Isochorismate pyruvate lyase: Difference between revisions
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==Isochorismate== | ==Isochorismate== | ||
Isochorismate is the end product of the shikimate pathway that is essential for the synthesis of many primary and secondary metabolites. It is synthesized from chorismate by '''isochorismate synthase''' enzyme. Chorismate is the common precursor for synthesis of aromatic amino acids, cofactors, phenazines and siderophores. | Isochorismate is the end product of the shikimate pathway that is essential for the synthesis of many primary and secondary metabolites. It is synthesized from chorismate by '''isochorismate synthase''' enzyme. Chorismate is the common precursor for synthesis of aromatic amino acids, cofactors, phenazines and siderophores. | ||
Many enzymes are involved in the pathway and these enzymes are present in microbes and plants and absent in mammals and provide potential targets for antimicrobial drugs and herbicides.Isochorismate pyruvate Lyase (IPL) is one such enzyme. | Many enzymes are involved in the pathway and these enzymes are present in microbes and plants and absent in mammals and provide potential targets for antimicrobial drugs and herbicides.Isochorismate pyruvate Lyase (IPL) is one such enzyme<ref>PMID:16248620</ref>. | ||
==Function== | ==Function== | ||
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==Significance== | ==Significance== | ||
This enzyme unlike others does not catalyze forming covalent enzyme-substrate intermediate or acid-base catalysis. Claisens rearrangement takes place, instead. The substrate is stabilized in an energitically unfavorable pseudoaxial conformation forcing the vanderwaals contact, producing steric strain on the substrate and provides electrostatic stabilization of the transition state. Lys 42 and Gln 90 are positioned to stabilize the developing negative charge of the polar transition product in the chorismate mutase reaction and the pyruvate byproduct in the IPL reaction. therefore the ordering of the active site loop shows induced fit of the enzyme upon substrate binding locks Lys 42 into place for catalysis. | This enzyme unlike others does not catalyze forming covalent enzyme-substrate intermediate or acid-base catalysis. Claisens rearrangement takes place, instead. The substrate is stabilized in an energitically unfavorable pseudoaxial conformation forcing the vanderwaals contact, producing steric strain on the substrate and provides electrostatic stabilization of the transition state. Lys 42 and Gln 90 are positioned to stabilize the developing negative charge of the polar transition product in the chorismate mutase reaction and the pyruvate byproduct in the IPL reaction. therefore the ordering of the active site loop shows induced fit of the enzyme upon substrate binding locks Lys 42 into place for catalysis. | ||
==3D structures of isochorismate pyruvate lyase== | ==3D structures of isochorismate pyruvate lyase== | ||
Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}} | |||
[[3log]] – MtIPL/isochorismate synthase - ''Mycobacterium tuberculosis''<br /> | [[3log]] – MtIPL/isochorismate synthase - ''Mycobacterium tuberculosis''<br /> | ||
[[3rv6]], [[3rv7]], [[3rv8]], [[3rv9]], [[3st6]], [[3veh]] - MtIPL/isochorismate synthase + inhibitor<br /> | [[3rv6]], [[3rv7]], [[3rv8]], [[3rv9]], [[3st6]], [[3veh]] - MtIPL/isochorismate synthase + inhibitor<br /> | ||
[[2h9c]] – PaIPL residues 1-99 – ''Pseudomonas aeruginosa''<br /> | [[2h9c]] – PaIPL residues 1-99 – ''Pseudomonas aeruginosa''<br /> | ||
[[2h9d]] - PaIPL | [[3hgw]] – PaIPL (mutant)<br /> | ||
[[2h9d]] - PaIPL + pyruvate<br /> | |||
[[3rem]] – PaIPL + pyruvate + salicylate<br /> | |||
[[3hgx]], [[3ret]] – PaIPL (mutant) + pyruvate + salicylate<br /> | |||
== References == | |||
<references/> | |||
==Additional Resources== | |||
For additional information, see: [[Amino Acid Synthesis & Metabolism]] | For additional information, see: [[Amino Acid Synthesis & Metabolism]] | ||
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[[Category:Topic Page]] | [[Category:Topic Page]] | ||