PROSITE documentation PDOC00152Tryptophan synthase beta chain pyridoxal-phosphate attachment site
Tryptophan synthase (EC 4.2.1.20) catalyzes the last step in the biosynthesis of tryptophan: the conversion of indoleglycerol phosphate and serine, to tryptophan and glyceraldehyde 3-phosphate [1,2]. It has two functional domains: one for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate and the other for the synthesis of tryptophan from indole and serine. In bacteria and plants [3], each domain is found on a separate subunit (α and β chains), while in fungi the two domains are fused together on a single multifunctional protein.
The β chain of the enzyme requires pyridoxal-phosphate as a cofactor. The pyridoxal-phosphate group is attached to a lysine residue. The region around this lysine residue also contains two histidine residues which are part of the pyridoxal-phosphate binding site. The signature pattern for the tryptophan synthase β chain is derived from that conserved region.
Last update:December 2004 / Pattern and text revised.
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PROSITE method (with tools and information) covered by this documentation:
| 1 | Authors | Crawford I.P. |
| Title | Evolution of a biosynthetic pathway: the tryptophan paradigm. | |
| Source | Annu. Rev. Microbiol. 43:567-600(1989). | |
| PubMed ID | 2679363 | |
| DOI | 10.1146/annurev.mi.43.100189.003031 |
| 2 | Authors | Hyde C.C. Miles E.W. |
| Title | The tryptophan synthase multienzyme complex: exploring structure-function relationships with X-ray crystallography and mutagenesis. | |
| Source | Biotechnology (N.Y.) 8:27-32(1990). | |
| PubMed ID | 1366510 |
| 3 | Authors | Berlyn M.B. Last R.L. Fink G.R. |
| Title | A gene encoding the tryptophan synthase beta subunit of Arabidopsis thaliana. | |
| Source | Proc. Natl. Acad. Sci. U.S.A. 86:4604-4608(1989). | |
| PubMed ID | 2734310 |
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