5-エノイルピルビニルシキミ酸-3-リン酸合成酵素、5-エノイルピルビニルシキミ酸-3-リン酸シンターゼ

関: 3-phosphoshikimate 1-carboxyvinyltransferase、EPSP synthase

WordNet

a salt of phosphoric acid (同)orthophosphate, inorganic_phosphate
carbonated drink with fruit syrup and a little phosphoric acid

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〈U〉リン酸塩 / 《複数形で》リン酸肥料

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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2017/01/06 05:28:46」(JST)

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5-enolpyruvylshikimate-3-phosphate (EPSP) synthase is an enzyme produced by plants and microorganisms. It catalyzes the chemical reaction:

phosphoenolpyruvate + 3-phosphoshikimate phosphate + 5-enolpyruvylshikimate-3-phosphate (EPSP)

Thus, the two substrates of this enzyme are phosphoenolpyruvate (PEP) and 3-phospho-shikimate, whereas its two products are phosphate and 5-enolpyruvylshikimate-3-phosphate.

It is the biological target of the herbicide glyphosate, and a glyphosate-resistant version of this gene has been used in genetically modified crops.

Nomenclature

The enzyme belongs to the family of transferases, to be specific those transferring aryl or alkyl groups other than methyl groups. The systematic name of this enzyme class is phosphoenolpyruvate:3-phosphoshikimate 5-O-(1-carboxyvinyl)-transferase. Other names in common use include:

5-enolpyruvylshikimate-3-phosphate synthase,
3-enolpyruvylshikimate 5-phosphate synthase,
3-enolpyruvylshikimic acid-5-phosphate synthetase,
5'-enolpyruvylshikimate-3-phosphate synthase,
5-enolpyruvyl-3-phosphoshikimate synthase,
5-enolpyruvylshikimate-3-phosphate synthetase,
5-enolpyruvylshikimate-3-phosphoric acid synthase,
enolpyruvylshikimate phosphate synthase, and
3-phosphoshikimate 1-carboxyvinyl transferase.

Structure

EPSP synthase is a monomeric enzyme with a molecular mass of about 46,000.^[2]^[3]^[4] It is composed of two domains, which are joined by protein strands. This strand acts as a hinge, and can bring the two protein domains closer together. When a substrate binds to the enzyme, ligand bonding causes the two parts of the enzyme to clamp down around the substrate in the active site.

EPSP synthase has been divided into two groups according to glyphosate sensitivity. Class I enzyme, contained in plants and in some bacteria, is inhibited at low micromolar glyphosate concentrations, whereas class II enzyme, found in other bacteria, is resistant to inhibition by glyphosate.^[5]

Shikimate pathway

EPSP synthase participates in the biosynthesis of the aromatic amino acids phenylalanine, tyrosine and tryptophan via the shikimate pathway in bacteria, fungi, and plants. EPSP synthase is produced only by plants and micro-organisms; the gene coding for it is not in the mammalian genome.^[6]^[7] Gut flora of some animals contain EPSPS.^[8]

Reaction

EPSP synthase catalyzes the reaction which converts shikimate-3-phosphate plus phosphoenolpyruvate to 5-enolpyruvylshikimate-3-phosphate (EPSP).^[9]

Herbicide target

EPSP synthase is the biological target for the herbicide glyphosate. Glyphosate is a competitive inhibitor of PEP, acting as a transition state analog that binds more tightly to the EPSPS-S3P complex than PEP and inhibits the shikimate pathway. This binding leads to inhibition of the enzyme's catalysis and shuts down the pathway. Eventually this results in organism death from lack of aromatic amino acids the organism requires to survive.^[5]^[10]

A version of the enzyme that both was resistant to glyphosate and that was still efficient enough to drive adequate plant growth was identified by Monsanto scientists after much trial and error in an Agrobacterium strain called CP4, which was found surviving in a waste-fed column at a glyphosate production facility; this version of enzyme, CP4 EPSPS, is the one that has been engineered into several genetically modified crops.^[5]^[11]

References

^ Priestman MA, Healy ML, Funke T, Becker A, Schönbrunn E (October 2005). "Molecular basis for the glyphosate-insensitivity of the reaction of 5-enolpyruvylshikimate 3-phosphate synthase with shikimate". FEBS Lett. 579 (25): 5773–80. doi:10.1016/j.febslet.2005.09.066. PMID 16225867.
^ Goldsbrough, Peter (1990). "Goldsbrough, Peter B., et al. "Gene amplification in glyphosate tolerant tobacco cells." Plant science 72.1 (1990): 53-62.". Plant Science. 72 (1): 53–62. doi:10.1016/0168-9452(90)90186-r.
^ Abdel-Meguid SS, Smith WW, Bild GS (Dec 1985). "Crystallization of 5-enolpyruvylshikimate 3-phosphate synthase from Escherichia coli". Journal of Molecular Biology. 186 (3): 673. doi:10.1016/0022-2836(85)90140-8. PMID 3912512.
^ Ream JE, Steinrücken HC, Porter CA, Sikorski JA (May 1988). "Purification and Properties of 5-Enolpyruvylshikimate-3-Phosphate Synthase from Dark-Grown Seedlings of Sorghum bicolor". Plant Physiology. 87 (1): 232–8. doi:10.1104/pp.87.1.232. PMC 1054731. PMID 16666109.
^ ^a ^b ^c Pollegioni L, Schonbrunn E, Siehl D (Aug 2011). "Molecular basis of glyphosate resistance-different approaches through protein engineering". The FEBS Journal. 278 (16): 2753–66. doi:10.1111/j.1742-4658.2011.08214.x. PMC 3145815. PMID 21668647.
^ Funke T, Han H, Healy-Fried ML, Fischer M, Schönbrunn E (Aug 2006). "Molecular basis for the herbicide resistance of Roundup Ready crops". Proceedings of the National Academy of Sciences of the United States of America. 103 (35): 13010–5. Bibcode:2006PNAS..10313010F. doi:10.1073/pnas.0603638103. JSTOR 30050705. PMC 1559744. PMID 16916934.
^ Maeda H, Dudareva N (2012). "The shikimate pathway and aromatic amino Acid biosynthesis in plants". Annual Review of Plant Biology. 63 (1): 73–105. doi:10.1146/annurev-arplant-042811-105439. PMID 22554242. The AAA pathways consist of the shikimate pathway (the prechorismate pathway) and individual postchorismate pathways leading to Trp, Phe, and Tyr.... These pathways are found in bacteria, fungi, plants, and some protists but are absent in animals. Therefore, AAAs and some of their derivatives (vitamins) are essential nutrients in the human diet, although in animals Tyr can be synthesized from Phe by Phe hydroxylase....The absence of the AAA pathways in animals also makes these pathways attractive targets for antimicrobial agents and herbicides.
^ Cerdeira AL, Duke SO (2006). "The current status and environmental impacts of glyphosate-resistant crops: a review". Journal of Environmental Quality. 35 (5): 1633–58. doi:10.2134/jeq2005.0378. PMID 16899736.
^ Jaworski EK (1972). "Mode of action of N-phosphonomethyl-glycine: inhibition of aromatic amino acid biosynthesis". J Agric Food Chem. 20: 1195–1198. doi:10.1021/jf60184a057.
^ Schönbrunn E, Eschenburg S, Shuttleworth WA, Schloss JV, Amrhein N, Evans JN, Kabsch W (Feb 2001). "Interaction of the herbicide glyphosate with its target enzyme 5-enolpyruvylshikimate 3-phosphate synthase in atomic detail". Proceedings of the National Academy of Sciences of the United States of America. 98 (4): 1376–80. Bibcode:2001PNAS...98.1376S. doi:10.1073/pnas.98.4.1376. PMC 29264. PMID 11171958.
^ Green JM, Owen MD (Jun 2011). "Herbicide-resistant crops: utilities and limitations for herbicide-resistant weed management". Journal of Agricultural and Food Chemistry. 59 (11): 5819–29. doi:10.1021/jf101286h. PMC 3105486. PMID 20586458.

UpToDate Contents

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English Journal

Construction of iron-polymer-graphene nanocomposites with low nonspecific adsorption and strong quenching ability for competitive immunofluorescent detection of biomarkers in GM crops.

Yin K1, Liu A2, Shangguan L1, Mi L1, Liu X1, Liu Y1, Zhao Y1, Li Y1, Wei W1, Zhang Y1, Liu S1.
Biosensors & bioelectronics.Biosens Bioelectron.2017 Apr 15;90:321-328. doi: 10.1016/j.bios.2016.11.070. Epub 2016 Dec 1.
We developed a new immunofluorescent biosensor by utilizing a novel nanobody (Nb) and iron-polymer-graphene nanocomposites for sensitive detection of 5-enolpyruvylshikimate-3-phosphate synthase from Agrobacdterium tumefaciens strain CP4 (CP4-EPSPS), which considered as biomarkers of genetically modi
PMID 27940234

Non-target-site glyphosate resistance in Conyza bonariensis is based on modified subcellular distribution of the herbicide.

Kleinman Z1, Rubin B1.
Pest management science.Pest Manag Sci.2017 Jan;73(1):246-253. doi: 10.1002/ps.4293. Epub 2016 May 20.
BACKGROUND: Conyza spp. were the first broadleaf weeds reported to have evolved glyphosate resistance. Several mechanisms have been proposed for glyphosate resistance. In an effort to elucidate the mechanism of this resistance in Conyza bonariensis, possible target-site and non-target-site mechanism
PMID 27098558

EPSPS Gene Copy Number and Whole-Plant Glyphosate Resistance Level in Kochia scoparia.

Gaines TA1, Barker AL1, Patterson EL1, Westra P1, Westra EP1, Wilson RG2, Jha P3, Kumar V3, Kniss AR4.
PloS one.PLoS One.2016 Dec 16;11(12):e0168295. doi: 10.1371/journal.pone.0168295. eCollection 2016.
Glyphosate-resistant (GR) Kochia scoparia has evolved in dryland chemical fallow systems throughout North America and the mechanism of resistance involves 5-enolpyruvylshikimate-3-phosphate synthase (EPSPS) gene duplication. Agricultural fields in four states were surveyed for K. scoparia in 2013 an
PMID 27992501

Japanese Journal

Expression of a bacterial aroA mutant, aroA-M1, encoding 5-enolpyruvylshikimate-3-phosphate synthase for the production of glyphosate-resistant tobacco plants

Wang He-Yong,Li Yun-Feng,Xie Long-Xu [他],XU Peilin
Journal of plant research 116(6), 455-460, 2003-12-01
NAID 10012004898

59. Glyphosate 処理が花の形態と色素形成に与える影響

島田淳巳,竹内澄代,木村靖夫
植物化学調節学会研究発表記録集 (38), 76, 2003-10-10
… Glyphosate, a nonselective herbicide, is known to inhibit biosynthesis of aromatic amino acids by inhibition of the shikimate pathway enzyme 5-enolpyruvylshikimate-3-phosphate synthase that catalyzes the production of phenylalanine, tyrosine and tryptophan. …
NAID 110001899861

A T42M Substitution in Bacterial 5-Enolpyruvylshikimate-3-phosphate Synthase (EPSPS) Generates Enzymes with Increased Resistance to Glyphosate(Biochemistry & Molecular Biology)

He Ming,Nie Yan-Fang,Xu Peilin
Bioscience, biotechnology, and biochemistry 67(6), 1405-1409, 2003-06-23
… Mutants of class I enolpyruvylshikimate 3-phosphate synthase (EPSPS) with resistance to glyphosate were produced in a previous study using the staggered extension process with aroA genes from S. …
NAID 110002694238

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★リンクテーブル★

リンク元	「5-エノイルピルビニルシキミ酸-3-リン酸合成酵素」「EPSP synthase」「3-phosphoshikimate 1-carboxyvinyltransferase」「5-エノイルピルビニルシキミ酸-3-リン酸シンターゼ」
関連記事	「phosphate」「synthase」

「5-エノイルピルビニルシキミ酸-3-リン酸合成酵素」

EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase)
	Ribbon diagram of EPSP synthase
Identifiers
Symbol	EPSP_synthase
Pfam	PF00275
InterPro	IPR001986
PROSITE	PDOC00097
SCOP	1eps
SUPERFAMILY	1eps
Available protein structures:
Pfam	structures
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary

Search
PMC	articles
PubMed	articles
NCBI	proteins

EPSP Synthase (3-phosphoshikimate 1-carboxyvinyltransferase)
	EPSP synthase liganded with shikimate.
Identifiers
EC number	2.5.1.19
CAS number	9068-73-9
Databases
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB structures	RCSB PDB PDBe PDBsum
Gene Ontology	AmiGO / EGO
Search
PMC	articles
PubMed	articles
NCBI	proteins

　　[★]

英: 5-enolpyruvylshikimate-3-phosphate synthase、EPSP synthase
関: 3-ホスホシキミ酸1-カルボキシビニルトランスフェラーゼ、5-エノイルピルビニルシキミ酸-3-リン酸シンターゼ、EPSP合成酵素、EPSPシンターゼ

「EPSP synthase」

　　[★] 5-エノイルピルビニルシキミ酸-3-リン酸合成酵素、EPSP合成酵素、EPSPシンターゼ

関: 3-phosphoshikimate 1-carboxyvinyltransferase、5-enolpyruvylshikimate-3-phosphate synthase

「3-phosphoshikimate 1-carboxyvinyltransferase」

　　[★]

3-ホスホシキミ酸1-カルボキシビニルトランスフェラーゼ

関: 5-enolpyruvylshikimate-3-phosphate synthase、EPSP synthase

「5-エノイルピルビニルシキミ酸-3-リン酸シンターゼ」

　　[★]

英: 5-enolpyruvylshikimate-3-phosphate synthase
関: 5-エノイルピルビニルシキミ酸-3-リン酸合成酵素

「phosphate」

　　[★]

n.

(化合物)リン酸塩、リン酸エステル、ホスフェート、フォスフェート、リン酸

関: inorganic phosphate、orthophosphate、orthophosphoric acid、phospho、phosphoester、phosphoric、phosphoric acid、phosphoric acid ester、phosphorus

「synthase」

　　[★]

n.

(脱離酵素リアーゼの逆反応である合成方向の反応を指す) シンターゼ, 合成酵素, 付加酵素

関: lyase、synthetase、transferase

[pmid16225867-1] Priestman MA, Healy ML, Funke T, Becker A, Schönbrunn E (October 2005). "Molecular basis for the glyphosate-insensitivity of the reaction of 5-enolpyruvylshikimate 3-phosphate synthase with shikimate". FEBS Lett. 579 (25): 5773–80. doi:10.1016/j.febslet.2005.09.066. PMID 16225867.

[2] Goldsbrough, Peter (1990). "Goldsbrough, Peter B., et al. "Gene amplification in glyphosate tolerant tobacco cells." Plant science 72.1 (1990): 53-62.". Plant Science. 72 (1): 53–62. doi:10.1016/0168-9452(90)90186-r.

[3] Abdel-Meguid SS, Smith WW, Bild GS (Dec 1985). "Crystallization of 5-enolpyruvylshikimate 3-phosphate synthase from Escherichia coli". Journal of Molecular Biology. 186 (3): 673. doi:10.1016/0022-2836(85)90140-8. PMID 3912512.

[4] Ream JE, Steinrücken HC, Porter CA, Sikorski JA (May 1988). "Purification and Properties of 5-Enolpyruvylshikimate-3-Phosphate Synthase from Dark-Grown Seedlings of Sorghum bicolor". Plant Physiology. 87 (1): 232–8. doi:10.1104/pp.87.1.232. PMC 1054731. PMID 16666109.

[Pollegioni-5] Pollegioni L, Schonbrunn E, Siehl D (Aug 2011). "Molecular basis of glyphosate resistance-different approaches through protein engineering". The FEBS Journal. 278 (16): 2753–66. doi:10.1111/j.1742-4658.2011.08214.x. PMC 3145815. PMID 21668647.

[Funke_2006-6] Funke T, Han H, Healy-Fried ML, Fischer M, Schönbrunn E (Aug 2006). "Molecular basis for the herbicide resistance of Roundup Ready crops". Proceedings of the National Academy of Sciences of the United States of America. 103 (35): 13010–5. Bibcode:2006PNAS..10313010F. doi:10.1073/pnas.0603638103. JSTOR 30050705. PMC 1559744. PMID 16916934.

[MaedaDudareva2012-7] Maeda H, Dudareva N (2012). "The shikimate pathway and aromatic amino Acid biosynthesis in plants". Annual Review of Plant Biology. 63 (1): 73–105. doi:10.1146/annurev-arplant-042811-105439. PMID 22554242. The AAA pathways consist of the shikimate pathway (the prechorismate pathway) and individual postchorismate pathways leading to Trp, Phe, and Tyr.... These pathways are found in bacteria, fungi, plants, and some protists but are absent in animals. Therefore, AAAs and some of their derivatives (vitamins) are essential nutrients in the human diet, although in animals Tyr can be synthesized from Phe by Phe hydroxylase....The absence of the AAA pathways in animals also makes these pathways attractive targets for antimicrobial agents and herbicides.

[pmid16899736-8] Cerdeira AL, Duke SO (2006). "The current status and environmental impacts of glyphosate-resistant crops: a review". Journal of Environmental Quality. 35 (5): 1633–58. doi:10.2134/jeq2005.0378. PMID 16899736.

[9] Jaworski EK (1972). "Mode of action of N-phosphonomethyl-glycine: inhibition of aromatic amino acid biosynthesis". J Agric Food Chem. 20: 1195–1198. doi:10.1021/jf60184a057.

[pmid11171958-10] Schönbrunn E, Eschenburg S, Shuttleworth WA, Schloss JV, Amrhein N, Evans JN, Kabsch W (Feb 2001). "Interaction of the herbicide glyphosate with its target enzyme 5-enolpyruvylshikimate 3-phosphate synthase in atomic detail". Proceedings of the National Academy of Sciences of the United States of America. 98 (4): 1376–80. Bibcode:2001PNAS...98.1376S. doi:10.1073/pnas.98.4.1376. PMC 29264. PMID 11171958.

[GreenOwen2011-11] Green JM, Owen MD (Jun 2011). "Herbicide-resistant crops: utilities and limitations for herbicide-resistant weed management". Journal of Agricultural and Food Chemistry. 59 (11): 5819–29. doi:10.1021/jf101286h. PMC 3105486. PMID 20586458.

v t e Enzymes

Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis

Regulation	Allosteric regulation Cooperativity Enzyme inhibitor

Classification	EC number Enzyme superfamily Enzyme family List of enzymes

Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics

Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list)

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案内

5-enolpyruvylshikimate-3-phosphate synthase