Tryptophan synthase

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== Function ==
== Function ==
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'''Tryptophan synthase''' (TrpS) is an α2β2 tetramer participating in the biosynthesis of tryptophan<ref>PMID:11893063</ref>. TrpS '''α subunit''' catalyzes the formation of indole and glyceraldehyde-3-phosphate (G3P) from indole-3-glycerol phosphate (IGP). The '''β subunit''' catalyzes in a pyridoxal-phosphate (PLP) dependent reaction the formation of tryptophan (Trp) from indole and serine. The diffusion of indole from the α to the β subunit is facilitated via a hydrophobic channel connecting the subunits.
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'''Tryptophan synthase''' (TrpS) is an α2β2 tetramer participating in the biosynthesis of tryptophan (Trp)<ref>PMID:11893063</ref>. TrpS '''α subunit''' catalyzes the formation of indole and glyceraldehyde-3-phosphate (G3P) from indole-3-glycerol phosphate (IGP). The '''β subunit''' catalyzes in a pyridoxal-phosphate (PLP) dependent reaction the formation of tryptophan (Trp) from indole and serine. The diffusion of indole from the α to the β subunit is facilitated via a hydrophobic channel connecting the subunits. '''Dimethylallyl tryptophan synthase''' (DMTS) calyces the alkylation of Trp by dimethylallyl phosphate to form 4-(γ,γ-dimethylallyl)-Trp<ref>PMID:1605639</ref>.
== Relevance ==
== Relevance ==

Revision as of 10:48, 29 January 2024

Tryptophan synthase α subunit (yellow, salmon) and β subunit (cyan, green) of the α2β2 tetramer complex with pyridoxal-phosphate, glycerol-3-phosphate and Na+ ion (purple) 1wbj

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References

  1. ↑ Miles EW. Tryptophan synthase: a multienzyme complex with an intramolecular tunnel. Chem Rec. 2001;1(2):140-51. PMID:11893063
  2. ↑ Gebler JC, Poulter CD. Purification and characterization of dimethylallyl tryptophan synthase from Claviceps purpurea. Arch Biochem Biophys. 1992 Jul;296(1):308-13. PMID:1605639 doi:10.1016/0003-9861(92)90577-j
  3. ↑ Shen H, Yang Y, Wang F, Zhang Y, Ye N, Xu S, Wang H. Characterization of the putative tryptophan synthase beta-subunit from Mycobacterium tuberculosis. Acta Biochim Biophys Sin (Shanghai). 2009 May;41(5):379-88. PMID:19430702
  4. ↑ Kulik V, Hartmann E, Weyand M, Frey M, Gierl A, Niks D, Dunn MF, Schlichting I. On the structural basis of the catalytic mechanism and the regulation of the alpha subunit of tryptophan synthase from Salmonella typhimurium and BX1 from maize, two evolutionarily related enzymes. J Mol Biol. 2005 Sep 23;352(3):608-20. PMID:16120446 doi:10.1016/j.jmb.2005.07.014

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Michal Harel, Alexander Berchansky, Joel L. Sussman, Amer Ali

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