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• W2063292893 abstract "The tryptophan synthase α2β2 bi-enzyme complex catalyzes the last two steps in the synthesis of l-tryptophan (l-Trp). The α-subunit catalyzes cleavage of 3-indole-d-glycerol 3'-phosphate (IGP) to give indole and d-glyceraldehyde 3'-phosphate (G3P). Indole is then transferred (channeled) via an interconnecting 25Å-long tunnel, from the α-subunit to the β-subunit where it reacts with l-Ser in a pyridoxal 5'-phosphate-dependent reaction to give l-Trp and a water molecule. The efficient utilization of IGP and l-Ser by tryptophan synthase to synthesize l-Trp utilizes a system of allosteric interactions that (1) function to switch the α-site on and off at different stages of the β-subunit catalytic cycle, and (2) prevent the escape of the channeled intermediate, indole, from the confines of the α- and β-catalytic sites and the interconnecting tunnel. This review discusses in detail the chemical origins of the allosteric interactions responsible both for switching the α-site on and off, and for triggering the conformational changes between open and closed states which prevent the escape of indole from the bienzyme complex." @default.
• W2063292893 created "2016-06-24" @default.
• W2063292893 creator A5085832228 @default.
• W2063292893 date "2012-03-01" @default.
• W2063292893 modified "2023-10-17" @default.
• W2063292893 title "Allosteric regulation of substrate channeling and catalysis in the tryptophan synthase bienzyme complex" @default.
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• W2063292893 doi "https://doi.org/10.1016/j.abb.2012.01.016" @default.
• W2063292893 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3702454" @default.
• W2063292893 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/22310642" @default.
• W2063292893 hasPublicationYear "2012" @default.
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