Reaction: L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate = L-tryptophan + glyceraldehyde 3-phosphate + H2O
For diagram click here and mechanism here.
Other name(s): L-tryptophan synthetase; indoleglycerol phosphate aldolase; tryptophan desmolase; tryptophan synthetase; L-serine hydro-lyase (adding indoleglycerol-phosphate)
Systematic name: L-serine hydro-lyase [adding 1-C-(indol-3-yl)glycerol 3-phosphate; L-tryptophan and glyceraldehyde-3-phosphate-forming]
Comments: A pyridoxal-phosphate protein. The α-subunit catalyses the conversion of 1-C-(indol-3-yl)glycerol 3-phosphate to indole and glyceraldehyde 3-phosphate. The indole then migrates to the β-subunit where, with serine in the presence of pyridoxal 5'-phosphate, it is converted to tryptophan. Also catalyses the conversion of serine and indole into tryptophan and water, and of 1-C-(indol-3-yl)glycerol 3-phosphate into indole and glyceraldehyde phosphate (the latter reaction was listed formerly as EC 4.1.2.8). In some organisms, this enzyme is part of a multifunctional protein, together with one or more other components of the system for the biosynthesis of tryptophan [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)].
Links to other databases: BRENDA, EXPASY, GTD, KEGG, PDB, CAS registry number: 9014-52-2
References:
1. Crawford, I.P. and Yanofsky, C. On the separation of the tryptophan synthetase of Escherichia coli into two protein components. Proc. Natl. Acad. Sci. USA 44 (1958) 1161-1170. [PMID: 16590328]
2. Creighton, T.E. and Yanofsky, C. Chorismate to tryptophan (Escherichia coli) - anthranilate synthetase, PR transferase, PRA isomerase, InGP synthetase, tryptophan synthetase. Methods Enzymol. 17A (1970) 365-380.
3. Hütter, R., Niederberger, P. and DeMoss, J.A. Tryptophan biosynthetic genes in eukaryotic microorganisms. Annu. Rev. Microbiol. 40 (1986) 55-77. [PMID: 16526091]
4. Hyde, C.C., Ahmed, S.A., Padlan, E.A., Miles, E.W. and Davies, D.R. Three-dimensional structure of the tryptophan synthase α2β2 multienzyme complex from Salmonella typhimurium. J. Biol. Chem. 263 (1988) 17857-17871. [PMID: 3053720]
5. Woehl, E. and Dunn, M.F. Mechanisms of monovalent cation action in enzyme catalysis: the tryptophan synthase α-, β-, and αβ-reactions. Biochemistry 38 (1999) 7131-7141. [PMID: 10353823]