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 ןמto 2 classes: AroH class which is monofunctional and thק bifunctional AroQ.
'''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>. Overlaying the structure of the unliganded CHM with that of the complex shos a movement of the second shell residues Arg 72 and Gln 75 which can allow the entry of the transition state analog to the active site pocket. <scene name='91/916399/Cv/2'>TextToBeDisplayed</scene>
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==

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky