Sandbox Reserved 325
From Proteopedia
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=Chorismate Mutase= | =Chorismate Mutase= | ||
==Introduction== | ==Introduction== | ||
| - | The gene Rv1885c from ''Mycobacteriam tuberculosis'' encodes for a non-functional chorismate mutase (*MtCM)<ref name="pizza" /> | + | The gene Rv1885c from ''Mycobacteriam tuberculosis'' encodes for a non-functional chorismate mutase (*MtCM)<ref name="pizza" />. This non-functional mutase has a 33-amino-acid cleavable sequence. Chorismate mutase only occurs in bacteria, higher plants, and fungi, due to the fact that the shikimate pathway is only found in these organisms <ref name="strat">. |
Revision as of 01:03, 2 April 2011
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| 2f6l, resolution 1.70Å () | |||||||||
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| Gene: | Rv1885c (Mycobacterium tuberculosis) | ||||||||
| Activity: | Chorismate mutase, with EC number 5.4.99.5 | ||||||||
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| Resources: | FirstGlance, OCA, RCSB, PDBsum | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
| This Sandbox is Reserved from January 10, 2010, through April 10, 2011 for use in BCMB 307-Proteins course taught by Andrea Gorrell at the University of Northern British Columbia, Prince George, BC, Canada. |
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Contents |
Chorismate Mutase
Introduction
The gene Rv1885c from Mycobacteriam tuberculosis encodes for a non-functional chorismate mutase (*MtCM)[1]. This non-functional mutase has a 33-amino-acid cleavable sequence. Chorismate mutase only occurs in bacteria, higher plants, and fungi, due to the fact that the shikimate pathway is only found in these organisms [2]. This pathway allows for the biosynthesis of aromatic amino acids tryptophan, tyrosine, and phenylalanine [1]. The production of tyrosine and phenylalanine is achieved by what is called a Claisen arrangement. first converting chorismate to prephenate. Prephenate then reacts with prephenate dehydratase and prephenate dehydrogenase which forms phenylpyruvate and hydroxyphenylpyruvate. After this occursm aminotransferase converts hydroxy-phenylpyruvate and phenylpyruvate to phenylalanine and tyrosine. Chorismate mutase provides a 2x106 fold increase in the rate of reaction, in comparison to the uncatalyzed reaction [3]. It is the only example of an enzyme catalyzing a percyclic reaction [2]
Structure
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Mechanism
Chorismate mutase is an essential enzyme in the shikimate pathway [1]. This pathway allows for the biosynthesis of aromatic amino acids tryptophan, tyrosine, and phenylalanine [1]. The production of tyrosine and phenylalanine is achieved by what is called a Claisen arrangement. first converting chorismate to prephenate. Prephenate then reacts with prephenate dehydratase and prephenate dehydrogenase which forms phenylpyruvate and hydroxyphenylpyruvate. After this occursm aminotransferase converts hydroxy-phenylpyruvate and phenylpyruvate to phenylalanine and tyrosine. Chorismate mutase provides a 2x106 fold increase in the rate of reaction, in comparison to the uncatalyzed reaction [4]. It is the only example of an enzyme catalyzing a percyclic reaction [2]
Chorismate Mutase and Tuberculosis
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References
- ↑ 1.0 1.1 1.2 1.3 Kim SK, Reddy SK, Nelson BC, Vasquez GB, Davis A, Howard AJ, Patterson S, Gilliland GL, Ladner JE, Reddy PT. Biochemical and structural characterization of the secreted chorismate mutase (Rv1885c) from Mycobacterium tuberculosis H37Rv: an *AroQ enzyme not regulated by the aromatic amino acids. J Bacteriol. 2006 Dec;188(24):8638-48. PMID:17146044 doi:188/24/8638
- ↑ 2.0 2.1 2.2 . Chorismate mutase is an essential enzyme in the shikimate pathway <ref> PMID:17146044 </li> <li id="cite_note-2">[[#cite_ref-2|↑]] 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</li> <li id="cite_note-3">[[#cite_ref-3|↑]] 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</li></ol></ref>
