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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

Reaction

1-C-(indol-3-yl)glycerol 3-phosphate
=
indole
 +
D-glyceraldehyde 3-phosphate

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 Lyases
         4.2 Carbon-oxygen lyases
             4.2.1 Hydro-lyases
                4.2.1.20 tryptophan synthase

Activating Compound

Activating Compound on EC 4.2.1.20 - tryptophan synthase

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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
-