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
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results (General Information
General Information on EC 4.2.1.20 - tryptophan synthase
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GENERAL INFORMATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
evolution
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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
metabolism
physiological function
additional information
malfunction
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
malfunction
double-deletion mutant (DELTAtrpB1DELTAtrpB2) displays Trp auxotrophy, whereas individual single mutants (DELTAtrpB1 and DELTAtrpB2 strains) do not. To examine the capacity of TrpB1 and TrpB2 in Trp synthesis via indole salvage, DtrpEB1 and DtrpEB2 mutant strains are constructed using strain KUW1 (DELTApyrFDtrpE) as a host, eliminating the route for endogenous indole synthesis. Indole complements the Trp auxotrophies of DELTAtrpEB1 (DELTApyrFDELTAtrpEDELTAtrpB1) and DELTAtrpEB2 (DELTApyrFDELTAtrpEDELTAtrpB2) to similar levels. The results indicate that TrpB1 and TrpB2 both contribute to Trp biosynthesis in Thermococcus kodakarensis and can utilize free indole, and that indole salvage does not necessarily rely on TrpB2 to a greater extent
metabolism
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
metabolism
the enzyme is involved in L-tryptophan biosynthesis
physiological function
Vitis vinifera x Vitis vinifera
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involved in aromatic amino acid metabolism
physiological function
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involved in aromatic amino acid metabolism
physiological function
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structure analysis indicate that Mycobacterium tuberculosis TrpB exhibits a typical beta/alpha barrel structure
physiological function
AtTSBtype2 function is not essential under standard growth conditions
physiological function
as part of its native alphabetabetaalpha complex, subunit TrpB efficiently produces tryptophan and tryptophan analogs. Activity drops considerably when it is used as a stand-alone catalyst without the alpha-subunit. This lost activity can be recovered by mutations that reproduce the effects of complexation with the alpha-subunit
physiological function
residue Lys87 of the beta subunit plays multiple catalytic roles, it bonds to the pyridoxal phosphate cofactor, activates C4' for nucleophilic attack via a protonated Schiff base nitrogen, and abstracts and returns protons to pyridoxal phosphate-bound substrates. The protonation state of the epsilon-amino group switches between protonated and neutral states as the beta-subunit undergoes conversion from one intermediate to the next during catalysis
physiological function
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residue Lys87 of the beta subunit plays multiple catalytic roles, it bonds to the pyridoxal phosphate cofactor, activates C4' for nucleophilic attack via a protonated Schiff base nitrogen, and abstracts and returns protons to pyridoxal phosphate-bound substrates. The protonation state of the epsilon-amino group switches between protonated and neutral states as the beta-subunit undergoes conversion from one intermediate to the next during catalysis
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physiological function
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AtTSBtype2 function is not essential under standard growth conditions
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additional information
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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
additional information
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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
