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 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> | |||
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