Editing Tryptophan synthase (section)

==Disease relevance==
As humans do not have tryptophan synthase, this enzyme has been explored as a potential [[drug target]].<ref name="Drug Target">{{cite journal |vauthors=Chaudhary K, Roos DS | title = Protozoan genomics for drug discovery | journal = Nat Biotechnol | volume = 23 | issue = 9 | pages = 1089–91 |date=September 2005 | pmid = 16151400 | doi = 10.1038/nbt0905-1089| pmc = 7096809 }}</ref> However, it is thought that bacteria have alternate mechanisms to produce amino acids which might make this approach less effective. In either case, even if the drug only weakens bacteria, it might still be useful as the bacteria are already vulnerable in the hostile host environment. As such, the inhibition of tryptophan synthase along with other PLP-enzymes in amino acid metabolism has the potential to help solve medical problems.<ref name="Weakness">{{cite journal |vauthors=Becker D, Selbach M, Rollenhagen C, Ballmaier M, Meyer TF, Mann M, Bumann D | title = Robust Salmonella metabolism limits possibilities for new antimicrobials | journal = Nature | volume = 440 | issue = 7082 | pages = 303–7 |date=March 2006 | pmid = 16541065 | doi = 10.1038/nature04616| s2cid = 4426157 }}</ref>

Inhibition of tryptophan synthase and other PLP-enzymes in amino acid metabolism has been suggested for:
* Treatment of [[tuberculosis]]<ref name="Drug Target" />
* Treatment of [[Human eye|ocular]] and [[genital]] infections<ref name="Infections">{{cite journal |vauthors=Caldwell HD, Wood H, Crane D, Baily R | title = Polymorphisms in Chlamydia trachomatis tryptophan synthase genes differentiate between genital and ocular isolates | journal = J Clin Invest | volume = 111 | issue = 11 | pages = 1757–69 |date=June 2003 | pmid = 12782678 | doi = 10.1172/JCI17993| pmc = 156111 }}</ref>
* Treatment of [[cryptosporidiosis]]<ref name="Drug Target"/>
* [[Herbicide]] use<ref name="Herbicide">{{cite journal |vauthors=Kulik V, Hartmann E, Weyand M, Frey M, Gierl A, Niks D, Dunn MF, Schlichting I | title = On the structural basis of the catalytic mechanism and the regulation of the α-subunit of tryptophan synthase from Salmonella typhimurium and BXI from maize, two evolutionarily related enzymes | journal = J Mol Biol | volume = 352 | issue = 3 | pages = 608–20 |date=September 2005 | pmid = 16120446 | doi = 10.1016/j.jmb.2005.07.014}}</ref>