|
|
| Line 2: |
Line 2: |
| == Function == | | == Function == |
|
| |
|
| '''5-enolpyruvylshikimate 3-phosphate (EPSP) synthase''' is a key enzyme for the biosynthesis of aromatic amino acids in plants and many microbes. Consequently. EPSP synthase catalyzes the addition of phosphoenol pyruvate (PEP) to shikimate-3-phosphate, generating 5-enolpyruvylshikimate-3-phosphate, which is a precursor for phenylalanine and tyrosine<ref>PMID:16225867</ref>. | | '''5-enolpyruvylshikimate 3-phosphate (EPSP) synthase''' is a key enzyme for the biosynthesis of aromatic amino acids in plants and many microbes. Consequently. EPSP synthase catalyzes the addition of phosphoenol pyruvate (PEP) to shikimate-3-phosphate (S3P), generating 5-enolpyruvylshikimate-3-phosphate, which is a precursor for phenylalanine and tyrosine<ref>PMID:16225867</ref>. |
|
| |
|
| == Relevance == | | == Relevance == |
Revision as of 21:27, 19 January 2016
| Function
5-enolpyruvylshikimate 3-phosphate (EPSP) synthase is a key enzyme for the biosynthesis of aromatic amino acids in plants and many microbes. Consequently. EPSP synthase catalyzes the addition of phosphoenol pyruvate (PEP) to shikimate-3-phosphate (S3P), generating 5-enolpyruvylshikimate-3-phosphate, which is a precursor for phenylalanine and tyrosine[1].
Relevance
EPSP synthase is a target for drugs and herbicides.
Structural insights
The enzyme has two domains, with the active site found in the interdomain cleft. There is a substantial structural change upon substrate binding, resulting in a closed formation. Glyphosate (also known as Roundup) occupies the binding site of the second substrate, phosphoenol pyruvate.
- ↑ Priestman MA, Healy ML, Funke T, Becker A, Schonbrunn E. Molecular basis for the glyphosate-insensitivity of the reaction of 5-enolpyruvylshikimate 3-phosphate synthase with shikimate. FEBS Lett. 2005 Oct 24;579(25):5773-80. PMID:16225867 doi:10.1016/j.febslet.2005.09.066
|
3D structures of EPSP synthase
Updated on 19-January-2016
{"openlevels":0}
- 5-enolpyruvylshikimate 3-phosphate (EPSP) synthase
- 1eps – EcEPSP – Escherichia coli
- 1p88, 1p89 - EcEPSP N terminal - NMR
- 1rf5 - SpEPSP – Streptococcus pneumoniae
- 2bjb, 2o15 – MtEPSP – Mycobacterium tuberculosis
- 2gg4 – AgEPSP – Agrobacterium
- 3roi, 3tr1, 4gfp – CbEPSP – Coxiella burnetii
- 3ti2 - VcEPSP N terminal – Vibrio cholerae
- 3rmt – EPSP – Bacillus halodurans
- EPSP synthase binary complex
- EPSP synthase ternary complex
- 1g6s - EcEPSP + S3P + glyphosate
- 2qft, 2qfu, 3fjz, 3fk1 - EcEPSP (mutant) + S3P + glyphosate
- 2aay - EcEPSP + shikimate + glyphosate
- 1rf6 - SpEPSP + S3P + glyphosate
- 2gga - AgEPSP + S3P + glyphosate
- 2ggd - AgEPSP (mutant) + S3P + glyphosate
- 2o0e - MtEPSP + S3P + phosphoenolpyruvate
- 3nvs - VcEPSP + S3P + glyphosate
- 3slh - CbEPSP + S3P + glyphosate
References
