Chorismate mutase: Difference between revisions
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<StructureSection load=' | <StructureSection load='2fp2' size='340' side='right' caption='Bacillus subtilis chorismate mutase complex with transition state analog (PDB code [[2fp2]]).' scene=''> | ||
== 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 ןמto 2 classes: AroH class which is monofunctional and thק bifunctional AroQ. | ||
== Disease == | == Disease == | ||
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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>. | |||
</StructureSection> | </StructureSection> | ||
== References == | == References == | ||
<references/> | <references/> |