Chorismate mutase

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^[1]. CHM is divided ןמto 2 classes: AroH class which is monofunctional and thק bifunctional AroQ.

Relevance

CHM 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^[2].

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^[3]. 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.

Chorismate mutase 3D structures

3D structures of chorismate mutase