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
-
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
-
synthesis
-
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
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RENATURED/Commentary 
ORGANISM
UNIPROT
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 25°C
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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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effect of ficoll-70 on the alpha subunit of tryptophan synthase. Crowding by ficoll perturbs the native state and the partially folded state of the subunit. Ficoll interacts with the residues that constitute the stable core of the protein
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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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