Chorismate mutase
From Proteopedia
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== Function == | == Function == | ||
| - | '''Chorismate mutase''' (CHM) is a key enzyme in the biosynthesis of aromatic amino acids Phe and Tyr. CHM catalyzes the rearrangement of chorismate to prephenate which is the precursor of Phe and Tyr<ref>PMID:21638687</ref>. CHM is divided | + | '''Chorismate mutase''' (CHM) is a key enzyme in the biosynthesis of aromatic amino acids Phe and Tyr. CHM catalyzes the rearrangement of chorismate to prephenate which is the precursor of Phe and Tyr<ref>PMID:21638687</ref>. CHM is divided into 2 classes: '''AroH''' class which is monofunctional and the bifunctional '''AroQ'''. |
| + | *'''Bifunctional chorismate mutase/hexadienyl dehydratase''' catalyze 2 subsequent reactions in the biosynthesis of Phe<ref>PMID:37586588</ref>. | ||
== Relevance == | == Relevance == | ||
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== Structural highlights == | == Structural highlights == | ||
| - | The 3D structure of the complex of CHM with transition state analog shows the CHM structure containing a dimer of pseudosymmetry but only the N-terminal half contains an available active site pocket. The transition state analog is buried in the active site pocket and forms extensive H-bond network with CHM. Arg 49 and Arg 134 which are part of this network are conserved in all the known CHMs<ref>PMID:16499927</ref>. | + | The 3D structure of the complex of CHM with transition state analog shows the CHM structure containing a dimer of pseudosymmetry but only the N-terminal half contains an available active site pocket. The <scene name='91/916399/Cv/4'>transition state analog is buried in the active site pocket and forms extensive H-bond network</scene> with CHM. Water molecule is shown as red sphere. <scene name='91/916399/Cv/5'>Arg 49 and Arg 134</scene> (in magenra) which are part of this network are conserved in all the known CHMs<ref>PMID:16499927</ref>. Overlaying the structure of the unliganded CHM with that of the complex shoes a movement of the <scene name='91/916399/Cv/6'>second shell residues Arg 72 and Gln 75</scene> (in lavender) which can allow the entry of the transition state analog to the active site pocket. |
==Chorismate mutase 3D structures== | ==Chorismate mutase 3D structures== | ||
Current revision
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References
- ↑ Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644
- ↑ Stocker C, Khatanbaatar T, Bressan L, Würth-Roderer K, Cordara G, Krengel U, Kast P. Novel exported fusion enzymes with chorismate mutase and cyclohexadienyl dehydratase activity: shikimate pathway enzymes teamed up in no man's land. J Biol Chem. 2023 Aug 14:105161. PMID:37586588 doi:10.1016/j.jbc.2023.105161
- ↑ Asojo OA, Dranow DM, Serbzhinskiy D, Subramanian S, Staker B, Edwards TE, Myler PJ. Crystal structure of chorismate mutase from Burkholderia thailandensis. Acta Crystallogr F Struct Biol Commun. 2018 May 1;74(Pt 5):294-299. doi:, 10.1107/S2053230X1800506X. Epub 2018 Apr 16. PMID:29717997 doi:http://dx.doi.org/10.1107/S2053230X1800506X
- ↑ Okvist M, Dey R, Sasso S, Grahn E, Kast P, Krengel U. 1.6 A crystal structure of the secreted chorismate mutase from Mycobacterium tuberculosis: novel fold topology revealed. J Mol Biol. 2006 Apr 14;357(5):1483-99. Epub 2006 Feb 6. PMID:16499927 doi:http://dx.doi.org/10.1016/j.jmb.2006.01.069
