Sandbox Reserved 325: Difference between revisions
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There is one <scene name='Sandbox_Reserved_325/Disulfide/1'>disulfide bridge</scene> in chorismate mutase <ref name="pizza" />. It is between Cys <sub>160</sub> and Cys <sub>193</sub> <ref name="pizza" />. | There is one <scene name='Sandbox_Reserved_325/Disulfide/1'>disulfide bridge</scene> in chorismate mutase <ref name="pizza" />. It is between Cys <sub>160</sub> and Cys <sub>193</sub> <ref name="pizza" />. | ||
Chorismate mutase has a 33-amino-acid cleavable sequence <ref name="pizza" />. The N-terminal sequence of ''M. tuberculosis'' chorismate mutase is able to function in ''E. coli'' which suggests that ''M. tuberulosis'' chorismate mutase belongs to the AroQ class of the chorismate mutases<ref name="CMArt2" />. Another factor that suggests that ''M. tuberculosis'' chorismate mutase belongs to the AroQ class of chorismate mutases is that it has has a predominantly α-helical structure, which is similar to the chorismate mutases of ''E. coli'' and yeast, which also belong to the AroQ group of chorismate mutases <ref name="CMArt2" />. | Chorismate mutase has a 33-amino-acid cleavable sequence <ref name="pizza" />. The N-terminal sequence of ''M. tuberculosis'' chorismate mutase is able to function in ''E. coli'' which suggests that ''M. tuberulosis'' chorismate mutase belongs to the AroQ class of the chorismate mutases<ref name="CMArt2" />. Another factor that suggests that ''M. tuberculosis'' chorismate mutase belongs to the AroQ class of chorismate mutases is that it has has a predominantly α-helical structure, which is similar to the chorismate mutases of ''E. coli'' and yeast, which also belong to the AroQ group of chorismate mutases <ref name="CMArt2" />. | ||
