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 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
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
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)
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
-
denaturation of recombinant wild-type and mutant alpha-subunit monomers and dimers with urea, refolding of all forms as monomers
-
insoluble rcombinant alpha-subunit, expressed in strain BL212(DE3), is denatured by 6 M urea, refolding
-
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
-
unfolding and refolding of wild-type and mutant alpha-subunits using urea, comparison of the folding process differences, thermodynamic parameters
-
urea-induced equilibrium unfolding reaction
-
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
synthesis
-
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
-
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
-
analysis
-
the enzyme complex is a model enzyme for understanding allosteric regulation
biotechnology
-
enzyme is a target for structure-based design of herbicides