4.2.1.20: tryptophan synthase
This is an abbreviated version!
For detailed information about tryptophan synthase, go to the full flat file.
Word Map on EC 4.2.1.20
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4.2.1.20
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pain
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pyridoxal
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typhimurium
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myofascial
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alpha-subunits
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beta-subunits
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5'-phosphate
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aldimine
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vanilloid
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indole-3-glycerol
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trapezius
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nociceptive
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nose
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cone-shaped
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melastatin
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palpation
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bienzyme
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epiphyses
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quinonoid
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craniofacial
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miles
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pear-shaped
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tension-type
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polycystin
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sternocleidomastoid
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beta-site
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tryptophanase
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l-trp
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urea-induced
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temporalis
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suboccipital
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metacarpal
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bulbous
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phalanx
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tryptophanyl-trna
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taut
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assessor
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scapula
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chaffeensis
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indoline
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ehrlichia
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levator
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5'-phosphate-dependent
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eyebrows
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masseter
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dimethylallyl
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trpcs
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capitis
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exostoses
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polymodal
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biotechnology
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synthesis
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analysis
- 4.2.1.20
- pain
- pyridoxal
- typhimurium
-
myofascial
- alpha-subunits
- beta-subunits
- 5'-phosphate
-
aldimine
-
vanilloid
-
indole-3-glycerol
-
trapezius
-
nociceptive
-
nose
-
cone-shaped
-
melastatin
-
palpation
-
bienzyme
-
epiphyses
-
quinonoid
-
craniofacial
- miles
-
pear-shaped
-
tension-type
-
polycystin
-
sternocleidomastoid
-
beta-site
- tryptophanase
- l-trp
-
urea-induced
-
temporalis
-
suboccipital
-
metacarpal
-
bulbous
-
phalanx
-
tryptophanyl-trna
-
taut
- assessor
-
scapula
- chaffeensis
- indoline
- ehrlichia
-
levator
-
5'-phosphate-dependent
-
eyebrows
-
masseter
-
dimethylallyl
-
trpcs
-
capitis
- exostoses
-
polymodal
- biotechnology
- synthesis
- analysis
Reaction
Synonyms
alpha2beta2 tryptophan synthase, alphaTS, AtTSB1, beta subunit of tryptophan synthase, indoleglycerol phosphate aldolase, It-TSA, L-serine hydro-lyase (adding indoleglycerol-phosphate), L-tryptophan synthetase, PtTSA, Rv1612, synthase, tryptophan, TrB, Trp synthase, Trp synthase beta, TrpA, trpB, TrpB1, TrpB2, TrpB2a, TrpB2i, TrpB2o, TRPS, tryptophan desmolase, tryptophan synthase, tryptophan synthase alpha subunit, tryptophan synthase alpha-subunit, tryptophan synthase alpha2beta2 complex, tryptophan synthase beta, tryptophan synthase beta 1, tryptophan synthase beta subunit, tryptophan synthetase, TS, TSA, TSase, TSB, TSB1, TSbeta
ECTree
4.2.1.20 tryptophan synthaseAdvanced search results
results (
results (Subunits
Subunits on EC 4.2.1.20 - tryptophan synthase
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SUBUNIT 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
dimer
heterotetramer
monomer
tetramer
additional information
?
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alpha subunit, x * 28800, calculation from amino acid sequence, x * 31000, SDS-PAGE
?
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2 * 39700-41000, beta subunit, 1 * 82000, beta2 subunit, ultracentrifugation, SDS-PAGE
?
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89000, B2 subunit, polyacrylamide gel electrophoresis, 2 * 43000, B subunit, SDS-PAGE
dimer
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2 * 77000, sedimentation equilibrium in 6 M guanidine hydrochloride
dimer
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TrpB2 does not bind to the alpha-subunit and forms homodimers, TrpB1 alone forms homodimers
heterotetramer
2 * 27700 (subunit TrpA) + 2 * 42600 (subunit TrpB1), calculated from sequence, tryptophan synthase is composed of subunit TrpA and subunit TrpB. Thermococcus kodakarensis possess two paralogs of subunit B, TrpB1 and TrpB2. TrpB2 catalyzes the TrpB reaction but does not interact with TrpA as in the case of TrpB1
heterotetramer
2 * 27700 (subunit TrpA) + 2 * 49300 (subunit TrpB2), calculated from sequence, tryptophan synthase is composed of subunit TrpA and subunit TrpB. Thermococcus kodakarensis possess two paralogs of subunit B, TrpB1 and TrpB2. TrpB2 catalyzes the TrpB reaction but does not interact with TrpA as in the case of TrpB1
heterotetramer
2 * 20800 + 2 * 67400, heterotetramer from subunits TrpA and TrpB1, SDS-PAGE
heterotetramer
2 * 27700 + 2 * 42600, heterotetramer from subunits TrpA and TrpB1, calculated from amino acid sequence
tetramer
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2 * 275000 + 2 * 42500, recombinant alpha2beta2 enzyme complex, SDS-PAGE
tetramer
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alpha2beta2 complex
tetramer
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alpha2beta2 complex, structural organization
tetramer
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alpha2beta2 complex, structure model
tetramer
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alpha2beta2 complex, structure-function relationship
tetramer
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alpha2beta2 enzyme complex
tetramer
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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
tetramer
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alphabetabetaalpha complex of TRpA and TrpB1, sedimentation equilibrium
additional information
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activities of alpha and beta subunits are coordinated by allosteric interactions
additional information
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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
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dimer formation seems to be associated with the formation of protein aggregates in vivo
additional information
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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
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structural analysis, wild-type and mutant beta-subunit dimers, hairpin loop in the beta-subunit, overview
additional information
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the alpha-subunit contains no disulfide bond, conformational stabilization mechanism
additional information
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the alpha-subunit is a TIM barrel protein, structure analysis
additional information
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high association constant for the hyperthermophile enzyme subunits, pH-dependence of the molecular weights
additional information
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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
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activities of alpha and beta subunits are coordinated by allosteric interactions
additional information
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sequence alignment of alpha-subunit
additional information
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conformational states, overview, subunit dissociation in presence of guanidinium hydrochloride
additional information
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crystal structure analysis, structure-function relationship, overview
additional information
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salt-bridges extending between the subunits involve alphaAsp56, betaLys167, beta-Asp305, and betaR141
additional information
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structural analysis, wild-type and mutant beta-subunit dimers, hairpin loop in the beta-subunit, overview
additional information
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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
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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
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structure models
additional information
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three-dimensional structure of the alphaloop6 in the closed conformation with hydrogen bond between Gly181 ans Ser178
additional information
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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
additional information
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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
