Chorismate synthase
From Proteopedia
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<StructureSection load='1qxo' size='340' side='right' caption='Caption for this structure' scene=''> | <StructureSection load='1qxo' size='340' side='right' caption='Caption for this structure' scene=''> | ||
| - | the article describing Jmol <ref>PMID:21638687</ref> to the rescue. | ||
== Function == | == Function == | ||
| - | '''Chorismate synthase''' (CS) or '''5-enolpyruvylshikimate-3-phosphate phopholyase''' 5-enolpyruvylshikimate-3-phosphate (EPSP) | + | '''Chorismate synthase''' (CS) or '''5-enolpyruvylshikimate-3-phosphate phopholyase''' is the seventh enzyme in the shikimate pathway which catalyzes the transition of phosphenol pyruvate to chorismate in prokaryotic bacteria and plants. Chorismate is a precursor for the synthesis of aromatic amino acids in the bacteria<ref>PMID:23697663</ref>. Cs also plays a role in the biosynthesis of nucleotides. CS catalyzes the conversion of 5-enolpyruvylshikimate-3-phosphate (EPSP) to chorismate. The activity of CS requires the presence of FMN. |
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== Relevance == | == Relevance == | ||
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| + | CS inhibitors which inhibit the shikimate pathway, serve as antimicrobial agents<ref>PMID:18445278</ref>. | ||
== Structural highlights == | == Structural highlights == | ||
| - | + | The 3D structure of CS complex with its cofactor FMN and its substrate EPSP shows the EPSP binding site as very hydrophobic containing numerous Arg. Lys and His residues. The FMN cofactor has numerous interactions with CS and its phosphate moiety is located in the dimer interface and interacts with residues of the other monomer as well<ref>PMID:14656434</ref>. | |
</StructureSection> | </StructureSection> | ||
Revision as of 08:24, 18 April 2020
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3D structures of chorismate synthase
References
- ↑ Pitchandi P, Hopper W, Rao R. Comprehensive database of Chorismate synthase enzyme from shikimate pathway in pathogenic bacteria. BMC Pharmacol Toxicol. 2013 May 22;14:29. doi: 10.1186/2050-6511-14-29. PMID:23697663 doi:http://dx.doi.org/10.1186/2050-6511-14-29
- ↑ Ely F, Nunes JE, Schroeder EK, Frazzon J, Palma MS, Santos DS, Basso LA. The Mycobacterium tuberculosis Rv2540c DNA sequence encodes a bifunctional chorismate synthase. BMC Biochem. 2008 Apr 29;9:13. doi: 10.1186/1471-2091-9-13. PMID:18445278 doi:http://dx.doi.org/10.1186/1471-2091-9-13
- ↑ Maclean J, Ali S. The structure of chorismate synthase reveals a novel flavin binding site fundamental to a unique chemical reaction. Structure. 2003 Dec;11(12):1499-511. PMID:14656434
