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/> | ||
Revision as of 10:26, 6 July 2022
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 ןמto 2 classes: AroH class which is monofunctional and thק bifunctional AroQ. DiseaseRelevanceStructural 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. Arg 49 and Arg 134 which are part of this network are conserved in all the known CHMs[2].
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ReferencesReferences
- ↑ Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644
- ↑ Okvist M, Dey R, Sasso S, Grahn E, Kast P, Krengel U. 1.6 A crystal structure of the secreted chorismate mutase from Mycobacterium tuberculosis: novel fold topology revealed. J Mol Biol. 2006 Apr 14;357(5):1483-99. Epub 2006 Feb 6. PMID:16499927 doi:http://dx.doi.org/10.1016/j.jmb.2006.01.069