Chorismate mutase
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 transition state analog is buried in the active site pocket and forms extensive H-bond network with CHM. Water molecule is shown as red sphere. Arg 49 and Arg 134 (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 second shell residues Arg 72 and Gln 75 (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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