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 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[2].
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[3].
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 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 structures
3D structures of chorismate mutase
