Category:Complex:tryptophan synthase: Difference between revisions
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Revision as of 06:30, 29 July 2007
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Description (originally from EcoCyc[1][2]) tryptophan synthase
Comments (originally from EcoCyc[1][2]) The overall tryptophan synthase reaction consists of a sequence of two partial reactions. The α subunit of the complex carries out the aldol cleavage of indole-3-glycerol phosphate to indole + glyceraldehyde-3-phosphate. The β subunit is responsible for the synthesis of L-tryptophan from indole + L-serine. The α2-β2 complex, which alone catalyzes the overall reaction, proceeds at two independent α/β sites via catalysis of the α reaction on the α subunit component, channeling the product (indole) to the pyridoxal phosphate site on the β component, where, in the presence of L-serine, it is converted to tryptophan. Indole does not appear in solution and is not a free intermediate. There is apparent subunit communication mediated by transduced conformational changes between the subunits, whereby the rates of the α and β reactions are strongly enhanced by, respectively, the β and α subunits [3].
References
- ↑ 1.0 1.1 EcoCyc (release 10.6; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
- ↑ 2.0 2.1 EcoCyc (release 11.1; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
- ↑ Lim, WK et al. (1991) Relative activities and stabilities of mutant Escherichia coli tryptophan synthase alpha subunits. J Bacteriol 173 1886-93 PubMed
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