Sandbox Reserved 325: Difference between revisions
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Chorismate has an active site, which is used for the catalysis of the shikimate pathway.<ref name="pizza" /> The <scene name='Sandbox_Reserved_325/Active_site/1'>active site</scene> is made of Arg <sub>49</sub>,Lys <sub>60</sub>, Arg <sub>72</sub>, Thr <sub>105</sub>, Glu <sub>109</sub>, and Arg <sub>134</sub>.<ref name="pizza" /> This active site exists through electrostatic interactions with chorismate and hydrogen bonding between the amino acids <ref name="CMArt2" />. The active site forms within a single chain.<ref name="pizza" /> The active site can form without any help from the second half of the dimer.<ref name="pizza" /> | Chorismate has an active site, which is used for the catalysis of the shikimate pathway.<ref name="pizza" /> The <scene name='Sandbox_Reserved_325/Active_site/1'>active site</scene> is made of Arg <sub>49</sub>,Lys <sub>60</sub>, Arg <sub>72</sub>, Thr <sub>105</sub>, Glu <sub>109</sub>, and Arg <sub>134</sub>.<ref name="pizza" /> This active site exists through electrostatic interactions with chorismate and hydrogen bonding between the amino acids <ref name="CMArt2" />. The active site forms within a single chain.<ref name="pizza" /> The active site can form without any help from the second half of the dimer.<ref name="pizza" /> | ||
The molecular weight of chorismate mutase is 36,000 Da.<ref name="pizza" /> Based on | The molecular weight of chorismate mutase is 36,000 Da.<ref name="pizza" /> Based on that each monomeric subunit has a molecular weight of 18,474 Da, the molecular weight of the molecule supports the theory that it is a dimer.<ref name="pizza" /> This is also supported by that all chorismate mutases that occur naturally are either trimers or dimers.<ref name="pizza" /> ''M. tuberculosis'' chorismate mutase is similar to the chorismate mutases of yeast and ''E. coli'' in the regards that they all are homodimers.<ref name="CMArt2" /> | ||
There are no allosteric regulatory sites on chorismate mutase, which supports the theory that it is not regulated by the aromatic amino acids that are the products of the shikimate pathway.<ref name="pizza" /> | There are no allosteric regulatory sites on chorismate mutase, which supports the theory that it is not regulated by the aromatic amino acids that are the products of the shikimate pathway.<ref name="pizza" /> | ||
