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spinqualitylabelsall models PDB ID 2f6l Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image
2f6l, resolution 1.70Å ()
Gene:	Rv1885c (Mycobacterium tuberculosis)
Activity:	Chorismate mutase, with EC number 5.4.99.5
Structural annotation: Resources: InterPro : Ipr002701, Ipr008240 Pfam : PF01817 SCOP : d2f6la1, d2f6lb1 UniProt : O07746
Functional annotation: Biological process: aromatic amino acid family biosynthetic process Molecular function: chorismate mutase activity
Evolutionary conservation: Toggle Conservation Colors: Rows = identical sequences: Further Information: Caveats, Explanation, Complete Results at ConSurfDB
Resources:	FirstGlance, OCA, RCSB, PDBsum
Coordinates:	save as pdb, mmCIF, xml

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Contents 1 Chorismate Mutase 1.1 Introduction 1.2 Structure 1.3 Mechanism 1.4 Chorismate Mutase and Tuberculosis 1.5 References

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]. In Escherichia coli, chorismate mutase has a periplasmic destination^[1]. In M. tuberculosis there is in abscence of a periplasmic compartment for chorismate mutase, so it secretes into the periplasmic compartment of M. tuberculosis^[1]

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 ^[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. ↑ ^{1.0 1.1 1.2 1.3 1.4 1.5 1.6} 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. ↑ ^{2.0 2.1 2.2} Kast P, Grisostomi C, Chen IA, Li S, Krengel U, Xue Y, Hilvert D. A strategically positioned cation is crucial for efficient catalysis by chorismate mutase. J Biol Chem. 2000 Nov 24;275(47):36832-8. PMID:10960481 doi:10.1074/jbc.M006351200
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
4. ↑ 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