Sandbox Reserved 769: Difference between revisions
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Tryptophan synthase typically exists as an α-ββ-α complex. The α subunit has an α/β barrel, which is formed from eight parallel beta strands with eight parallel α-helicies packed around it.The β-subunit consists of two domains called the N-terminal domain and C-terminal domain.<ref name="cite7">http://tryptophan.net/Trpsynthase/Tryptophan%20Synthase.html</ref> | Tryptophan synthase typically exists as an α-ββ-α complex. The α subunit has an α/β barrel, which is formed from eight parallel beta strands with eight parallel α-helicies packed around it.The β-subunit consists of two domains called the N-terminal domain and C-terminal domain.<ref name="cite7">http://tryptophan.net/Trpsynthase/Tryptophan%20Synthase.html</ref> | ||
===Hydrophobic | ===Hydrophobic Channel=== | ||
The α and β active sites are separated by a 30 Å long hydrophobic channel contained within the enzyme allowing for the diffusion of indole. If the channel did not exist, the indole formed at an α active site would quickly diffuse away and be lost to the cell as it is hydrophobic and can easily cross membranes. As such, the channel is essential for enzyme complex function<ref name="cite6">http://www.annualreviews.org/doi/abs/10.1146/annurev.biochem.70.1.149</ref> | The α and β active sites are separated by a 30 Å long hydrophobic channel contained within the enzyme allowing for the diffusion of indole. If the channel did not exist, the indole formed at an α active site would quickly diffuse away and be lost to the cell as it is hydrophobic and can easily cross membranes. As such, the channel is essential for enzyme complex function<ref name="cite6">http://www.annualreviews.org/doi/abs/10.1146/annurev.biochem.70.1.149</ref> | ||
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===Active Sites=== | ===Active Sites=== | ||
[[Image:Active Site 2.gif]] | [[Image:Active Site 2.gif]] | ||
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β subunit reaction: The βLys87, βGlu109, and βSer377 are thought to be directly involved in the catalysis as shown.<ref name="cite7">http://tryptophan.net/Trpsynthase/Tryptophan%20Synthase.html</ref> | β subunit reaction: The βLys87, βGlu109, and βSer377 are thought to be directly involved in the catalysis as shown.<ref name="cite7">http://tryptophan.net/Trpsynthase/Tryptophan%20Synthase.html</ref> | ||
==Medical Relevance== | |||
As humans do not have tryptophan synthase, this enzyme has been explored as a potential drug target. | |||
Inhibition of tryptophan synthase in amino acid metabolism has been suggested for:<ref name="info">http://en.wikipedia.org/wiki/Tryptophan_synthase</ref> | |||
• Treatment of tuberculosis | |||
• Treatment of ocular and genital infections | |||
• Treatment of cryptosporidiosis | |||
• Herbicide use | |||
==References== | ==References== | ||
<references /> | <references /> | ||
