Chorismate mutase: Difference between revisions
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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== | ||
Latest revision as of 12:09, 28 January 2025
FunctionChorismate 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[1]. CHM is divided into 2 classes: AroH class which is monofunctional and the bifunctional AroQ.
RelevanceCHM belongs to the aromatic acids biogenesis pathway in prokaryotes which differs from that of humans. Hence, the presence of CHM indicates the presence of virulent bacteria and its detection is used in developing rational therapeutics against bacterial virulence[3]. Structural highlightsThe 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 with CHM. Water molecule is shown as red sphere. (in magenra) which are part of this network are conserved in all the known CHMs[4]. Overlaying the structure of the unliganded CHM with that of the complex shoes a movement of the (in lavender) which can allow the entry of the transition state analog to the active site pocket. Chorismate mutase 3D structures3D structures of chorismate mutase
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ReferencesReferences
- ↑ 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