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 hide
4.2.1.20
-
RECOMMENDED NAME
GeneOntology No.
tryptophan synthase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
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
L-serine + indole = L-tryptophan + H2O
show the reaction diagram
(1b)
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
addition
-
-
-
-
C-O bond cleavage
-
-
condensation
elimination
-
-
of H2O, of NH3, C-O bond cleavage
-
replacement
-
-
beta-position of amino acid
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Biosynthesis of antibiotics
-
-
Biosynthesis of secondary metabolites
-
-
Glycine, serine and threonine metabolism
-
-
Metabolic pathways
-
-
Phenylalanine, tyrosine and tryptophan biosynthesis
-
-
tryptophan metabolism
-
-
SYSTEMATIC NAME
IUBMB Comments
L-serine hydro-lyase [adding 1-C-(indol-3-yl)glycerol 3-phosphate; L-tryptophan and glyceraldehyde-3-phosphate-forming]
A pyridoxal-phosphate protein. The alpha-subunit catalyses the conversion of 1-C-(indol-3-yl)glycerol 3-phosphate to indole and D-glyceraldehyde 3-phosphate (this reaction was included formerly under EC 4.1.2.8). The indole migrates to the beta-subunit where, in the presence of pyridoxal 5'-phosphate, it is combined with L-serine to form L-tryptophan. In some organisms this enzyme is part of a multifunctional protein that also includes one or more of the enzymes EC 2.4.2.18 (anthranilate phosphoribosyltransferase), EC 4.1.1.48 (indole-3-glycerol-phosphate synthase), EC 4.1.3.27 (anthranilate synthase) and EC 5.3.1.24 (phosphoribosylanthranilate isomerase). In thermophilic organisms, where the high temperature enhances diffusion and causes the loss of indole, a protein similar to the beta subunit can be found (EC 4.2.1.122). That enzyme cannot combine with the alpha unit of EC 4.2.1.20 to form a complex.
CAS REGISTRY NUMBER
COMMENTARY hide
9014-52-2
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
isozymes AtTSB1 and AtTSBtype2
UniProt
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
strain CB149
Uniprot
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
-
-
-
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
HB8
Uniprot
Manually annotated by BRENDA team
Vitis vinifera x Vitis riparia
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-
-
Manually annotated by BRENDA team
Vitis vinifera x Vitis vinifera
-
-
-
Manually annotated by BRENDA team
isozyme TSB type 2
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-
Manually annotated by BRENDA team
isozyme TSB type 2
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-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
-
the family of trpB2 genes, identified in the genomes of several microorganisms and plants, can be further divided into the trpB2i, located within the tryptophan operon, and the trpB2o/trpB2a, located outside the operon, subfamilies. The deduced amino acid sequence identities within and between the TrpB1 andTrpB2 families are about 60% and 30%, respectively
malfunction
Q9YGA9 and Q5JDJ1, Q9YGA9 and Q9YGB0
tryptophan synthase is composed of subunit TrpA and subunit TrpB. Thermococcus kodakarensis possess two paralogs of subunit B, TrpB1 and TrpB2. TrpB1 and TrpB2 both contribute to Trp biosynthesis. TrpB2 catalyzes the TrpB reaction but does not interact with TrpA as in the case of TrpB1. The double-deletion mutant (DELTAtrpB1DELTAtrpB2) displays Trp auxotrophy, whereas individual single mutants (DELTAB1 and DELTAB2 strains) do not; tryptophan synthase is composed of subunit TrpA and subunit TrpB. Thermococcus kodakarensis possess two paralogs of subunit B, TrpB1 and TrpB2. TrpB1 and TrpB2 both contribute to Trp biosynthesis. TrpB2 catalyzes the TrpB reaction but does not interact with TrpA as in the case of TrpB1. The double-deletion mutant (DELTAtrpB1DELTAtrpB2) displays Trp auxotrophy, whereas individual single mutants (DELTAB1 and DELTAB2 strains) do not
metabolism
Q9YGA9 and Q5JDJ1, Q9YGA9 and Q9YGB0
the last two steps of L-tryptophan biosynthesis are catalyzed by Trp synthase, a heterotetramer composed of TrpA and TrpB. TrpB catalyzes the condensation of indole, synthesized by TrpA, and serine to Trp. Thermococcus kodakarensis possesses two paralogs of subunit B, TrpB1 and TrpB2. TrpB1 and TrpB2 both contribute to Trp biosynthesis; the last two steps of L-tryptophan biosynthesis are catalyzed by Trp synthase, a heterotetramer composed of TrpA and TrpB. TrpB catalyzes the condensation of indole, synthesized by TrpA, and serine to Trp. Thermococcus kodakarensis possesses two paralogs of subunit B, TrpB1 and TrpB2. TrpB1 and TrpB2 both contribute to Trp biosynthesis
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
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
(3S)-2,3-dihydro-5-fluoro-L-tryptophan
?
show the reaction diagram
-
isomerization
-
-
?
1-(indol-3-yl)glycerol 3-phosphate
D-glyceraldehyde 3-phosphate + indole
show the reaction diagram
1-(indol-3-yl)glycerol 3-phosphate + L-serine
L-tryptophan + D-glyceraldehyde 3-phosphate
show the reaction diagram
1-(indol-3-yl)glycerol 3-phosphate + L-serine
L-tryptophan + D-glyceraldehyde 3-phosphate + H2O
show the reaction diagram
1-C-(indol-3-yl)glycerol 3-phosphate
D-glyceraldehyde 3-phosphate + indole
show the reaction diagram
2-amino-3-butenoic acid
2-oxobutyric acid + NH3
show the reaction diagram
2-mercaptoethanol + L-serine + pyridoxal phosphate
S-pyruvylmercaptoethanol + pyridoxamine phosphate + H2O
show the reaction diagram
5-fluoro-L-tryptophan
?
show the reaction diagram
-
isomerization
-
-
?
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
indole + L-serine
L-tryptophan + H2O
show the reaction diagram
indole-3-glycerol phosphate
indole + D-glyceraldehyde 3-phosphate
show the reaction diagram
indoleglycerol phosphate
indole + D-glyceraldehyde 3-phosphate
show the reaction diagram
Q9YGA9 and Q5JDJ1, Q9YGA9 and Q9YGB0
the reaction is catalyzed by the tryptophan synthase alpha-subunit TrpA
-
-
r
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-Ser + indole
L-tryptophan + H2O
show the reaction diagram
-
reaction catalyzed by the beta subunit
-
-
ir
L-serine
pyruvate + NH3
show the reaction diagram
L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate
L-tryptophan + D-glyceraldehyde 3-phosphate + H2O
show the reaction diagram
L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate
L-tryptophan + glyceraldehyde 3-phosphate + H2O
show the reaction diagram
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-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-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-chloroindole
7-chlorotryptophan + H2O
show the reaction diagram
-
-
-
-
?
L-serine + 7-fluoroindole
7-fluorotryptophan + H2O
show the reaction diagram
L-serine + 7-methylindole
7-methyltryptophan + H2O
show the reaction diagram
-
-
-
-
?
L-serine + indole
L-tryptophan
show the reaction diagram
-
-
-
-
-
L-serine + indole
L-tryptophan + H2O
show the reaction diagram
L-serine + indole
tryptophan + H2O
show the reaction diagram
L-serine + indoline
dihydro-iso-L-tryptophan + H2O
show the reaction diagram
-
-
i.e. DIT
?
L-serine + indoline
dihydroiso-L-tryptophan
show the reaction diagram
-
wild-type and mutant D305A enzymes
-
?
L-serine + indoline
dihydroiso-L-tryptophan + H2O
show the reaction diagram
-
-
i.e. DIT
?
L-serine + N-(4'-trifluoromethoxybenzenesulfonyl)-2-aminoethyl phosphate
?
show the reaction diagram
-
-
-
-
?
L-serine + N-(4'-trifluoromethoxybenzoyl)-2-aminoethyl phosphate
?
show the reaction diagram
-
-
-
-
?
L-serine + thiophenol
(S)-phenyl-L-cysteine + H2O
show the reaction diagram
-
-
-
-
?
L-tryptophan + D-glyceraldehyde 3-phosphate + H2O
indole-3-glycerol phosphate + L-serine
show the reaction diagram
-
r
r
-
serine + indole
tryptophan + H2O
show the reaction diagram
-
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
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
1-(indol-3-yl)glycerol 3-phosphate
D-glyceraldehyde 3-phosphate + indole
show the reaction diagram
1-(indol-3-yl)glycerol 3-phosphate + L-serine
L-tryptophan + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
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
-
-
-
-
?
indoleglycerol phosphate
indole + D-glyceraldehyde 3-phosphate
show the reaction diagram
Q9YGA9 and Q5JDJ1, Q9YGA9 and Q9YGB0
the reaction is catalyzed by the tryptophan synthase alpha-subunit TrpA
-
-
r
L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate
L-tryptophan + D-glyceraldehyde 3-phosphate + H2O
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 + indole
L-tryptophan + H2O
show the reaction diagram
L-serine + indole
tryptophan + H2O
show the reaction diagram
-
beta-subunit of the bienzyme complex, beta-reaction
-
?
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
additional information
-
the alpha-subunit contains no prosthetic group
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Cd2+
enzyme is up-regulated in plants treated with Cd2+. Overexpression in Arabidopsis and Solanum lycopersicum confers tolerance to cadmium stress
DL-glycerol 3-phosphate
-
enhances beta-reaction activity of mutant D305N and K167T
Li+
-
has an effect on the conformational equilibrium
Mg2+
-
highest activity with 0.18 M Mg2+
NaCl
-
ligand binding sites, effector on the action of activators or inhibitors, overview
Rb+
-
has an effect on the conformational equilibrium
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2,3-dihydro-L-tryptophan
-
very good competitive inhibitor
-
4-(2-aminophenylthio)butylphosphonic acid
4-(2-hydroxy-5-fluorophenylthio)butylphosphonic acid
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
5,5'-dithiobis(2-nitrobenzoate)
-
-
6-azido-L-tryptophan
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
DL-glycerol 3-phosphate
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
indole-3-acetylglycine
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
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
oxindolyl-L-alanine
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
-
-
-
trans-L-2-amino-4-methoxy-3-butenoic acid
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
COMMENTARY hide
LITERATURE
IMAGE
betaine
-
1 M betaine activates the enzyme 1.8fold in the absence of monovalent cations
Cs+
-
wild-type enzyme alpha-site is activated by the formation of the alpha-aminoacrylate Schiff base at the beta-site
guanidine hydrochloride
-
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
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
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
polyethylene glycol 8000
-
5% (w/v) activates the enzyme 2.1fold in the absence of monovalent cations
Sucrose
-
2 M sucrose activates the enzyme 3.3fold in the absence of monovalent cations
taurine
-
0.5 M taurine activates the enzyme 3fold in the absence of monovalent cations
Triton X-100
-
Trion X-100 leads to the emergence of the highest relative activity at 0.02% (v/v)
Tween-80
-
activates at 0.04%
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]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.01 - 1.62
1-(indol-3-yl)glycerol 3-phosphate
1.1
D-glyceraldehyde 3-phosphate
-
cosubstrate L-Trp, i.e. reverse reaction
0.000074 - 4.471
indole
0.6 - 5.7
L-Ser
0.0076 - 110
L-serine
0.02
serine
-
serine deaminase reaction
additional information
additional information
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00017 - 6
1-(indol-3-yl)glycerol 3-phosphate
0.007 - 70.29
indole
1.4
indoline
Salmonella enterica subsp. enterica serovar Typhimurium
-
overall-reaction, mutant D305A enzyme, pH 7.8, 25C, in presence of 100 mM Cs+
5.4
L-Ser
Salmonella enterica subsp. enterica serovar Typhimurium
-
cosubstrate indole
0.00017 - 48.21
L-serine
0.06
serine
Salmonella enterica subsp. enterica serovar Typhimurium
-
serine deaminase reaction
additional information
L-serine
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
17 - 99
indole
48 - 99
L-serine
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
12.8
glycerol 3-phosphate
-
pH 7.8, 20C
0.45
Indole-3-acetamide
-
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
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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+
85
-
indole + L-Ser
110
-
overall activity, purified enzyme complex
119
-
beta-reaction, purified enzyme complex
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+
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
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7
-
alpha-and beta-reaction
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
8.5
-
overall reaction
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
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
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 60
-
alpha-reaction assay at
30
-
assay at
70
-
alpha-reaction
85
Q9YGA9 and Q5JDJ1, Q9YGA9 and Q9YGB0
assay at; assay at
90
-
beta-reaction
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
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
COMMENTARY hide
LITERATURE
SOURCE
-
terminal, of young plants
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Aquifex aeolicus (strain VF5)
Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / 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)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
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)
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)