENDA team
isozyme TSB type 2
-
-
Manually annotated by BRENDA team
Zea mays B73
isozyme TSB type 2
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
physiological function
-
structure analysis indicate that Mycobacterium tuberculosis TrpB exhibits a typical beta/alpha barrel structure
physiological function
Vitis vinifera x Vitis riparia, Vitis vinifera x Vitis vinifera
-
involved in aromatic amino acid metabolism
physiological function
Q9FFW8
AtTSBtype2 function is not essential under standard growth conditions
physiological function
Arabidopsis thaliana Col-0
-
AtTSBtype2 function is not essential under standard growth conditions
-
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
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
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
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
show the reaction diagram
-
-
-
-
?
(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine
L-tryptophan + D-glyceraldehyde 3-phosphate + H2O
show the reaction diagram
-, Q659I8
-
-
-
?
1-(indol-3-yl)glycerol 3-phosphate
D-glyceraldehyde 3-phosphate + indole
show the reaction diagram
-
alpha-subunit of the bienzyme complex, alpha-reaction
-
?
1-(indol-3-yl)glycerol 3-phosphate
D-glyceraldehyde 3-phosphate + indole
show the reaction diagram
-
alpha-subunit of the bienzyme complex, alpha-reaction
-
?
1-(indol-3-yl)glycerol 3-phosphate
D-glyceraldehyde 3-phosphate + indole
show the reaction diagram
-
alpha-subunit of the bienzyme complex, alpha-reaction
-
?
1-(indol-3-yl)glycerol 3-phosphate
D-glyceraldehyde 3-phosphate + indole
show the reaction diagram
-
alpha-subunit of the bienzyme complex, alpha-reaction
-
?
1-(indol-3-yl)glycerol 3-phosphate
D-glyceraldehyde 3-phosphate + indole
show the reaction diagram
-
alpha-subunit of the bienzyme complex, alpha-reaction
-
?
1-(indol-3-yl)glycerol 3-phosphate
D-glyceraldehyde 3-phosphate + indole
show the reaction diagram
-
alpha-subunit of the bienzyme complex, alpha-reaction
-
?
1-(indol-3-yl)glycerol 3-phosphate
D-glyceraldehyde 3-phosphate + indole
show the reaction diagram
-
alpha-subunit of the bienzyme complex, alpha-reaction
-
?
1-(indol-3-yl)glycerol 3-phosphate
D-glyceraldehyde 3-phosphate + indole
show the reaction diagram
-
alpha-subunit of the bienzyme complex, alpha-reaction
-
?
1-(indol-3-yl)glycerol 3-phosphate
D-glyceraldehyde 3-phosphate + indole
show the reaction diagram
-
alpha-subunit of the bienzyme complex, alpha-reaction
-
?
1-(indol-3-yl)glycerol 3-phosphate
D-glyceraldehyde 3-phosphate + indole
show the reaction diagram
-
alpha-subunit of the bienzyme complex, alpha-reaction
-
?
1-(indol-3-yl)glycerol 3-phosphate
D-glyceraldehyde 3-phosphate + indole
show the reaction diagram
-
alpha-subunit of the bienzyme complex, alpha-reaction
-
?
1-(indol-3-yl)glycerol 3-phosphate
D-glyceraldehyde 3-phosphate + indole
show the reaction diagram
-
alpha-subunit of the bienzyme complex, alpha-reaction
-
?
1-(indol-3-yl)glycerol 3-phosphate
D-glyceraldehyde 3-phosphate + indole
show the reaction diagram
-
alpha-subunit of the bienzyme complex, alpha-reaction
-
?
1-(indol-3-yl)glycerol 3-phosphate
D-glyceraldehyde 3-phosphate + indole
show the reaction diagram
-
alpha-subunit of the bienzyme complex, alpha-reaction
-
?
1-(indol-3-yl)glycerol 3-phosphate
D-glyceraldehyde 3-phosphate + indole
show the reaction diagram
-
alpha-subunit of the bienzyme complex, alpha-reaction
-
?
1-(indol-3-yl)glycerol 3-phosphate
D-glyceraldehyde 3-phosphate + indole
show the reaction diagram
-
alpha-subunit of the bienzyme complex, alpha-reaction
-
?
1-(indol-3-yl)glycerol 3-phosphate
D-glyceraldehyde 3-phosphate + indole
show the reaction diagram
-
alpha-subunit of the bienzyme complex, alpha-reaction
-
?
1-(indol-3-yl)glycerol 3-phosphate
D-glyceraldehyde 3-phosphate + indole
show the reaction diagram
-
alpha-subunit of the bienzyme complex, alpha-reaction
-
?
1-(indol-3-yl)glycerol 3-phosphate
D-glyceraldehyde 3-phosphate + indole
show the reaction diagram
-
alpha-subunit of the bienzyme complex, alpha-reaction
-
?
1-(indol-3-yl)glycerol 3-phosphate
D-glyceraldehyde 3-phosphate + indole
show the reaction diagram
-
alpha-subunit of the bienzyme complex, alpha-reaction
-
?
1-(indol-3-yl)glycerol 3-phosphate
D-glyceraldehyde 3-phosphate + indole
show the reaction diagram
-
alpha-subunit of the bienzyme complex, alpha-reaction
-
?
1-(indol-3-yl)glycerol 3-phosphate
D-glyceraldehyde 3-phosphate + indole
show the reaction diagram
-
alpha-subunit of the bienzyme complex, alpha-reaction
-
?
1-(indol-3-yl)glycerol 3-phosphate
D-glyceraldehyde 3-phosphate + indole
show the reaction diagram
-
alpha-subunit of the bienzyme complex, alpha-reaction
-
?
1-(indol-3-yl)glycerol 3-phosphate
D-glyceraldehyde 3-phosphate + indole
show the reaction diagram
-
alpha-subunit of the bienzyme complex, alpha-reaction
-
?
1-(indol-3-yl)glycerol 3-phosphate
D-glyceraldehyde 3-phosphate + indole
show the reaction diagram
-
alpha-subunit of the bienzyme complex, alpha-reaction
-
?
1-(indol-3-yl)glycerol 3-phosphate
D-glyceraldehyde 3-phosphate + indole
show the reaction diagram
-
alpha-subunit of the bienzyme complex, alpha-reaction
-
?
1-(indol-3-yl)glycerol 3-phosphate
D-glyceraldehyde 3-phosphate + indole
show the reaction diagram
-, Q8U094
alpha-subunit of the bienzyme complex, alpha-reaction
-
?
1-(indol-3-yl)glycerol 3-phosphate
D-glyceraldehyde 3-phosphate + indole
show the reaction diagram
-
alpha-subunit of the bienzyme complex, alpha-reaction
-
?
1-(indol-3-yl)glycerol 3-phosphate
D-glyceraldehyde 3-phosphate + indole
show the reaction diagram
-
alpha-subunit of the bienzyme complex, alpha-reaction
-
?
1-(indol-3-yl)glycerol 3-phosphate
D-glyceraldehyde 3-phosphate + indole
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
alpha-subunit of the bifunctional enzyme complex, alpha-reaction
-
?
1-(indol-3-yl)glycerol 3-phosphate
D-glyceraldehyde 3-phosphate + indole
show the reaction diagram
-
alpha-subunit of the bifunctional enzyme complex, alpha-reaction
-
?
1-(indol-3-yl)glycerol 3-phosphate + L-serine
L-tryptophan + D-glyceraldehyde 3-phosphate + H2O
show the reaction diagram
-
-
-
-
-
1-(indol-3-yl)glycerol 3-phosphate + L-serine
L-tryptophan + D-glyceraldehyde 3-phosphate + H2O
show the reaction diagram
-
-
-
-
-
1-(indol-3-yl)glycerol 3-phosphate + L-serine
L-tryptophan + D-glyceraldehyde 3-phosphate + H2O
show the reaction diagram
-
-
-
-
-
1-(indol-3-yl)glycerol 3-phosphate + L-serine
L-tryptophan + D-glyceraldehyde 3-phosphate + H2O
show the reaction diagram
-
-
-
-
1-(indol-3-yl)glycerol 3-phosphate + L-serine
L-tryptophan + D-glyceraldehyde 3-phosphate + H2O
show the reaction diagram
-
-
-
-
-
1-(indol-3-yl)glycerol 3-phosphate + L-serine
L-tryptophan + D-glyceraldehyde 3-phosphate + H2O
show the reaction diagram
-
-
-
-
?
1-(indol-3-yl)glycerol 3-phosphate + L-serine
L-tryptophan + D-glyceraldehyde 3-phosphate + H2O
show the reaction diagram
-
r
-
-
1-(indol-3-yl)glycerol 3-phosphate + L-serine
L-tryptophan + D-glyceraldehyde 3-phosphate + H2O
show the reaction diagram
-
catalyzed by alpha2beta2 holoenzyme
-
-
1-(indol-3-yl)glycerol 3-phosphate + L-serine
L-tryptophan + D-glyceraldehyde 3-phosphate + H2O
show the reaction diagram
-
catalyzed by alpha2beta2 holoenzyme, hybrid enzyme with alpha subunit of E. coli or Salmonella typhimurium active in this reaction, 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
show the reaction diagram
-
alpha reaction
-
-
r
1-(indol-3-yl)glycerol 3-phosphate + L-serine
L-tryptophan + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
?
1-(indol-3-yl)glycerol 3-phosphate + L-serine
L-tryptophan + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
?
1-(indol-3-yl)glycerol 3-phosphate + L-serine
L-tryptophan + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
?
1-(indol-3-yl)glycerol 3-phosphate + L-serine
L-tryptophan + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
?
1-(indol-3-yl)glycerol 3-phosphate + L-serine
L-tryptophan + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
alpha-subunit of the bienzyme complex, alpha-reaction
-
?
2-amino-3-butenoic acid
2-oxobutyric acid + NH3
show the reaction diagram
-
vinylglycine
-
-
2-mercaptoethanol + L-serine + pyridoxal phosphate
S-pyruvylmercaptoethanol + pyridoxamine phosphate + H2O
show the reaction diagram
-
-
-
-
beta-chloro-L-alanine
pyruvate + NH3 + HCl
show the reaction diagram
-
in absence of indole
-
?
beta-chloro-L-alanine + indole
L-tryptophan + HCl
show the reaction diagram
-
-
-
?
indole + D-glyceraldehyde 3-phosphate
indole-3-glycerol phosphate
show the reaction diagram
-
r
r
-
indole + D-glyceraldehyde 3-phosphate
indole-3-glycerol phosphate
show the reaction diagram
-
r
r
-
indole + D-glyceraldehyde 3-phosphate
indole-3-glycerol phosphate
show the reaction diagram
-
r
r
-
indole + L-serine
L-tryptophan + H2O
show the reaction diagram
-
-
-
-
-
indole + L-serine
L-tryptophan + H2O
show the reaction diagram
-
-
-
-
-
indole + L-serine
L-tryptophan + H2O
show the reaction diagram
-
-
-
-
indole + L-serine
L-tryptophan + H2O
show the reaction diagram
-
-
-
-
-
indole + L-serine
L-tryptophan + H2O
show the reaction diagram
-
-
-
-
indole + L-serine
L-tryptophan + H2O
show the reaction diagram
-
-
-
-
indole + L-serine
L-tryptophan + H2O
show the reaction diagram
-
-
-
-
-
indole + L-serine
L-tryptophan + H2O
show the reaction diagram
-
-
-
-
indole + L-serine
L-tryptophan + H2O
show the reaction diagram
-
-
-
-
-
indole + L-serine
L-tryptophan + H2O
show the reaction diagram
-
-
-
-
-
indole + L-serine
L-tryptophan + H2O
show the reaction diagram
-
-
-
-
indole + L-serine
L-tryptophan + H2O
show the reaction diagram
-
-
-
-
?
indole + L-serine
L-tryptophan + H2O
show the reaction diagram
-
hybrid enzyme with alpha subunit of E. coli or Salmonella typhimurium shows low activity in this reaction
-
-
-
indole + L-serine
L-tryptophan + H2O
show the reaction diagram
-
catalyzed by beta2 subunit
-
-
-
indole + L-serine
L-tryptophan + H2O
show the reaction diagram
-
catalyzed by beta2 subunit
-
-
indole + L-serine
L-tryptophan + H2O
show the reaction diagram
-
catalyzed by beta2 subunit
-
-
-
indole + L-serine
L-tryptophan + H2O
show the reaction diagram
-
hybrid enzyme with beta2 subunit of E. coli or Salmonella typhimurium inactive in this reaction
-
-
-
indole + L-serine
L-tryptophan + H2O
show the reaction diagram
-
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
show the reaction diagram
-
-
-
-
-
indole-3-glycerol phosphate
indole + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
-
indole-3-glycerol phosphate
indole + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
-
-
indole-3-glycerol phosphate
indole + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
-
-
indole-3-glycerol phosphate
indole + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
-
indole-3-glycerol phosphate
indole + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
r
r
-
indole-3-glycerol phosphate
indole + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
r
r
-
indole-3-glycerol phosphate
indole + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
r
r
-
indole-3-glycerol phosphate
indole + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
mechanism
r
-
indole-3-glycerol phosphate
indole + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
hybrid enzyme with beta2 subunit of E. coli or Salmonella typhimurium active in this reaction
-
-
-
indole-3-glycerol phosphate
indole + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
catalyzed by alpha-subunit
-
-
indole-3-glycerol phosphate
indole + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
catalyzed by alpha-subunit
-
-
indole-3-glycerol phosphate
indole + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
catalyzed by alpha-subunit
-
-
indole-3-glycerol phosphate
indole + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
catalyzed by alpha-subunit
-
-
-
indole-3-glycerol phosphate
indole + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
reaction is catalyzed by alpha-subunit. Structural basis of the catalytic mechanism and regulation of the alpha-subunit
-
-
?
indoline + L-serine
dihydroisotryptophan + H2O
show the reaction diagram
-
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
?
show the reaction diagram
-
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-serine
pyruvate + NH3
show the reaction diagram
-
-
-
-
L-serine
pyruvate + NH3
show the reaction diagram
-
catalyzed by beta2-subunit
-
-
L-serine
pyruvate + NH3
show the reaction diagram
-
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 + glyceraldehyde 3-phosphate + H2O
show the reaction diagram
-
-
-
-
?
L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate
L-tryptophan + glyceraldehyde 3-phosphate + H2O
show the reaction diagram
-
-
-
-
?
L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate
L-tryptophan + glyceraldehyde 3-phosphate + H2O
show the reaction diagram
-
-
-
-
?
L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate
L-tryptophan + glyceraldehyde 3-phosphate + H2O
show the reaction diagram
-
Trp is a precursor of several important signalling molecules in Pseudomonas spp., overview
-
-
?
L-serine + 2-methylindole
2-methyltryptophan + H2O
show the reaction diagram
-
-
-
-
?
L-serine + 4-bromoindole
4-bromotryptophan + H2O
show the reaction diagram
-
-
-
-
?
L-serine + 4-bromoindole
4-bromotryptophan + H2O
show the reaction diagram
-
weak reaction
-
-
?
L-serine + 4-methylindole
4-methyltryptophan + H2O
show the reaction diagram
-
-
-
-
?
L-serine + 5-bromoindole
5-bromotryptophan + H2O
show the reaction diagram
-
-
-
-
?
L-serine + 5-chloroindole
5-chlorotryptophan + H2O
show the reaction diagram
-
-
-
-
?
L-serine + 5-fluoroindole
5-fluorotryptophan + H2O
show the reaction diagram
-
-
-
-
?
L-serine + 5-fluoroindole
5-fluorotryptophan + H2O
show the reaction diagram
-
-
-
-
?
L-serine + 5-methylindole
5-methyltryptophan + H2O
show the reaction diagram
-
-
-
-
?
L-serine + 6-bromoindole
6-bromotryptophan + H2O
show the reaction diagram
-
-
-
-
?
L-serine + 6-chloroindole
6-chlorotryptophan + H2O
show the reaction diagram
-
-
-
-
?
L-serine + 6-fluoroindole
6-fluorotryptophan + H2O
show the reaction diagram
-
-
-
-
?
L-serine + 6-methylindole
6-methyltryptophan + H2O
show the reaction diagram
-
-
-
-
?
L-serine + 7-bromoindole
7-bromotryptophan + H2O
show the reaction diagram
-
-
-
-
?
L-serine + 7-bromoindole
7-bromotryptophan + H2O
show the reaction diagram
-
weak reaction
-
-
?
L-serine + 7-chloroindole
7-chlorotryptophan + H2O
show the reaction diagram
-
-
-
-
?
L-serine + 7-fluoroindole
7-fluorotryptophan + H2O
show the reaction diagram
-
-
-
-
?
L-serine + 7-fluoroindole
7-fluorotryptophan + H2O
show the reaction diagram
-
weak reaction
-
-
?
L-serine + 7-methylindole
7-methyltryptophan + H2O
show the reaction diagram
-
-
-
-
?
L-serine + indole
L-tryptophan + H2O
show the reaction diagram
-
-
-
-
?
L-serine + indole
L-tryptophan + H2O
show the reaction diagram
P0A877
-
-
-
?
L-serine + indole
L-tryptophan + H2O
show the reaction diagram
-
-
-
-
?
L-serine + indole
L-tryptophan + H2O
show the reaction diagram
-
-
-
-
?
L-serine + indole
L-tryptophan + H2O
show the reaction diagram
-
-
-
-
?
L-serine + indole
L-tryptophan + H2O
show the reaction diagram
-
-
-
-
?
L-serine + indole
L-tryptophan + H2O
show the reaction diagram
-
-
-
-
?
L-serine + indole
L-tryptophan + H2O
show the reaction diagram
-
-
-
-
?
L-serine + indole
L-tryptophan + H2O
show the reaction diagram
-
-
-
-
?
L-serine + indole
L-tryptophan + H2O
show the reaction diagram
Q9FFW8
-
-
-
?
L-serine + indole
L-tryptophan + H2O
show the reaction diagram
-
beta-subunit of the bienzyme complex, beta-reaction
-
?
L-serine + indole
L-tryptophan + H2O
show the reaction diagram
-
beta-subunit of the bienzyme complex, beta-reaction
-
?
L-serine + indole
L-tryptophan + H2O
show the reaction diagram
-
beta-subunit of the bienzyme complex, beta-reaction
-
?
L-serine + indole
L-tryptophan + H2O
show the reaction diagram
-
beta-subunit of the bienzyme complex, beta-reaction
-
?
L-serine + indole
L-tryptophan + H2O
show the reaction diagram
-
beta-subunit of the bienzyme complex, beta-reaction
-
?
L-serine + indole
L-tryptophan + H2O
show the reaction diagram
-
beta-subunit of the bienzyme complex, beta-reaction
-
?
L-serine + indole
L-tryptophan + H2O
show the reaction diagram
-
beta-subunit of the bienzyme complex, beta-reaction
-
?
L-serine + indole
L-tryptophan + H2O
show the reaction diagram
-
beta-subunit of the bienzyme complex, beta-reaction
-
?
L-serine + indole
L-tryptophan + H2O
show the reaction diagram
-
beta-subunit of the bienzyme complex, beta-reaction
-
?
L-serine + indole
L-tryptophan + H2O
show the reaction diagram
-
beta-subunit of the bienzyme complex, beta-reaction
-
?
L-serine + indole
L-tryptophan + H2O
show the reaction diagram
-
beta-subunit of the bienzyme complex, beta-reaction
-
?
L-serine + indole
L-tryptophan + H2O
show the reaction diagram
-
beta-subunit of the bienzyme complex, beta-reaction
-
?
L-serine + indole
L-tryptophan + H2O
show the reaction diagram
-
beta-subunit of the bienzyme complex, beta-reaction
-
?
L-serine + indole
L-tryptophan + H2O
show the reaction diagram
-
beta-subunit of the bienzyme complex, beta-reaction
-
?
L-serine + indole
L-tryptophan + H2O
show the reaction diagram
-
beta-subunit of the bienzyme complex, beta-reaction
-
?
L-serine + indole
L-tryptophan + H2O
show the reaction diagram
-
beta-subunit of the bienzyme complex, beta-reaction
-
?
L-serine + indole
L-tryptophan + H2O
show the reaction diagram
-
beta-subunit of the bienzyme complex, beta-reaction
-
?
L-serine + indole
L-tryptophan + H2O
show the reaction diagram
-
beta-subunit of the bienzyme complex, beta-reaction
-
?
L-serine + indole
L-tryptophan + H2O
show the reaction diagram
-
beta-subunit of the bienzyme complex, beta-reaction
-
?
L-serine + indole
L-tryptophan + H2O
show the reaction diagram
-
beta-subunit of the bienzyme complex, beta-reaction
-
?
L-serine + indole
L-tryptophan + H2O
show the reaction diagram
-
beta-subunit of the bienzyme complex, beta-reaction
-
?
L-serine + indole
L-tryptophan + H2O
show the reaction diagram
-
beta-subunit of the bienzyme complex, beta-reaction
-
?
L-serine + indole
L-tryptophan + H2O
show the reaction diagram
-
beta-subunit of the bienzyme complex, beta-reaction
-
?
L-serine + indole
L-tryptophan + H2O
show the reaction diagram
-
beta-subunit of the bienzyme complex, beta-reaction
-
?
L-serine + indole
L-tryptophan + H2O
show the reaction diagram
-, Q8U094
beta-subunit of the bienzyme complex, beta-reaction
-
?
L-serine + indole
L-tryptophan + H2O
show the reaction diagram
-
beta-subunit of the bienzyme complex, beta-reaction
-
?
L-serine + indole
L-tryptophan + H2O
show the reaction diagram
-
beta-subunit of the bienzyme complex, beta-reaction
-
?
L-serine + indole
L-tryptophan + H2O
show the reaction diagram
-
beta-subunit of the bienzyme complex, beta-reaction
-
?
L-serine + indole
L-tryptophan + H2O
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
beta-subunit of the bifunctional enzyme complex, beta-reaction
-
?
L-serine + indole
L-tryptophan + H2O
show the reaction diagram
-
beta-subunit of the bifunctional enzyme complex, beta-reaction
-
?
L-serine + indole
L-tryptophan + H2O
show the reaction diagram
-
beta reaction
-
-
ir
L-serine + indole
L-tryptophan + H2O
show the reaction diagram
Arabidopsis thaliana Col-0
Q9FFW8
-
-
-
?
L-serine + indole
L-tryptophan + H2O
show the reaction diagram
Escherichia coli MG1655
-
-
-
-
?
L-serine + indole
L-tryptophan + H2O
show the reaction diagram
Zea mays B73
-
-
-
-
?
L-serine + indole
tryptophan + H2O
show the reaction diagram
-
-
-
-
?
L-serine + indole
tryptophan + H2O
show the reaction diagram
-
beta-subunit of the bienzyme complex, beta-reaction
-
?
L-serine + indole
L-tryptophan
show the reaction diagram
-
-
-
-
-
L-serine + indoline
dihydroiso-L-tryptophan
show the reaction diagram
-
wild-type and mutant D305A enzymes
-
?
L-serine + indoline
dihydro-iso-L-tryptophan + H2O
show the reaction diagram
-
-
i.e. DIT
?
L-serine + indoline
dihydroiso-L-tryptophan + H2O
show the reaction diagram
-
-
i.e. DIT
?
serine + indole
tryptophan + H2O
show the reaction diagram
-
-
-
?
L-tryptophan + D-glyceraldehyde 3-phosphate + H2O
indole-3-glycerol phosphate + L-serine
show the reaction diagram
-
r
r
-
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
?
-
-
enzyme switches between open inactive conformation and closed active conformation, overview
-
?
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
?
-
-
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
?
-
-
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
?
-
-
structure-activity relationship dependent on temperature for alpha- and 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
?
-
-
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
?
-
-
catalyzed reaction and structure of the tryptophan synthase complex, overview
-
-
-
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
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
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
show the reaction diagram
-
-
-
-
?
(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine
L-tryptophan + D-glyceraldehyde 3-phosphate + H2O
show the reaction diagram
-, Q659I8
-
-
-
?
1-(indol-3-yl)glycerol 3-phosphate
D-glyceraldehyde 3-phosphate + indole
show the reaction diagram
-
alpha-subunit of the bienzyme complex, alpha-reaction
-
?
1-(indol-3-yl)glycerol 3-phosphate
D-glyceraldehyde 3-phosphate + indole
show the reaction diagram
-
alpha-subunit of the bienzyme complex, alpha-reaction
-
?
1-(indol-3-yl)glycerol 3-phosphate + L-serine
L-tryptophan + D-glyceraldehyde 3-phosphate + H2O
show the reaction diagram
-
-
-
-
?
1-(indol-3-yl)glycerol 3-phosphate + L-serine
L-tryptophan + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
alpha-subunit of the bienzyme complex, alpha-reaction
-
?
L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate
L-tryptophan + glyceraldehyde 3-phosphate + H2O
show the reaction diagram
-
-
-
-
?
L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate
L-tryptophan + glyceraldehyde 3-phosphate + H2O
show the reaction diagram
-
-
-
-
?
L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate
L-tryptophan + glyceraldehyde 3-phosphate + H2O
show the reaction diagram
-
Trp is a precursor of several important signalling molecules in Pseudomonas spp., overview
-
-
?
L-serine + indole
L-tryptophan + H2O
show the reaction diagram
-
-
-
-
?
L-serine + indole
L-tryptophan + H2O
show the reaction diagram
-
beta-subunit of the bienzyme complex, beta-reaction
-
?
L-serine + indole
L-tryptophan + H2O
show the reaction diagram
-
beta-subunit of the bienzyme complex, beta-reaction
-
?
L-serine + indole
tryptophan + H2O
show the reaction diagram
-
beta-subunit of the bienzyme complex, beta-reaction
-
?
additional information
?
-
-
last 2 steps of the tryptophan biosynthesis
-
?
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
?
-
-
catalyzed reaction and structure of the tryptophan synthase complex, overview
-
-
-
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
pyridoxal 5'-phosphate
-
2 mol bound per mol of beta2 subunit
pyridoxal 5'-phosphate
-
Km: 0.18 mM
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
forms a Schiff base with the epsilon amino-group of Lys87
pyridoxal 5'-phosphate
-
spectroscopic properties
pyridoxal 5'-phosphate
-
forms an alpha-aminoacrylate Schiffbase intermediate with L-serine
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
-
dependent
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
P0A879
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
-
structure in complex with substrate, overview
pyridoxal 5'-phosphate
-
the coenzyme for reactions catalyzed at the active site of the beta-subunit
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
-
additional information
-
the alpha-subunit contains no prosthetic group
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Cd2+
-, P14671
enzyme is up-regulated in plants treated with Cd2+. Overexpression in Arabidopsis and Solanum lycopersicum confers tolerance to cadmium stress
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+
-
the enzyme contains three Cs+ ions
DL-glycerol 3-phosphate
-
enhances beta-reaction activity of mutant D305N and K167T
K+
-
stimulation, Km: 140 mM
K+
-
monovalent cations are effectors of the 2-step beta-reaction, role in reaction equilibrium and rate-limitation, overview
K+
-
enhances beta-reaction activity of wild-type and mutants, except for mutant D56A
K+
-
has an effect on the conformational equilibrium
Li+
-
has an effect on the conformational equilibrium
Na+
-
monovalent cations are effectors of the 2-step beta-reaction, role in reaction equilibrium and rate-limitation, overview
Na+
-
involved in the thermal stability and activity equilibrium of the enzyme complex, overview
Na+
-
enhances beta-reaction activity of wild-type
Na+
-
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
Na+
-
highest activity with 0.15 M Na+
NaCl
-
ligand binding sites, effector on the action of activators or inhibitors, overview
NH4+
-
enhances beta-reaction activity of all wild-type and mutants
NH4+
-
activates the wild-type enzyme and mutant D305A
NH4+
-
has little effect on the conformational equilibrium
Rb+
-
has an effect on the conformational equilibrium
Mg2+
-
highest activity with 0.18 M Mg2+
additional information
-
effects of Na+ and Cs+ in the intermediate formation between L-serine and aniline
additional information
-
monovalent cations are involved in the thermal stability and activity equilibrium of the enzyme complex, overview
additional information
-
the beta-reaction is influenced by protons, monovalent cations, and alpha-subunit ligands, that modulate the distribution between open and closed conformation
additional information
-
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
additional information
-
the enzyme shows high tolerance to ammonium chloride from hair acid hydrolysis industries waste water, and shows no inhibition by ammonium chloride up to 75 mg/ml
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
4-(2-aminophenylthio)butylphosphonic acid
-
phosphonate inhibitor
4-(2-aminophenylthio)butylphosphonic acid
-
-
4-(2-hydroxy-5-fluorophenylthio)butylphosphonic acid
-
phosphonate inhibitor
4-(2-hydroxy-5-fluorophenylthio)butylphosphonic acid
-
-
4-(2-hydroxyphenylsulfinyl)butylphosphonic acid
-
phosphonate inhibitor
4-(2-hydroxyphenylsulfinyl)butylphosphonic acid
-
-
4-(2-hydroxyphenylthio)-1-butenyl-phosphonic acid
-
-
4-(2-hydroxyphenylthio)-1-butenylphosphoric acid
-
phosphonate inhibitor
4-(2-hydroxyphenylthio)butylphosphonic acid
-
phosphonate inhibitor
4-(2-hydroxyphenylthio)butylphosphonic acid
-
-
5,5'-dithiobis(2-nitrobenzoate)
-
-
alpha-glycerol 3-phosphate
-
alpha-site substrate analogue, reduces the inducing effect caused by monovalent cation effectors
Aniline
-
nucleophilic analogue used in place of indole leads to formation of intermediate, but no amino acid formation
benzimidazole
-
wild-type and mutant D305A enzymes
DL-alpha-glycerol 3-phosphate
-
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
-
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
-
inhibits beta-reaction activity of wild-type and mutant D56A
DL-glycerol 3-phosphate
-
wild-type and mutant enzymes, in presence of monovalent cations
DL-glycerol 3-phosphate
-
inhibits the reaction of indole with the enzyme
indole 3-propanol phosphate
-
-
Indole-3-acetamide
-
allosteric effector, binds to the alpha-subunit, inhibitory on the alpha-reaction
indole-3-acetyl-L-alanine
-
allosteric effector, binds to the beta-subunit
indole-3-acetyl-L-aspartate
-
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
-
inhibitor of the alpha-subunit
indole-3-acetyl-L-valine
-
allosteric effector, binds to the beta-subunit
indole-3-acetyl-L-valine
-
inhibitor of the alpha-subunit
indole-3-acetylglycine
-
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
-
inhibitor of the alpha-subunit
indole-3-acrylate
-
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
indoleacetic acid
-
3.5 mM, 50% inhibition
indoleacrylic acid
-
0.05 mM, 50% inhibition
indolebutanol phosphate
-
competitive in the catalysis of indoleglycerol phosphate cleavage, Ki: 0.0011 mM
indolebutyric acid
-
7.5 mM, 50% inhibition
indoleethanol phosphate
-
competitive in the catalysis of indoleglycerol phosphate cleavage, Ki: 0.05 mM
indolepropanol phosphate
-
competitive in the catalysis of indoleglycerol phosphate cleavage, Ki: 0.004 mM
Indolepropionic acid
-
7.5 mM, 50% inhibition
indolepyruvic acid
-
2.3 mM, 50% inhibition
K+
-
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
Na+
-
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
NH4+
-
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
-
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
-
Protamine sulfate
-
-
-
Urea
-
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
-
inhibition mechanism
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
Cs+
-
wild-type enzyme alpha-site is activated by the formation of the alpha-aminoacrylate Schiff base at the beta-site
guanidine hydrochloride
-
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
-
i.e. GuH+, involved in the thermal stability and activity equilibrium of the enzyme complex, overview
hydroxylamine
-
0.4-1.2 M, 7fold stimulation of alpha subunit
Na+
-
wild-type enzyme alpha-site is activated by the formation of the alpha-aminoacrylate Schiff base at the beta-site
NH4+
-
wild-type enzyme alpha-site is activated by the formation of the alpha-aminoacrylate Schiff base at the beta-site
Tween-80
-
activates at 0.04%
Indole-3-acetamide
-
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
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
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
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, 80C, 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, 80C, recombinant TrpA, alpha-reaction
1.1
-
D-glyceraldehyde 3-phosphate
-
cosubstrate L-Trp, i.e. reverse reaction
7.4e-05
-
Indole
Q9FFW8
recombinant isozyme AtTSBtype2, pH 8.2, 30C
0.007
-
Indole
-
recombinant isozyme TSB type 2, pH 8.2, 30C
0.011
-
Indole
-
cosubstrate L-Ser
0.018
-
Indole
-
cosubstrate L-Ser, presence of 20 mM Na+
0.025
-
Indole
-
pH 7.5, 80C, recombinant (TrpA-TrpB1)2 tetrameric complex, beta-reaction
0.04
-
Indole
-
pH 7.5, 80C, recombinant TrpB1, beta-reaction
0.044
-
Indole
-
cosubstrate L-Ser, presence of 20 mM Li+
0.05
-
Indole
-
cosubstrate L-Ser
0.067
-
Indole
-
cosubstrate L-Ser, presence of 20 mM Cs+
0.07
-
Indole
-
cosubstrate L-Ser
0.094
-
Indole
-
37C, beta-replacement, enzyme in solution
0.095
-
Indole
-
cosubstrate L-Ser, presence of 20 mM K+
0.15
-
Indole
-
37C, beta-replacement, enzyme encapsulated in tetramethylorthosilicate-derived wet silica gels
0.16
-
Indole
-
cosubstrate L-Ser
0.17
-
Indole
-
cosubstrate D-glyceraldehyde 3-phosphate
0.997
-
Indole
-
mutant Q128A
1.013
-
Indole
-
mutant T204A
1.485
-
Indole
-
mutant S249A
2.083
-
Indole
-
mutant S390A
2.342
-
Indole
-
mutant S99A
2.86
-
Indole
-
mutant N250A
2.906
-
Indole
-
mutant Q364A
4.471
-
Indole
-
mutant H100A
5.3
-
L-Ser
-
cosubstrate indole
5.7
-
L-Ser
-
cosubstrate indole
0.14
-
L-serine
-
in the presence of 250 mM NaCl, at pH 8.5 and 25C
0.27
-
L-serine
-
in the presence of 100 mM KCl, at pH 8.5 and 25C
0.52
-
L-serine
-
in the presence of 250 mM NaCl, at pH 7.8 and 25C
0.58
-
L-serine
-
in the presence of 100 mM KCl, at pH 7.8 and 25C
0.98
-
L-serine
-
37C, beta-replacement, enzyme in solution
0.983
-
L-serine
-
mutant T204A
1.052
-
L-serine
-
mutant Q128A
1.16
-
L-serine
-
37C, beta-elimination, enzyme in solution
1.17
-
L-serine
-
37C, beta-replacement, enzyme encapsulated in tetramethylorthosilicate-derived wet silica gels
1.235
-
L-serine
-
mutant S249A
1.41
-
L-serine
-
37C, beta-elimination, enzyme encapsulated in tetramethylorthosilicate-derived wet silica gels
1.6
-
L-serine
-
without monovalent cations, at pH 6.5 and 25C; without monovalent cations, at pH 7.8 and 25C
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 25C
1.9
-
L-serine
-
in the presence of 100 mM CsCl, at pH 8.5 and 25C
1.911
-
L-serine
-
mutant S390A
2.7
-
L-serine
-
without monovalent cations, at pH 8.5 and 25C
3.7
-
L-serine
-
pH 7.5, 80C, 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 25C
5.6
-
L-serine
-
in the presence of 100 mM CsCl, at pH 7.8 and 25C
6.2
-
L-serine
-
recombinant isozyme TSB type 2, pH 8.2, 30C
9
-
L-serine
-
in the presence of 100 mM CsCl, at pH 6.5 and 25C
15.8
-
L-serine
-
mutant H100A
35
-
L-serine
Q9FFW8
recombinant isozyme AtTSBtype2, pH 8.2, 30C
0.02
-
serine
-
serine deaminase reaction
110
-
L-serine
-
pH 7.5, 80C, recombinant TrpB1, beta-reaction
additional information
-
additional information
-
dissociation constants of the beta-subunit combined with the different subunits of wild-type and mutants
-
additional information
-
additional information
-
kinetics of the hydrogen-deuterium exchange reactions
-
additional information
-
additional information
-
kinetics
-
additional information
-
additional information
-
kinetics and temperature-dependence
-
additional information
-
additional information
-
kinetics, wild-type and mutants, isotope effects and effector influence
-
additional information
-
additional information
-
kinetic isotope effects with alpha-2H-L-Ser, and thermodynamics, wild-type and mutant
-
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
-
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
-
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
-
steady state kinetics
-
additional information
-
additional information
-
thermodynamic parameters of subunit association, kinetics
-
additional information
-
additional information
-
kinetics, beta-reaction
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.00017
-
1-(indol-3-yl)glycerol 3-phosphate
-
overall-reaction, pH 7.8, 25C, mutant T183V enzyme
0.00059
-
1-(indol-3-yl)glycerol 3-phosphate
-
alpha-reaction, pH 7.8, 25C, mutant T183V enzyme
0.063
-
1-(indol-3-yl)glycerol 3-phosphate
-
alpha-reaction, pH 7.8, 25C, wild-type enzyme
0.16
-
1-(indol-3-yl)glycerol 3-phosphate
-
overall-reaction, mutant R141A, pH 7.8, 25C
0.174
-
1-(indol-3-yl)glycerol 3-phosphate
-
pH 7.5, 80C, 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, 25C
0.3
-
1-(indol-3-yl)glycerol 3-phosphate
-
alpha-reaction, wild-type, and overall-reaction, wild-type and mutant D305A, pH 7.8, 25C
0.36
-
1-(indol-3-yl)glycerol 3-phosphate
-
alpha-reaction, mutant R141A, pH 7.8, 25C
0.44
-
1-(indol-3-yl)glycerol 3-phosphate
-
alpha-reaction, mutant D305A enzyme, pH 7.8, 25C
0.44
-
1-(indol-3-yl)glycerol 3-phosphate
-
alpha-reaction, mutant D305A, pH 7.8, 25C
2.61
-
1-(indol-3-yl)glycerol 3-phosphate
-
overall-reaction, pH 7.8, 25C, wild-type enzyme
3
6
1-(indol-3-yl)glycerol 3-phosphate
-
overall-reaction, pH 7.8, 25C, 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, 80C, recombinant (TrpA-TrpB1)2 tetrameric complex, alpha-reaction
0.007
-
Indole
Q9FFW8
recombinant isozyme AtTSBtype2, pH 8.2, 30C
0.0102
-
Indole
-
recombinant isozyme TSB type 2, pH 8.2, 30C
0.033
-
Indole
-
beta-reaction, mutant R141A, pH 7.8, 25C
0.88
-
Indole
-
beta-reaction, mutant D305A, pH 7.8, 25C
1.6
-
Indole
-
beta-reaction, wild-type, pH 7.8, 25C
2.531
-
Indole
-
mutant H100A
3.3
-
Indole
-
beta-reaction, pH 7.8, 25C, mutant T183V enzyme; beta-reaction, pH 7.8, 25C, wild-type enzyme
3.3
-
Indole
-
37C, beta-replacement, enzyme encapsulated in tetramethylorthosilicate-derived wet silica gels
3.41
-
Indole
-
cosubstrate L-Ser, presence of 20 mM Na+
4.2
-
Indole
-
pH 7.5, 80C, recombinant TrpB1, beta-reaction
4.27
-
Indole
-
cosubstrate L-Ser, presence of 20 mM Li+
4.51
-
Indole
-
beta-reaction, pH 7.8, 25C, wild-type enzyme
4.85
-
Indole
-
cosubstrate L-Ser, presence of 20 mM K+
5.24
-
Indole
-
beta-reaction, pH 7.8, 25C, mutant T183V enzyme
5.44
-
Indole
-
cosubstrate L-Ser, presence of 20 mM Cs+
6.08
-
Indole
-
beta-reaction, mutant D305A, pH 7.8, 25C
6.427
-
Indole
-
mutant Q364A
10
-
Indole
-
pH 7.5, 80C, recombinant (TrpA-TrpB1)2 tetrameric complex, beta-reaction
10.1
-
Indole
-
37C, 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
1.4
-
indoline
-
overall-reaction, mutant D305A enzyme, pH 7.8, 25C, in presence of 100 mM Cs+
0.00017
-
L-serine
-
overall-reaction, pH 7.8, 25C, mutant T183V enzyme
0.0155
-
L-serine
Q9FFW8
recombinant isozyme AtTSBtype2, pH 8.2, 30C
0.0223
-
L-serine
-
recombinant isozyme TSB type 2, pH 8.2, 30C
0.15
-
L-serine
-
37C, beta-elimination, enzyme encapsulated in tetramethylorthosilicate-derived wet silica gels
0.16
-
L-serine
-
37C, beta-replacement, enzyme encapsulated in tetramethylorthosilicate-derived wet silica gels
0.24
-
L-serine
-
without monovalent cations, at pH 6.5 and 25C
0.26
-
L-serine
-
37C, beta-elimination, enzyme in solution
0.4
-
L-serine
-
overall-reaction, mutant D305A enzyme, pH 7.8, 25C, in presence of Na+
0.8
-
L-serine
-
overall-reaction, mutant D305A enzyme, pH 7.8, 25C, in presence of K+
0.88
-
L-serine
-
beta-reaction and overall-reaction, mutant D305A enzyme, pH 7.8, 25C
0.91
-
L-serine
-
without monovalent cations, at pH 7.8 and 25C
1.37
-
L-serine
-
without monovalent cations, at pH 8.5 and 25C
1.6
-
L-serine
-
beta-reaction, wild-type enzyme, pH 7.8, 25C
1.9
-
L-serine
-
in the presence of 250 mM NaCl, at pH 6.5 and 25C; in the presence of 250 mM NaCl, at pH 8.5 and 25C
1.987
-
L-serine
-
mutant H100A
2
-
L-serine
-
overall-reaction, wild-type enzyme, pH 7.8, 25C
2.08
-
L-serine
-
in the presence of 100 mM KCl, at pH 6.5 and 25C
2.61
-
L-serine
-
overall-reaction, pH 7.8, 25C, wild-type enzyme
2.8
-
L-serine
-
in the presence of 250 mM NaCl, at pH 7.8 and 25C
3
6
L-serine
-
overall-reaction, pH 7.8, 25C, wild-type enzyme
3.3
-
L-serine
-
beta-reaction, pH 7.8, 25C, mutant T183V enzyme; beta-reaction, pH 7.8, 25C, wild-type enzyme
3.462
-
L-serine
-
mutant Q364A
3.8
-
L-serine
-
pH 7.5, 80C, recombinant TrpB1, beta-reaction
4
-
L-serine
-
in the presence of 100 mM KCl, at pH 8.5 and 25C
4.51
-
L-serine
-
beta-reaction, pH 7.8, 25C, wild-type enzyme
4.8
-
L-serine
-
in the presence of 100 mM KCl, at pH 7.8 and 25C
5
-
L-serine
-
overall-reaction, mutant D305A enzyme, pH 7.8, 25C, in presence of NH4+
5.24
-
L-serine
-
beta-reaction, pH 7.8, 25C, mutant T183V enzyme
6
-
L-serine
-
in the presence of 100 mM CsCl, at pH 6.5 and 25C
6.08
-
L-serine
-
beta-reaction and overall-reaction, mutant D305A enzyme, pH 7.8, 25C
6.15
-
L-serine
-
in the presence of 100 mM CsCl, at pH 8.5 and 25C
7.106
-
L-serine
-
mutant N250A
7.8
-
L-serine
-
overall-reaction, mutant D305A enzyme, pH 7.8, 25C, in presence of Cs+
8
-
L-serine
-
overall-reaction, wild-type enzyme, pH 7.8, 25C, in presence of Na+
8
-
L-serine
-
pH 7.5, 80C, recombinant (TrpA-TrpB1)2 tetrameric complex, beta-reaction
8.2
-
L-serine
-
37C, beta-replacement, enzyme in solution
8.7
-
L-serine
-
in the presence of 100 mM CsCl, at pH 7.8 and 25C
10.3
-
L-serine
-
overall-reaction, wild-type enzyme, pH 7.8, 25C, in presence of NH4+
10.69
-
L-serine
-
mutant S249A
12
-
L-serine
-
overall-reaction, wild-type enzyme, pH 7.8, 25C, in presence of K+
13.22
-
L-serine
-
mutant S99A
14
-
L-serine
-
overall-reaction, wild-type enzyme, pH 7.8, 25C, in presence of Cs+
16.35
-
L-serine
-
mutant T204A
20.48
-
L-serine
-
mutant S390A
21.47
-
L-serine
-
mutant Q128A
0.06
-
serine
-
serine deaminase reaction
additional information
-
L-serine
-
in the presence of 100 mM CsCl, at pH 8.5 and 25C
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
-
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
12.8
-
glycerol 3-phosphate
-
pH 7.8, 20C
0.95
-
indole-3-acetyl-L-alanine
-
pH 7.8, 20C
1.67
-
indole-3-acetyl-L-aspartate
-
pH 7.8, 20C
0.48
-
indole-3-acetyl-L-valine
-
pH 7.8, 20C
1.2
-
indole-3-acetylglycine
-
pH 7.8, 20C
3.5
-
indoleacetic acid
-
-
0.05
-
indoleacrylic acid
-
-
0.0011
-
indolebutanol phosphate
-
competitive in the catalysis of indoleglycerol phosphate cleavage
7.5
-
indolebutyric acid
-
-
0.05
-
indoleethanol phosphate
-
competitive in the catalysis of indoleglycerol phosphate cleavage
0.004
-
indolepropanol phosphate
-
competitive in the catalysis of indoleglycerol phosphate cleavage
7.5
-
Indolepropionic acid
-
-
2.3
-
indolepyruvic acid
-
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
inhibition kinetics
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.608
-
-
-
2.8
-
-
indole production from 1-(indol-3-yl)glycerol 3-phosphate
8.5
-
-
alpha-reaction, purified enzyme complex
10.53
-
-
-
70
-
-
mutant K167T, in presence of Na+
75
-
-
mutant D56A, in presence of Na+
85
-
-
indole + L-Ser
110
-
-
overall activity, purified enzyme complex
119
-
-
beta-reaction, purified enzyme complex
125
-
-
indole-3-glycerol phosphate + L-serine
190
-
-
wild-type enzyme, in presence of guanidinum
275
-
-
indole + L-Ser
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
-
-
wild-type enzyme in presence of alpha-subunit
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
-
-
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
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7
-
-
alpha-and beta-reaction
7.5
-
-
assay at
7.6
-
-
optimum for the reactions: 1. indole-3-glycerol phosphate + L-Ser, 2. indole + L-Ser
7.8
8
-
beta2 subunit
8
-
-
recombinant enzyme
8.2
-
Q9FFW8
assay at
8.2
-
-
assay at
8.5
-
-
overall reaction
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6
8
-
alpha-subunit
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
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30
60
-
alpha-reaction assay at
30
-
Q9FFW8
assay at
30
-
-
assay at
40
-
-
recombinant enzyme
70
-
-
alpha-reaction
80
-
-
overall reaction
80
-
-
beta-reaction assay at
90
-
-
beta-reaction
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
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 70C, increasing activity from 70C to 100C, at 100C 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
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
terminal, of young plants
Manually annotated by BRENDA team
-
activity highest in shoot tips, less activity in young leaves and internodes, activity declines with maturation
Manually annotated by BRENDA team
additional information
Q9FFW8
while AtTSB1 is the predominantly expressed isoform in vegetative tissues, AtTSB1 and AtTSBtype2 reach similar transcript levels in seeds, tissue-specific expression pattern, overview
Manually annotated by BRENDA team
additional information
-
maize isozyme TSB type 2 is transcribed in various tissues
Manually annotated by BRENDA team
additional information
Arabidopsis thaliana Col-0
-
while AtTSB1 is the predominantly expressed isoform in vegetative tissues, AtTSB1 and AtTSBtype2 reach similar transcript levels in seeds, tissue-specific expression pattern, overview
-
Manually annotated by BRENDA team
additional information
Zea mays B73
-
maize isozyme TSB type 2 is transcribed in various tissues
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
Aquifex aeolicus (strain VF5)
Campylobacter jejuni subsp. jejuni serotype O:2 (strain NCTC 11168)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039)
Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039)
Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039)
Vibrio cholerae serotype O1 (strain M66-2)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
26200
-
-
recombinant TrpA monomer, sedimentation equilibrium
27500
-
-
alpha-subunit monomer, ultracentrifugation sedimentation equilibrium
43530
-
Q60142
calculated from amino acid sequence
50000
-
-
SDS-PAGE, recombinant protein
50220
-
-
mass spectroscopy
84000
88000
-
beta-subunit dimer, ultracentrifugation sedimentation equilibrium
91000
-
-
recombinant TrpB1 dimer, sedimentation equilibrium
98000
-
-
recombinant TrpB2 dimer, sedimentation equilibrium
107800
116500
-
different TrpA-TrpB2i complexes, gel filtration
134500
-
-
gel filtration
140000
-
-
recombinant alphabetabetaalpha complex of TRpA and TrpB1, sedimentation equilibrium
140000
-
-
enzyme complex alpha2beta2, ultracentrifugation sedimentation equilibrium
153000
-
-
sedimentation equilibrium centrifugation
additional information
-
-
determination of Stoke's radii of native, stable intermediates and unfolded conformers of the purified recombinant alpha-subunit dependent on urea concentrations
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
alpha subunit, x * 28800, calculation from amino acid sequence, x * 31000, SDS-PAGE
?
-
89000, B2 subunit, polyacrylamide gel electrophoresis, 2 * 43000, B subunit, SDS-PAGE
?
-
74000, SDS-PAGE
?
-
x * 25600-26300, alpha subunit, ultracentrifugation, SDS-PAGE
?
-
2 * 39700-41000, beta subunit, 1 * 82000, beta2 subunit, ultracentrifugation, SDS-PAGE
?
-
x * 33000 (alpha) + x * 51000 (beta), SDS-PAGE
dimer
-
2 * 74000, SDS-PAGE
dimer
-
2 * 77000, sedimentation equilibrium in 6 M guanidine hydrochloride
dimer
-
recombinant beta-subunit, SDS-PAGE and gel filtration
dimer
-
TrpB2 does not bind to the alpha-subunit and forms homodimers, TrpB1 alone forms homodimers
dimer
-
2 * 42500, recombinant beta-subunit, SDS-PAGE
dimer
-
2 * 50000, SDS-PAGE
heterotetramer
-
2 * 25500 + 2 * 41750, gel filtration
homodimer
P0A879
crystal structure
monomer
-
recombinant alpha-subunit, SDS-PAGE and gel filtration
monomer
-
TrpA alone forms monomers
monomer
-
1 * 27500, recombinant alpha-subunit, SDS-PAGE
tetramer
-
alpha2beta2 complex, structure model
tetramer
-
alpha2beta2 complex
tetramer
-
alpha2beta2 enzyme complex, SDS-PAGE and gel filtration
tetramer
-
alpha2beta2 complex, structure-function relationship
tetramer
-
alpha2beta2 complex, structural organization
tetramer
-
alphabetabetaalpha complex of TRpA and TrpB1, sedimentation equilibrium
tetramer
-
2 * 275000 + 2 * 42500, recombinant alpha2beta2 enzyme complex, SDS-PAGE
tetramer
-
alpha2beta2 enzyme complex
tetramer
-
X-ray crystallography, consists of an alpha2beta2 bienzyme complex with alphabeta dimeric units assembled as the tetrameric species via the beta-beta subunit interface, each alpha-subunit catalyzes the cleavage of 3-indole-D-glycerol 3'-phosphate to indole and D-glyceraldehyde 3-phosphate, the pyridoxal phosphate requiring beta-subunit catalyzes a beta-replacement reaction in which indole replaces the hydroxyl of L-Ser, giving L-Trp
monomer
-
1 * 29000, alpha-subunit, SDS-PAGE
additional information
-
activities of alpha and beta subunits are coordinated by allosteric interactions
additional information
-
kinetics of assembly of subunits
additional information
-
the alpha-subunit contains no disulfide bond, conformational stabilization mechanism
additional information
-
dimer formation seems to be associated with the formation of protein aggregates in vivo
additional information
-
molecular dissection of the alpha-subunit
additional information
-
the alpha-subunit is a TIM barrel protein, structure analysis
additional information
-
crystal structure analysis, structure-function relationship, overview
additional information
-
conformational states, overview, subunit dissociation in presence of guanidinium hydrochloride
additional information
-
structure and conformation regulating the activity and allosteric communication in the enzyme complex, modeling of the high activity closed form and the low activity open form dependent on temperature, conversion from the open to the closed form at high temperature
additional information
-
structure models
additional information
-
salt-bridges extending between the subunits involve alphaAsp56, betaLys167, beta-Asp305, and betaR141
additional information
-
three-dimensional structure of the alphaloop6 in the closed conformation with hydrogen bond between Gly181 ans Ser178
additional information
-
structural analysis, wild-type and mutant beta-subunit dimers, hairpin loop in the beta-subunit, overview
additional information
-
structure and conformation regulating the activity and allosteric communication in the enzyme complex, modeling of the high activity closed form and the low activity open form
additional information
-
recombinantly expressed alpha-subunit forms monomers of 26.7 kDa, while the recombinant beta-subunits B1 and B2 both form dimers of 49.4 and 61.7 kDa, respectively
additional information
-
NMR measurement and determination of wild-type and mutant enzyme structures, complexed with L-tryptophane, in presence or absence of allosteric ligands, such as Na+, NH4+, Cs+, and DL_alpha-glycerol 3-phosphate, overview
additional information
-
high association constant for the hyperthermophile enzyme subunits, pH-dependence of the molecular weights
additional information
-
determination of secondary structure of the isolated alpha-subunit by NMR measurements, the alpha-subunit is a 29 kDa TIM barrel protein, tertiary interactions, overview
additional information
-
(betaalpha)8 TIM barrel protein
additional information
-
the hyperthermophilic archaeon Sulfolobus solfataricus does not contain a TrpB1 protein, as other prototypical tryptophan synthases, but instead two members of the phylogenetically distinct family of TrpB2 proteins, which are encoded within, sTrpB2i, and outside, sTrpB2a, the tryptophan operon. sTrpB2a does not functionally or structurally interact with sTrpA, whereas sTrpB2i substantially activates sTrpA in a unidirectional manner. In the absence of catalysis, no physical complex between sTrpB2i and sTrpA is detected. Stoichiometry of the complex is 1 subunit of sTrpA per 2 subunits of sTrpB2i, which corresponds to a alphabetabeta quaternary structure and testifies to a strong negative cooperativity for the binding of the alpha-monomers to the betabeta-dimer. The alphabetabeta complex remains stable during the whole catalytic cycle and disintegrates into alpha- and betabeta-subunits upon the release of the reaction product tryptophan, structure-function relationship, overview
additional information
-
structure and conformation of the alpha/beta-complex, the isolated monomers show structural flexibility versus the alpha/beta-dimeric unit, H-bond formations in different states, overview
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
10 mg/ml purified recombinant alpha-subunit, hanging drop vapour diffusion method, 298K, equal volume, 0.001 ml, of protein solution and reservoir solution are mixed and placed over 0.5 ml reservoir solution, precipitant solution: 0.5 M ammonium sulfate, 0.1 M trisodium citrate dihydrate, 1.0 M lithium sulfate monohydrate, pH 5.6, first crystals after 7-10 days, maximal size within 2 weeks, X-ray diffraction structure determination and analysis at 2.8 A resolution
-
crystal structures of apo-beta2 and holo-beta2 from Escherichia coli is determined at 3.0 and 2.9 A resolutions. The apo-type and holo-type molecule retain a dimeric form in solution. The subunit structures of both the apo-beta2 and the holo-beta2 forms consist of two domains, (N domain, C domain). The pyridoxal 5-phosphate-bound holo-form has multiple interactions between the two domains and a long loop (residues 260-310), which are missing in the apo-form
P0A879
crystal structures of wild-type and mutant P38L/Y173F alpha-subunit, 2.8 A and 1.8 A resolution, hanging-drop vapour diffusion method
-
hanging drop vapour diffusion method. Crystal structure of the tryptophan synthase alpha-subunit determined at 2.3 A resolution. Structure of tryptophan synthase alpha-subunit from Escherichia coli is compared to structure of alpha2beta2 complex from Salmonella typhimurium
-
wild-type and P28L/Y173F double mutant alpha-subunits are crystallized at 25C by the hanging-drop vapor-diffusion method. X-ray diffraction data are collected to 2.5 A resolution from the wild-type crystals and to 1.8 A from the crystals of the double mutant. The wild-type crystals belonged to the monoclinic space group C2 (a = 155.64 A, b = 44.54 A, c = 71.53 A and beta = 96.39) and the P28L/Y173F crystals to the monoclinic space group P 2(1) (a = 71.09 A, b = 52.70 A, c = 71.52 A, and beta = 91.49). The asymmetric unit of both structures contains two molecules of tryptophan synthase alpha-subunit
-
crystal structure of tryptophan synthase beta2 subunit determined at 2.2 A resolution, hanging drop vapour diffusion method. Crystals belong to the orthorhombic space group P2(1)2(1)2(1) with unit cell dimensions of a = 84.8 A, b = 110.5 A, c = 160.0 A
Q8U093
hanging drop vapour diffusion method, crystal structure of the alpha2beta2 complex, crystals belong to the orthorhombic space group of P2(1)2(1)2(1) with unit cell dimensions of a = 89.1 A, b = 220.3 A, c = 292.6 A
-
purified recombinant alpha-subunit, hanging drop vapour diffusion method, 10C, reservoir solution: 0.1 M MES-NaOH, pH 6.5, 12% PEG 20000, X-ray diffraction structure determination and analysis at 2.0 A resolution
Q8U094
crystal structures of the alpha-subunit of tryptophan synthase alone and in the alpha2beta2 complex
-
crystallization of wild-type and mutant S178P in presence or absence of alpha-subunit ligands, structure comparison
-
crystallization of wild-type enzyme alone and complexed with L-serine and 3-indolylpropanol 3'-phosphate, and of mutant T183V complexed with L-serine, 1-(indol-3-yl)glycerol 3-phosphate, and 3-indolylpropanol 3'-phosphate, hanging drop method in the dark at room temperature, equal volumes of protein solution, containing 10 mg/ml protein, 50 mM Na-bicine, pH 7.8, 10 mM Na-EDTA, 1 mM dithioerythritol, 0.02 mM pyridoxal 5'-phosphate, and of reservoir solution, containing 50 mM Na-bicine, pH 7.8, 5 mM dithioerythritol, 5 mM Na-EDTA, 0.1 mM pyridoxal 5'-phosphate, 2 mM spermine, 8-12% w/v PEG 8000, X-ray diffraction structure determination and analysis at different resolutions 1.45-2.3 A, comparison of crystal structures of the different complexes
-
hanging drop method, 10 mg/ml purified recombinant mutant S178P enzyme in 50 mM bicine, pH 7.8, with equal volume of reservoir solution: 50 mM bicine, 1 mM EDTA, 12% w/v PEG 8000, 1.4 mM spermine, pH 7.8, 21C, structure determination and functional investigation by polarized absorption microspectrophotometry
-
hanging drop vapour diffusion method
-
purified enzyme complexed with allosteric effectors indole-3-acetylglycine and indole-3-acetyl-L-aspartic acid, hanging drop method, in the dark at room temperature, equal volumes of protein and reservoir solution, the latter containing 9-12% PEG 8000, 1.5 mM spermine, 1 mM EDTA, 50 mM bicine, pH 7.8, X-ray diffraction structure determination and analysis at 2.5 A resolution, modeling
-
purified mutant A169L/C170W complexed with the alpha-active site substrate analogue 5-fluoro-indole-propanol-phosphate, X-ray diffraction structure determination and analysis at 2.25 A resolution
-
purified recombinant enzyme complex, structure determination and analysis
-
purified recombinant enzyme in complex with potential alpha-reaction phosphonate inhibitors, 5-10 mg/ml protein mixed with 1 mM inhibitor, in 50 mM bicine, 1 mM Na-EDTA, 0.8-1.5 mM spermine, 12% PEG 4000, to pH 7.8 with NaOH, X-ray diffraction structure determination and analysis at 2.3 A resolution or higher
-
purified recombinant wild-type enzyme alone or in complex with alpha-subunit substrate analogue indole propanol phosphate, 10 mg/ml in 50 mM bicine, pH 7.8, 10 mM Na-EDTA, 0.02 mM pyridoxal 5'-phosphate, 1 mM dithioerythritol, in the dark at room temperature, hanging drop method, equal volumes of protein and reservoir solution, the latter containing 50 mM bicine, pH 7.8, 5 mM dithioerytritol, 5 mM Na-EDTA, 0.1 mM pyridoxal 5'-phosphate, 2 mM spermine, 2 mM NaN3, and 8-12% w/v PEG 8000, with or without 7 mM indole propanol phosphate, X-ray diffraction structure determination and analysis at 1.4 A resolution, structure modeling
-
soaking native crystals for 10 min in a solution containing 90 mM Bis-Tris-propane (pH 7.8), 150 mM NaCl, 15% (w/v) PEG 8000, and 20% glycerol
-
structure and function of alpha subunit, beta subunit, alpha2beta2 complex
-
vapor diffusion method, using 1 mM dithiothreitol, 0.04% (w/v) NaN3, and 12% (w/v) polyethylene glycol 8000
-
crystal structure of alpha-subunit of tryptophan synthase, oil batch method, discussion of the thermostabilization mechanism of the tryptophan synthase alpha-subunit on the basis of crystal structures and DSC data of the alpha-subunit orthologs from mesophilic, extreme thermophilic, and hyperthermophilic organisms
P16608, -
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
37
-
-
30 min, 20% loss of activity
40
80
-
the enzyme activity decreases significantly when the temperature is above 40C. The activity of enzyme incubated at 80C is below 10% of that incubated at 10C
65
-
-
10 min, no loss of activity
67
-
-
10 min, rapid inactivation
additional information
-
-
effect of amino acid substitution at E49 of alpha-subunit on stability
additional information
-
-
denaturation temperatures of alpha subunit; pyridoxal 5'-phosphate stabilizes against thermal inactivation, Schiff-base forming amino acids destabilize holo beta subunit
additional information
-
-
denaturation temperatures of alpha subunit; ligands that promote subunit association (L-Ser, L-Trp, D-Trp) raise the inactivation temperature of alpha subunit
additional information
-
-
thermolabile inhibiting factor can be inactivated by heating to 60C
additional information
-
-
thermodynamic stability of alpha-subunit and N-terminal part of the alpha-subunit during folding and unfolding
additional information
-
-
thermodynamic stability and kinetic
additional information
-
-
heat treatment for purification of the recombinant alpha- and beta-subunits, individually expressed, reveals that both the 2 subunits are required for stabilizationof the activity
additional information
-
Q8U094
the alpha-subunit of the enzyme has extremely high thermostability, due to increase in ion pairs, decrease in cavity volume, and entropic effects, not by hydrophobic interactions
additional information
-
-
inactivation temperature of the alpha-subunit is enhanced by the formation of the enzyme complex alpha2beta2 by 17C
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
glycerol 15% v/v stablizes beta2 subunit
-
pyridoxal 5'-phosphate strongly stabilizes beta2 subunit
-
urea-induced equilibrium unfolding reaction
-
influence of ionic strength, stable in 1 M phosphate buffer, instable in 0.1M or 0.01 M phosphate buffer
-
binding of allosteric ligands stabilizes the enzyme's conformation
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-20C, lyophilized, several months stable
-
-20C, beta2-subunit, potassium phosphate buffer pH 6.5-6.6, EDTA, 2-mercaptoethanol, pyridoxal 5'-phosphate
-
0C, in cellulose triacetate, 6 months
-
-20C, frozen solution or suspension in 50% saturated ammonium sulfate, 40% residual activity after 3 years
-
4C, 1 M potassium phosphate buffer, pH 7.6, 1 mM pyridoxal 5'-phosphate, 2 mM PMSF, 24 h, 7% loss of activity
-
-20C, beta subunit, 50 mM sodium bicine buffer, pH 7.8, 1 mM EDTA, 0.04 mM pyridoxal 5'-phoshate, 2 mM DTT
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
recombinant isozyme AtTSBtype2 from Escherichia coli by nickel affinity chromatography
Q9FFW8
alpha subunit
-
beta2 subunit
-
DEAE-cellulose column chromatography and heparin-Sepharose column chromatography
-
alpha subunit
-
alpha2beta2 holoenzyme, beta2 holoenzyme, beta2 apoenzyme, alpha subunit
-
beta2 subunit
-
recombinant alpha-subunit
-
recombinant alpha-subunit and N-terminal part of the alpha-subunit of the enzyme, to over 95% purity
-
recombinant alpha-subunits of wild-type and mutant enzymes
-
soluble and refolded, solubilized recombinant alpha-subunit from expression in strain BL21(DE3)
-
using metal affinity chromatography
-
mutant enzyme
-
partial
-
alpha2,beta2 complex and dissociation into its subunits
-
recombinant alpha-subunit from Escherichia coli
Q8U094
recombinant alpha-subunit, beta-subunit, and enzyeme complex expressed in Escherichia coli
-
alpha2beta2 holoenzyme, beta2 holoenzyme, beta2 apoenzyme, alpha subunit
-
PD-10 column chromatography, desalting
-
recombinant alpha- and beta-subunits coexpressed in Escherichia coli, separation of alpha-subunit from beta-subunit by acid precipitation of the beta-subunit at pH 4.5, separation beta-subunit from alpha-subunit by heat denaturation of the alpha-subunit at 63C and pH 7.8
-
recombinant enzyme complex from Escherichia coli
-
recombinant mutant S178P from Escherichia coli
-
recombinant wild-type enzyme complex and of the beta-subunit dimer from Escherichia coli CB149
-
native enzyme complex, and recombinant alpha- and beta-subunit from expression in Escherichia coli
-
recombinant TrpA, TrpB1, and TrpB2 from Escherichia coli
-
recombinant isozyme ZmTSBtype2 from Escherichia coli by nickel affinity chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expressed in Escherichia coli
-
glutathione S-transferase fusion protein with alpha and beta subunits
-
isolation of alpha subunit mutants
-
overexpression in Arabidopsis and Solanum lycopersicum confers tolerance to cadmium stress
-, P14671
TSB phylogenetic analysis and tree, functional expression of isozyme AtTSBtype2 in Escherichia coli
Q9FFW8
expressed in Escherichia coli
-
alpha-subunit
-
DNA and amino acid sequence determination of the alpha-subunit of the enzyme, overexpression of the alpha-subunit and the larger N-terminal part of the alpha-subunit, amino acid residues 1-188, in inclusion bodies
-
expression in Escherichia coli strain BL21(DE3)
-
expression of the alpha-subunit in strain BL21(DE3) as soluble and insoluble protein
-
expression of wild-type and mutant F139W, T24M/F139W, and T24L/F139W alpha-subunits as monomers, expression of mutant T24A/F139W, T24S/F139W and T24K/F139W alpha-subunits as soluble dimers in strain RB797
-
overexpression of the alpha-subunit in strain RB797
-
wild-type and P28L/Y173F double mutant alpha-subunits are overexpressed in Escherichia coli
-
into the pDrive Cloning vector and into the pCRII vector
-, Q659I8
over-expressed in Mycobacterium tuberculosis H37Rv as a His-tagged fusion protein
-
genes trpA encoding the alpha-subunit and trpB encoding the beta-subunit are coexpressed or expressed individually in Escherichia coli strain JM109
-
overexpression of the alpha-subunit in Escherichia coli
Q8U094
Escherichia coli pretransformed with pSTB7, a high copy number plasmid expressing tryptophan synthase from Salmonella enterica, is commercially available (ATCC 37845)
-
expressed in Escherichia coli
-
coexpression of trpA and trp, encoding the alpha- and beta-subunit of the enzyme in Escherichia coli strain CB149 lacking the trp operon
-
expression of the enzyme complex in Escherichia coli
-
expression of wild-type and mutants enzymes in Escherichia coli
-
expression of wild-type enzyme complex and of the beta-subunit dimer in Escherichia coli CB149
-
expressionof mutant S178P in Escherichia coli
-
tryptophan synthase alpha2beta2 complex from Salmonella typhimurium is prepared from Escherichia coli containing the plasmid pEBA-10
-
genes trpA and trpB2i, expression of wild-type alpha- and beta-subunits, sTrpA and sTrpB2i, and of TrpA mutants in Escherichia coli strain Bl21(DE3)
-
expressed in Escherichia coli trpB point mutant (YS111) cells
-
independent expression of alpha- and beta-subunit encoded by genes Tk-trpA and Tk-trpB in Escherichia coli
-
genes trpA, trpB1, and trpB2, expression in Escherichia coli
-
expression in Escherichia coli BL21(DE3)
P16608, -
TSB phylogenetic analysis and tree, functional expression of isozyme ZmTSBtype2 in Escherichia coli
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
C170F
-
beta subunit, indole is channelled from the alpha site to the beta site in the physiologically relevant alphabeta reaction
D305A
-
mutation of a beta-subunit residue, no active site residue, altered subunit interaction
E109D
-
mutation of a beta-subunit active site residue, reduced reach and conformational freedom of the carboxylate functionality, accumulation of indole at the beta-site
E49X
-
effect of amino acid substitution at E49 of alpha-subunit on stability
F139W
-
replacement of Phe with Trp does not alter the stability to urea
F139W
-
kinetics of unfolding of alpha subunit
F139W
-
oligonucleotide-directed mutagenesis, recombinant alpha-subunit mutant, forms monomers
F258W
-
replacement of Phe with Trp does not alter the stability to urea
F258W
-
kinetics of unfolding of alpha subunit
F280A
-
beta-subunit dimers, unaltered activity compared to the wild-type enzyme
F280G
-
beta-subunit dimers, 72% reduced activity compared to the wild-type enzyme
F280P
-
beta-subunit dimers, 94% reduced activity compared to the wild-type enzyme
G281A
-
beta-subunit dimers, 46% reduced activity compared to the wild-type enzyme
G281R
-
reduced activity and weak association with alpha subunit
G281R
-
beta2 subunit, shift of pH-optimum from 7.5 to 9.8, mutant stimulated by NH4+
H273A
-
beta-subunit dimers, 2fold increased activity compared to the wild-type enzyme
I278A
-
beta-subunit dimers, 70% reduced activity compared to the wild-type enzyme
I278A/K283A
-
beta-subunit dimers, 92% reduced activity compared to the wild-type enzyme
I278V
-
beta-subunit dimers, 7% reduced activity compared to the wild-type enzyme
I278V/K283A
-
beta-subunit dimers, 35% reduced activity compared to the wild-type enzyme
I37A
P0A877
mutant lacks the hundreds of milliseconds unfolding reaction under strongly refolding conditions
I41A
P0A877
mutant lacks the hundreds of milliseconds unfolding reaction under strongly refolding conditions
I95A
P0A877
mutant lacks the hundreds of milliseconds unfolding reaction under strongly refolding conditions
I97A
P0A877
mutant lacks the hundreds of milliseconds unfolding reaction under strongly refolding conditions
K283A
-
beta-subunit dimers, 41% reduced activity compared to the wild-type enzyme
K87T
-
mutation of a beta-subunit active site residue, inactive mutant, which can form an external aldimine, but cannot form an alpha-aminoacrylate intermediate
L25A
P0A877
mutant lacks the hundreds of milliseconds unfolding reaction under strongly refolding conditions
L48A
P0A877
mutant lacks the hundreds of milliseconds unfolding reaction under strongly refolding conditions
L50A
P0A877
mutant lacks the hundreds of milliseconds unfolding reaction under strongly refolding conditions
L85A
P0A877
mutant lacks the hundreds of milliseconds unfolding reaction under strongly refolding conditions
L99A
P0A877
mutant lacks the hundreds of milliseconds unfolding reaction under strongly refolding conditions
M282A
-
beta-subunit dimers, 61% reduced activity compared to the wild-type enzyme
P132A
-
increase of activity of the alpha2beta2 complex
P132G
-
increase of activity of the alpha2beta2 complex
P28L/Y173F
-
wild-type crystals belonged to the monoclinic space group C2 (a = 155.64 A, b = 44.54 A, c =71.53 A and beta = 96.39) and the P28L/Y173F crystals to the monoclinic space group P 2(1) (a = 71.09 A, b = 52.70 A, c = 71.52 A, and beta = 91.49). The asymmetric unit of both structures contains two molecules of tryptophan synthase alpha-subunit
P38L/Y173F
-
P28L substitution induces the exposure of hydrophobic amino acids and decreases the secondary structure that causes the aggregation. The Y173E mutation suppresses to transfer a signal from the alpha-subunit core to the alpha-subunit surface involved in interactions with the beta-subunit and increases structural stability
P57A
-
increase of activity of the alpha2beta2 complex
R275A
-
beta-subunit dimers, 37% reduced activity compared to the wild-type enzyme
T24A/F139W
-
oligonucleotide-directed mutagenesis, recombinant alpha-subunit mutant, forms dimers
T24K/F139W
-
oligonucleotide-directed mutagenesis, recombinant alpha-subunit mutant, forms dimers
T24L/F139W
-
oligonucleotide-directed mutagenesis, recombinant alpha-subunit mutant, forms monomers
T24M/F139W
-
oligonucleotide-directed mutagenesis, recombinant alpha-subunit mutant, forms monomers
T24S/F139W
-
oligonucleotide-directed mutagenesis, recombinant alpha-subunit mutant, forms dimers
V23A
P0A877
mutant lacks the hundreds of milliseconds unfolding reaction under strongly refolding conditions
V276A
-
beta-subunit dimers, 46% reduced activity compared to the wild-type enzyme
V276A/K283A
-
beta-subunit dimers, 48% reduced activity compared to the wild-type enzyme
Y173F
-
oligonucleotide-directed mutagenesis, gene trpA, alpha-subunit residue exchange, altered fluorescence and folding properties
Y175F
-
oligonucleotide-directed mutagenesis, gene trpA, alpha-subunit residue exchange, altered fluorescence and folding properties
Y279A
-
beta-subunit dimers, 50% reduced activity compared to the wild-type enzyme
Y279F
-
beta-subunit dimers, 33% reduced activity compared to the wild-type enzyme
Y279L
-
beta-subunit dimers, 48% reduced activity compared to the wild-type enzyme
Y279P
-
beta-subunit dimers, 46% reduced activity compared to the wild-type enzyme
H100A
-
Km (indole), (L-serine) higher than wild-type, kcat (indole), (L-serine) significantly decreased compared to wild-type
N250A
-
Km (indole), (L-serine) higher than wild-type, kcat (indole), (L-serine) lower compared to wild-type
Q128A
-
Km (indole), (L-serine) higher than wild-type, kcat (indole) slightly lower than wild-type, kcat (L-serine) lower compared to wild-type
Q364A
-
Km (indole), (L-serine) higher than wild-type, kcat (indole), (L-serine) significantly decreased compared to wild-type
S249A
-
Km (indole), (L-serine) higher than wild-type, kcat (indole), (L-serine) lower compared to wild-type
S390A
-
Km (indole), (L-serine) higher than wild-type, kcat (indole), (L-serine) lower compared to wild-type
S99A
-
Km (indole), (L-serine) higher than wild-type, kcat (indole), (L-serine) lower compared to wild-type
T204A
-
Km (indole), (L-serine) higher than wild-type, kcat (indole), (L-serine) lower compared to wild-type
A169L/C170W
-
mutants of beta-subunit residues, altered kinetic properties and conformation
D124A
-
mutation significantly perturbs the secondary and tertiary structure
D130A
-
mutation significantly perturbs the secondary and tertiary structure
D305A
-
mutation of a salt-bridging residue of the beta-subunit, substitution decreases the affinity of the beta-site for the substrate L-serine, destabilizes the enzyme-bound alpha-aminoacrylate, and quinoid species, and changes the nucleophile specificity of the beta-reaction, increased rate of pyruvate formation compared to the wild-type enzyme
D305A
-
forms a bienzyme complex with impaired allosteric communication, altered beta-site substrate reaction specificity, the Na+ form of the alpha-site of the mutant is no longer activated by the formation of the alpha-aminoacrylate Schiff base at the beta-site, but this can be restored by replacing Na+ with NH4+ or Cs+
D305A
-
much broader substrate specificity for nucleophiles than the wild type enzyme
D305A
-
mutations that affects the allosteric equilibrium also has a dramatic effect on the reaction volume (DELTA V0)
D305N
-
site-directed mutagenesis, residue is involved in formation of salt bridges between the different subunits, kinetic and structural, conformational alterations, altered signaling by ligand binding, overview
D46A
-
mutation significantly perturbs the secondary and tertiary structure
D56A
-
site-directed mutagenesis, residue is involved in formation of salt bridges between the different subunits, kinetic and structural, conformational alterations, altered signaling by ligand binding, overview
D56A
-
site-directed mutagenesis, mutation in the alpha-subunit, replacement of the residue, which builds a salt bridge to the alpha-subunit, has deleterious effects, which can be repaired by increased temperature in combination with CsCl or NaCl plus alpha-glycerol 3-phosphate, an alpha-ligand, alteration of temperature dependence of the enzyme complex
D60Y
-
mutation inhibits the ligand-induced transition of the alpha subunit from an open to a closed conformation that serves to block the tunnel for the metabolite chanelling
E109A
-
catalytic activity with beta-chloro-L-Ala, but negligible activity with L-Ser, beta subunit
E109D
-
catalytic activity with beta-chloro-L-Ala, but reduced activity with L-Ser, beta subunit
E109D
-
modest but significant effects of 40 to 2000fold on the conformational equilibrium
E109D
-
mutations that affects the allosteric equilibrium also has a dramatic effect on the reaction volume (DELTA V0)
E49F
-
mutation inhibits the ligand-induced transition of the alpha subunit from an open to a closed conformation that serves to block the tunnel for the metabolite chanelling
F280A
-
beta-subunit dimers, unaltered activity compared to the wild-type enzyme
F280G
-
beta-subunit dimers, 72% reduced activity compared to the wild-type enzyme
F280P
-
beta-subunit dimers, 94% reduced activity compared to the wild-type enzyme
G181A
-
2fold decrease of activity compared to the wild type enzyme
G181F
-
mutant shows a significant change in the alphaloop6 structure
G181P
-
site-directed mutagenesis, replacement of an alphaloop6 residue, loss of the hydrogen bond between residues alphaG181 and betaS178 does not influence the intersubunit catalytic activity, but completely abolishes ligand-induced intersubunit signaling, stabilization of the inactive open conformation of the alpha-active site
G181P
-
mutant shows a significant change in the alphaloop6 structure
G181V
-
mutant shows a significant change in the alphaloop6 structure
G281A
-
beta-subunit dimers, 46% reduced activity compared to the wild-type enzyme
G51L
-
mutation inhibits the ligand-induced transition of the alpha subunit from an open to a closed conformation that serves to block the tunnel for the metabolite chanelling
H273A
-
beta-subunit dimers, 2fold increased activity compared to the wild-type enzyme
H86L
-
site-directed mutagenesis, exchange of His86, located adjacent to beta subunit Lys87, which forms an intermediate with the pyridoxal 5'-phosphate, leads to 20fold reduced binding of the cofactor and reduced formation the reaction intermediate, altered pH-profile
I278A
-
beta-subunit dimers, 70% reduced activity compared to the wild-type enzyme
I278A/K283A
-
beta-subunit dimers, 92% reduced activity compared to the wild-type enzyme
I278V
-
beta-subunit dimers, 7% reduced activity compared to the wild-type enzyme
I278V/K283A
-
beta-subunit dimers, 35% reduced activity compared to the wild-type enzyme
K167T
-
site-directed mutagenesis, residue is involved in formation of salt bridges between the different subunits, kinetic and structural, conformational alterations, altered signaling by ligand binding, overview
K167T
-
site-directed mutagenesis, mutation in the beta-subunit, replacement of the residue, which builds a salt bridge to the alpha-subunit, has deleterious effects, which can be repaired by increased temperature in combination with CsCl or NaCl plus alpha-glycerol 3-phosphate, an alpha-ligand, alteration of temperature dependence of the enzyme complex
K283A
-
beta-subunit dimers, 41% reduced activity compared to the wild-type enzyme
K87T
-
Lys87 represents an essential catalytic residue as acceptor of the alpha-proton of L-Ser, alpha subunit
M282A
-
beta-subunit dimers, 61% reduced activity compared to the wild-type enzyme
M282P
-
beta-subunit dimers, inactive mutant
R141A
-
forms a bienzyme complex with impaired allosteric communication, impaired beta-site catalytic acitivity, the Na+ form of the alpha-site of the mutant is no longer activated by the formation of the alpha-aminoacrylate Schiff base at the beta-site, no restoration by NH4+ or Cs+
R179L
-
mutation inhibits the ligand-induced transition of the alpha subunit from an open to a closed conformation that serves to block the tunnel for the metabolite chanelling
R275A
-
beta-subunit dimers, 37% reduced activity compared to the wild-type enzyme
S178P
-
site-directed mutagenesis, replacement of an betahelix6 residue, loss of the hydrogen bond between residues alphaG181 and betaS178 does not influence the intersubunit catalytic activity, but completely abolishes ligand-induced intersubunit signaling, stabilization of the inactive open conformation of the alpha-active site
S178P
-
site-directed mutagenesis, molecular modeling of the structural effects caused by the mutation, hydrogen bond with alphaGlu181 is interrupted, 2fold decreased activity of the beta-subunit, not affected, in contrast to the wild-type, by allosteric effectors indole-3-acetylglycine and DL-alpha-glycerol-3-phosphate in the beta-reaction, weaker binding of Na+
T183V
-
site-directed mutagenesis, isosteric alpha-subunit mutant, exchange of a highly conserved residue, strongly impaired allosteric alpha-beta communication, 100fold reduced alpha-reaction activity, beta-reaction activity is not affected, effects are due to a missing hydrogen bind between alphaT183 and the catalytic residue alphaAsp60
V276A
-
beta-subunit dimers, 46% reduced activity compared to the wild-type enzyme
V276A/K283A
-
beta-subunit dimers, 48% reduced activity compared to the wild-type enzyme
Y279A
-
beta-subunit dimers, 50% reduced activity compared to the wild-type enzyme
Y279F
-
beta-subunit dimers, 33% reduced activity compared to the wild-type enzyme
Y279L
-
beta-subunit dimers, 48% reduced activity compared to the wild-type enzyme
Y279P
-
beta-subunit dimers, 46% reduced activity compared to the wild-type enzyme
S206C
-
site-directed mutagenesis of subunit sTrpA, complex formation with subunit TrpB2i compared to wild-type TrpA
S229C
-
site-directed mutagenesis of subunit sTrpA, complex formation with subunit TrpB2i compared to wild-type TrpA
W65F
-
site-directed mutagenesis of subunit sTrpA, complex formation with subunit TrpB2i compared to wild-type TrpA
W88F
-
site-directed mutagenesis of subunit sTrpA, complex formation with subunit TrpB2i compared to wild-type TrpA
additional information
-, P14671
Trp-overproducing mutant trp5-1 is associated with high chlorophyll levels and low lipid peroxidation. The Trp-auxotroph mutant trp2-1 is sensitive to Cd2+
additional information
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the trp2-8 and trp2-5 mutants have the most dramatically reduced accumulation of TSB mRNA (7% and 34% of wild type, respectively). In contrast, trp2-9 and trp2-10 plants have modest, but reproducible, enhancement of TSB RNA (28% and 40% higher than the wild type, respectively). TSB protein levels in the trp2 mutants vary from very low (13% of wild type for trp2-5 and 15% for trp2-8) to significantly greater than that of wild type (50-60% higher for trp2-10, trp2-100and trp2-102)
additional information
Q9FFW8
construction of Attsbtype2 T-DNA insertion mutants,SALK lines 011904, 124293, 082810, and 162268, that show no obvious deviation from the wild-type
additional information
Arabidopsis thaliana Col-0
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construction of Attsbtype2 T-DNA insertion mutants,SALK lines 011904, 124293, 082810, and 162268, that show no obvious deviation from the wild-type
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M282P
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beta-subunit dimers, inactive mutant
additional information
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enzymatic properties of 93 mutants of the alpha subunit
additional information
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hydrogen-to-deuterium exchange in alpha-tryptophan synthase
Renatured/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
cooperative unfolding and 2-phase refolding mechanism and kinetics of the alpha-subunit and the N-terminas of the alpha-subunit alone, denaturing by urea at 25C
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denaturation of recombinant wild-type and mutant alpha-subunit monomers and dimers with urea, refolding of all forms as monomers
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insoluble rcombinant alpha-subunit, expressed in strain BL212(DE3), is denatured by 6 M urea, refolding
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the refolding of urea-denatured alpha-subunit of tryptophan synthase from Escherichia coli is monitored by pulse-quench hydrogen exchange mass spectrometry. An intermediate builds up rapidly and decays slowly over the first 100 seconds of folding, obligatory nature of the intermediate, the latter stages of the folding reaction of alpha-subunit of tryptophan synthase are under thermodynamic control
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unfolding and refolding of wild-type and mutant alpha-subunits using urea, comparison of the folding process differences, thermodynamic parameters
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urea-induced equilibrium unfolding reaction
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APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
synthesis
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Recycling of hair by acid hydrolysis has enormous economic importance. Enzymatic synthesis of L-tryptophan from hair acid hydrolysis industries wastewater with tryptophan synthase. The L-serine conversion rate reaches 95.1% with a final L-tryptophan concentration of 33.2 g/l
synthesis
Escherichia coli MG1655
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Recycling of hair by acid hydrolysis has enormous economic importance. Enzymatic synthesis of L-tryptophan from hair acid hydrolysis industries wastewater with tryptophan synthase. The L-serine conversion rate reaches 95.1% with a final L-tryptophan concentration of 33.2 g/l
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analysis
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the enzyme complex is a model enzyme for understanding allosteric regulation
biotechnology
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enzyme is a target for structure-based design of herbicides