Information on EC 2.2.1.9 - 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid synthase:
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The lowest common taxonomy group for this enzyme is: Escherichia coli

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EC NUMBERCOMMENTARY
2.2.1.9formerly a partial reaction of EC 2.5.1.64

RECOMMENDED NAMEGeneOntology No.
2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid synthaseGO:0070204

REACTIONREACTION DIAGRAMCOMMENTARYORGANISM UNIPROT ACCESSION NO.LITERATURE
isochorismate + 2-oxoglutarate = 5-enolpyruvoyl-6-hydroxy-2-succinyl-cyclohex-3-ene-1-carboxylate + CO2
show the reaction diagram		----

REACTION TYPEORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
decarboxylationEscherichia coli K-12--705201

PATHWAYKEGG LinkMetaCyc Link
1,4-dihydroxy-2-naphthoate biosynthesis I-PWY-5837
1,4-dihydroxy-2-naphthoate biosynthesis II (plants)-PWY-5791

SYSTEMATIC NAMEIUBMB Comments
isochorismate:2-oxoglutarate 4-oxopentanoatetransferase (decarboxylating)Requires Mg2+ for maximal activity. This enzyme is involved in the biosynthesis of vitamin K2 (menaquinone). In most anaerobes and all Gram-positive aerobes, menaquinone is the sole electron transporter in the respiratory chain and is essential for their survival. It had previously been thought that the products of the reaction were (1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate (SHCHC), pyruvate and CO2 but it is now known that two separate enzymes are involved: this enzyme and EC 4.2.99.20, 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase. Under basic conditions, the product can spontaneously lose pyruvate to form SHCHC.

SYNONYMSORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexadiene-1-carboxylate synthaseEscherichia coli K-12P17109-702035, 705130
2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthaseEscherichia coli K-12--705201
EcMenDEscherichia coli K-12--705130
MenDEscherichia coli--684159, 685086
MenDEscherichia coli K-12--702035, 705130, 705201
SEPHCHC synthaseEscherichia coli--685086
SHCHC synthaseEscherichia coli K-12--705201

CAS REGISTRY NUMBERCOMMENTARY
122007-88-9-

ORGANISMCOMMENTARYLITERATURESEQUENCE CODESEQUENCE DB SOURCE
Escherichia coli-684159, 685086--Manually annotated by BRENDA team
Escherichia coli K-12-702035, 705130P17109UniProtManually annotated by BRENDA team
Escherichia coli K-12-705201--Manually annotated by BRENDA team

GENERAL INFORMATIONORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
physiological functionEscherichia coli K-12-first enzyme in biosynthesis of menaquinone or vitamin K2, influence on electron transport in bacteria705130

SUBSTRATEPRODUCT                      REACTION DIAGRAMORGANISM UNIPROT ACCESSION NO. COMMENTARY/
Substrate		 LITERATURE/
Substrate		 COMMENTARY/
Product		 LITERATURE/
Product		 Reversibility
r=reversible
ir=irreversible
?=not specified
2,3-dihydroxybenzaldehyde + 2-oxoglutarate(5R)-5-(2,3-dihydroxyphenyl)-5-hydroxy-4-oxopentanoic acid + CO2
show the reaction diagram		Escherichia coli K-12-assay at pH 8705201---
2-bromobenzaldehyde + 2-oxoglutarate(5R)-5-(2-bromophenyl)-5-hydroxy-4-oxopentanoic acid + CO2
show the reaction diagram		Escherichia coli K-12-assay at pH 8705201---
2-chlorobenzaldehyde + 2-oxoglutarate(5R)-5-(2-chlorophenyl)-5-hydroxy-4-oxopentanoic acid + CO2
show the reaction diagram		Escherichia coli K-12-assay at pH 8705201---
2-fluorobenzaldehyde + 2-oxoglutarate(5R)-5-(2-fluorophenyl)-5-hydroxy-4-oxopentanoic acid + CO2
show the reaction diagram		Escherichia coli K-12-assay at pH 8705201---
2-fluorobenzaldehyde + oxaloacetate(1R)-1-(2-fluorophenyl)-1-hydroxypropan-2-one + 2 CO2
show the reaction diagram		Escherichia coli K-12-assay at pH 8705201---
2-fluorobenzaldehyde + pyruvate(1R)-1-(2-fluorophenyl)-1-hydroxypropan-2-one + CO2
show the reaction diagram		Escherichia coli K-12-assay at pH 8705201---
2-iodobenzaldehyde + 2-oxoglutarate(5R)-5-hydroxy-5-(2-iodophenyl)-4-oxopentanoic acid + CO2
show the reaction diagram		Escherichia coli K-12-assay at pH 8705201---
2-methylbenzaldehyde + 2-oxoglutarate(5R)-5-hydroxy-5-(2-methylphenyl)-4-oxopentanoic acid + CO2
show the reaction diagram		Escherichia coli K-12-assay at pH 8705201---
3,4-dihydroxybenzaldehyde + 2-oxoglutarate(5R)-5-(3,4-dihydroxyphenyl)-5-hydroxy-4-oxopentanoic acid + CO2
show the reaction diagram		Escherichia coli K-12-assay at pH 8705201---
3-fluorobenzaldehyde + 2-oxoglutarate(5R)-5-(3-fluorophenyl)-5-hydroxy-4-oxopentanoic acid + CO2
show the reaction diagram		Escherichia coli K-12-assay at pH 8705201---
3-iodobenzaldehyde + 2-oxoglutarate(5R)-5-hydroxy-5-(3-iodophenyl)-4-oxopentanoic acid + CO2
show the reaction diagram		Escherichia coli K-12-assay at pH 8705201---
3-methoxybenzaldehyde + 2-oxoglutarate(5R)-5-hydroxy-5-(3-methoxyphenyl)-4-oxopentanoic acid + CO2
show the reaction diagram		Escherichia coli K-12-assay at pH 8705201---
4-chlorbenzaldehyde + 2-oxoglutarate(5R)-5-(4-chlorophenyl)-5-hydroxy-4-oxopentanoic acid + CO2
show the reaction diagram		Escherichia coli K-12-assay at pH 8705201---
4-fluorobenzaldehyde + 2-oxoglutarate(5R)-5-(4-fluorophenyl)-5-hydroxy-4-oxopentanoic acid + CO2
show the reaction diagram		Escherichia coli K-12-assay at pH 8705201---
4-hydroxybenzaldehyde + 2-oxoglutarate(5R)-5-hydroxy-5-(4-hydroxyphenyl)-4-oxopentanoic acid + CO2
show the reaction diagram		Escherichia coli K-12-assay at pH 8705201---
acetaldehyde + 2-oxoglutarate(5R)-5-hydroxy-4-oxohexanoic acid + CO2
show the reaction diagram		Escherichia coli K-12-assay at pH 8705201---
benzaldehyde + 2-oxoglutarate(5R)-5-hydroxy-4-oxo-5-phenylpentanoic acid + CO2
show the reaction diagram		Escherichia coli K-12-assay at pH 8705201---
benzaldehyde + oxaloacetate(1R)-1-hydroxy-1-phenylpropan-2-one + 2 CO2
show the reaction diagram		Escherichia coli K-12-assay at pH 8705201---
benzaldehyde + pyruvate(1R)-1-hydroxy-1-phenylpropan-2-one + 2 CO2
show the reaction diagram		Escherichia coli K-12-assay at pH 8705201---
cyclohex-1-ene-1-carbaldehyde + 2-oxoglutarate(5R)-5-cyclohex-1-en-1-yl-5-hydroxy-4-oxopentanoic acid + CO2
show the reaction diagram		Escherichia coli K-12-assay at pH 8705201---
glyoxylate + 2-oxoglutarate5-hydroxy-4-oxopentanoic acid + 2 CO2
show the reaction diagram		Escherichia coli K-12-assay at pH 8705201---
hexanal + 2-oxoglutarate(5R)-5-hydroxy-4-oxodecanoic acid + CO2
show the reaction diagram		Escherichia coli K-12-assay at pH 8705201---
isochorismate + 2-oxoglutarate5-enolpyruvoyl-6-hydroxy-2-succinyl-cyclohex-3-ene-1-carboxylate + CO2
show the reaction diagram		Escherichia coli-the enzyme is involved in biosynthesis of vitamin K2 (menoquinone). Under basic conditions, the product can spontaneously lose pyruvate to form (1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate, under basic conditions, the product can spontaneously lose pyruvate to form (1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate685086--?
pyruvate + 2-oxoglutarate4-hydroxy-5-oxohexanoic acid + 2 CO2
show the reaction diagram		Escherichia coli K-12-assay at pH 8705201---
undec-10-enal + 2-oxoglutarate(5R)-5-hydroxy-4-oxopentadec-14-enoic acid + CO2
show the reaction diagram		Escherichia coli K-12-assay at pH 8705201---
isochorismate + 2-oxoglutarate(1R,2S,5S,6S)-5-[(1-carboxyethenyl)oxy]-2-(3-carboxypropanoyl)-6-hydroxycyclohex-3-ene-1-carboxylic acid + CO2
show the reaction diagram		Escherichia coli K-12-assay at pH 8705201---
additional information?-Escherichia coli-MenD participates in the menaquinone (vitamin K2) biosynthetic pathway684159---

NATURAL SUBSTRATESNATURAL PRODUCTSREACTION DIAGRAMORGANISM UNIPROT ACCESSION NO.COMMENTARY SUBSTRATELITERATURE
(Substrate)		COMMENTARY PRODUCTLITERATURE
(Product)
isochorismate + 2-oxoglutarate5-enolpyruvoyl-6-hydroxy-2-succinyl-cyclohex-3-ene-1-carboxylate + CO2
show the reaction diagram		Escherichia coli-the enzyme is involved in biosynthesis of vitamin K2 (menoquinone). Under basic conditions, the product can spontaneously lose pyruvate to form (1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate685086--
additional information?-Escherichia coli-MenD participates in the menaquinone (vitamin K2) biosynthetic pathway684159--

COFACTORORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATUREIMAGE
thiamine diphosphateEscherichia coli K-12--705130, 705201 2D-image

METALS and IONS ORGANISM UNIPROT ACCESSION NO.COMMENTARY LITERATURE
Mg2+Escherichia coli-required, Km: 0.08 mM685086

INHIBITORSORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

ACTIVATING COMPOUNDORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
thiamine diphosphateEscherichia coli-required, Km: 0.0024 mM685086 2D-image

KM VALUE [mM]KM VALUE [mM] MaximumSUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
1.5-2-oxoglutarateEscherichia coli-pH 7.8, 22°C685086 2D-image
0.053-isochorismateEscherichia coli-pH 7.8, 22°C685086 2D-image

TURNOVER NUMBER [1/s] TURNOVER NUMBER MAXIMUM[1/s] SUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
0.075-2-oxoglutarateEscherichia coli-pH 7.8, 22°C685086 2D-image
0.05-isochorismateEscherichia coli-pH 7.8, 22°C685086 2D-image

kcat/KM VALUE [1/mMs-1]kcat/KM VALUE [1/mMs-1] MaximumSUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

Ki VALUE [mM]Ki VALUE [mM] MaximumINHIBITORORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

IC50 VALUE [mM]IC50 VALUE [mM] MaximumINHIBITORORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

SPECIFIC ACTIVITY [µmol/min/mg] SPECIFIC ACTIVITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

pH OPTIMUMpH MAXIMUMORGANISM UNIPROT ACCESSION NO. COMMENTARYLITERATURE
78Escherichia coli-phosphate buffer685086
8-Escherichia coli K-12-assay at705201

pH RANGEpH RANGE MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

TEMPERATURE OPTIMUMTEMPERATURE OPTIMUM MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

TEMPERATURE RANGE TEMPERATURE MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

pI VALUEpI VALUE MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

SOURCE TISSUE ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE SOURCE
No entries in this field

LOCALIZATION ORGANISM UNIPROT ACCESSION NO. COMMENTARY GeneOntology No. LITERATURE SOURCE
No entries in this field

PDBSCOPCATHORGANISM
2x7j, downloadSCOP (2x7j)CATH (2x7j)Bacillus subtilis (strain 168)
2jla, downloadSCOP (2jla)CATH (2jla)Escherichia coli (strain K12)
2jlc, downloadSCOP (2jlc)CATH (2jlc)Escherichia coli (strain K12)
3flm, downloadSCOP (3flm)CATH (3flm)Escherichia coli (strain K12)
3hww, downloadSCOP (3hww)CATH (3hww)Escherichia coli (strain K12)
3hwx, downloadSCOP (3hwx)CATH (3hwx)Escherichia coli (strain K12)
3lq1, downloadSCOP (3lq1)CATH (3lq1)Listeria monocytogenes serotype 4b (strain F2365)

MOLECULAR WEIGHT MOLECULAR WEIGHT MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
61400-Escherichia coli K-12-gel filtration705130
62000-Escherichia coli K-12-SDS-PAGE702035

SUBUNITS ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
?Escherichia coli K-12P17109dimer or tetramer702035, 705130

POSTTRANSLATIONAL MODIFICATION ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

Crystallization/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
crystallization of the apoenzyme and holoenzyme forms of MenD. The apoenzyme crystals are obtained by sitting-drop vapour diffusion with 70% MPD. The crystals are too small to collect diffraction data and a search for better conditions is not successful. Single crystals of the holoenzyme with thiamin diphosphate and Mn2+ as cofactors are obtained by the hanging-drop vapour-diffusion method with 35% ethylene glycol as precipitant. Diffraction data are collected on a cryocooled crystal to a resolution of 2.0 AEscherichia coli-684159
sitting and hanging vapor diffusion method, hexagonal complex with thiamine diphosphate and Mn2+Escherichia coli K-12-705130
tetragonal crystal formEscherichia coli K-12-702035

pH STABILITYpH STABILITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

TEMPERATURE STABILITYTEMPERATURE STABILITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARYLITERATURE
additional information-Escherichia coli K-12-melting temperature 53°C, melting temperature 57.3°C of protein complex with thiamin diphosphate, melting temperature 54°C of protein complex with 2-oxoglutarate, melting temperature 54.5°C of protein complex with FAD702035

GENERAL STABILITYORGANISM UNIPROT ACCESSION NO.LITERATURE
2-oxoglutarate improves protein stabilityEscherichia coli K-12-702035
FAD improves protein stabilityEscherichia coli K-12-702035
thiamine diphosphate improves protein stabilityEscherichia coli K-12-702035

ORGANIC SOLVENT ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

OXIDATION STABILITY ORGANISM UNIPROT ACCESSION NO. LITERATURE
No entries in this field

STORAGE STABILITY ORGANISM UNIPROT ACCESSION NO. LITERATURE
4°C, desalting buffer with 50 mM phosphate, 1 mM thiamine diphosphate and 2 mM MgCl2, pH 8.0, 4 weeks, no significant loss of activityEscherichia coli K-12-705201

Purification/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
-Escherichia coli-684159, 685086
first step His-Trap chromatography, second step ion-exchange chromatography with Q column, third step chromatography with Superdex columnEscherichia coli K-12-702035
gel permeation chromatographyEscherichia coli K-12-705201
Ni2+ affinity column, size-exclusion columnEscherichia coli K-12-705130

Cloned/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
-Escherichia coli-684159, 685086
expression in Escherichia coli BL21Escherichia coli K-12-705201
overexpression in Escherichia coli BL21Escherichia coli K-12-702035

EXPRESSION ORGANISM UNIPROT ACCESSION NO. LITERATURE
No entries in this field

ENGINEERINGORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

Renatured/COMMENTARYORGANISM UNIPROT ACCESSION NO.LITERATURE
No entries in this field

APPLICATIONORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

REF. AUTHORS TITLE JOURNAL VOL. PAGES YEAR ORGANISMLINK TO PUBMEDSOURCE
684159Sieminska, E.A.; Macova, A.; Palmer, D.R.; Sanders, D.A.Crystallization and preliminary X-ray analysis of (1R,6R)-2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate (SHCHC) synthase (MenD) from Escherichia coliActa Crystallogr. Sect. F61489-4922005Escherichia coli PubMed
685086Jiang, M.; Cao, Y.; Guo, Z.F.; Chen, M.; Chen, X.; Guo, Z.Menaquinone biosynthesis in Escherichia coli: identification of 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate as a novel intermediate and re-evaluation of MenD activityBiochemistry4610979-109892007Escherichia coli PubMed
702035Priyadarshi, A.; Saleem, Y.; Nam, K.H.; Kim, K.S.; Park, S.Y.; Kim, E.E.; Hwang, K.Y.Structural insights of the MenD from Escherichia coli reveal ThDP affinityBiochem. Biophys. Res. Commun.380797-8012009Escherichia coli K-12 PubMed
705130Dawson, A.; Fyfe, P.K.; Hunter, W.N.Specificity and reactivity in menaquinone biosynthesis: the structure of Escherichia coli MenD (2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexadiene-1-carboxylate synthase)J. Mol. Biol.3841353-13682008Escherichia coli K-12 PubMed
705201Kurutsch, A.; Richter, M.; Brecht, V.; Sprenger, G.; Müller, M.MenD as a versatile catalyst for asymmetric synthesisJ. Mol. Catal. B6156-662009Escherichia coli K-12-

LINKS TO OTHER DATABASES (specific for EC-Number 2.2.1.9)
ExplorEnz
ExPASy
KEGG
MetaCyc
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
SYSTERS
Protein Mutant Database
InterPro (database of protein families, domains and functional sites)