Sandbox Reserved 325: Difference between revisions
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in Michaelis-Menten kinetics chorismate mutase has Km of 0.5 ± 0.05 mM and Kcat of 60 s<sup>-1 </sup>.<ref name="pizza" /> | in Michaelis-Menten kinetics chorismate mutase has Km of 0.5 ± 0.05 mM and Kcat of 60 s<sup>-1 </sup>.<ref name="pizza" /> | ||
Chorismate mutase is an essential enzyme in the shikimate pathway.<ref name="pizza"> PMID:17146044 </ref> This pathway allows for the biosynthesis of aromatic amino acids tryptophan, tyrosine, and phenylalanine.<ref name="pizza" /> The production of tyrosine and phenylalanine is achieved by what is called a Claisen rearrangement.<ref name="pizza" / > First by converting chorismate to prephenate.<ref name="pizza" /> Prephenate then reacts with prephenate dehydratase and prephenate dehydrogenase which forms phenylpyruvate and hydroxyphenylpyruvate.<ref name="pizza" / > After this occurs, aminotransferase converts hydroxy-phenylpyruvate and phenylpyruvate to phenylalanine and tyrosine.<ref name="pizza" /> Chorismate mutase provides a 2x10<sup>6</sup> fold increase in the rate of reaction, in comparison to the uncatalyzed reaction.<ref > P.D. Lyne, A.J. Mulholland, W.G. Richards. Insights into chorismate mutase catalysis from a combined qm/mm simulation of the enzyme reaction. Journal of the American Chemistry Society. 1995 117(45):11345-11350</ref> It is the only example of an enzyme catalyzing a percyclic reaction.<ref name="strat"> PMID:10960481 </ref> | Chorismate mutase is an essential enzyme in the shikimate pathway.<ref name="pizza"> PMID:17146044 </ref> This pathway allows for the biosynthesis of aromatic amino acids tryptophan, tyrosine, and phenylalanine.<ref name="pizza" /> The production of tyrosine and phenylalanine is achieved by what is called a Claisen rearrangement.<ref name="pizza" /> First by converting chorismate to prephenate.<ref name="pizza" /> Prephenate then reacts with prephenate dehydratase and prephenate dehydrogenase which forms phenylpyruvate and hydroxyphenylpyruvate.<ref name="pizza" / > After this occurs, aminotransferase converts hydroxy-phenylpyruvate and phenylpyruvate to phenylalanine and tyrosine.<ref name="pizza" /> Chorismate mutase provides a 2x10<sup>6</sup> fold increase in the rate of reaction, in comparison to the uncatalyzed reaction.<ref > P.D. Lyne, A.J. Mulholland, W.G. Richards. Insights into chorismate mutase catalysis from a combined qm/mm simulation of the enzyme reaction. Journal of the American Chemistry Society. 1995 117(45):11345-11350< /ref> It is the only example of an enzyme catalyzing a percyclic reaction.<ref name="strat"> PMID:10960481 < /ref> | ||
Chorismate mutase has optimal performance at 37 degrees Celcius and at pH 7.5, but it can still optimally a pH range from pH 4.0 to 7.5 <ref name="pizza" /> | Chorismate mutase has optimal performance at 37 degrees Celcius and at pH 7.5, but it can still optimally a pH range from pH 4.0 to 7.5 <ref name="pizza" /> | ||
