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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

Systematic Name

Systematic Name on EC 4.2.1.20 - tryptophan synthase

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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.