Information on EC 4.2.99.20 - 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
4.2.99.20
-
RECOMMENDED NAME
GeneOntology No.
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
5-enolpyruvoyl-6-hydroxy-2-succinylcyclohex-3-ene-1-carboxylate = (1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate + pyruvate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
elimination
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
1,4-dihydroxy-2-naphthoate biosynthesis
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-
Biosynthesis of secondary metabolites
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Metabolic pathways
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Ubiquinone and other terpenoid-quinone biosynthesis
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vitamin K metabolism
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SYSTEMATIC NAME
IUBMB Comments
5-enolpyruvoyl-6-hydroxy-2-succinylcyclohex-3-ene-1-carboxylate pyruvate-lyase [(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate-forming]
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 reactions carried out by this enzyme and EC 2.2.1.9, 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid synthase, were carried out by a single enzyme but this has since been disproved [2].
CAS REGISTRY NUMBER
COMMENTARY hide
122007-88-9
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
Q5HH39
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
-
involved in menaquinone biosynthesis
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(1R,2S,5S,6S)-2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate
(1R,6R)-2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate + pyruvate
show the reaction diagram
2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate
(1R,6R)-2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate + pyruvate
show the reaction diagram
-
assay at 37°C, pH 7.0
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-
?
5-enolpyruvoyl-6-hydroxy-2-succinyl-cyclohex-3-ene-1-carboxylate
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate + pyruvate
show the reaction diagram
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
5-enolpyruvoyl-6-hydroxy-2-succinyl-cyclohex-3-ene-1-carboxylate
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate + pyruvate
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
SHCHC synthase activity of MenH is not affected by the addition of a divalent ion (1 mM of Mg2+, Ba2+, Mn2+, Ca2+, Co2+, or Ni2+)
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0086 - 0.532
(1R,2S,5S,6S)-2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate
0.0083 - 0.118
2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate
0.0083 - 0.118
5-enolpyruvoyl-6-hydroxy-2-succinyl-cyclohex-3-ene-1-carboxylate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00058 - 147
(1R,2S,5S,6S)-2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate
0.18 - 167
5-enolpyruvoyl-6-hydroxy-2-succinyl-cyclohex-3-ene-1-carboxylate
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0392 - 14000
(1R,2S,5S,6S)-2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate
2803
67 - 20000000
2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate
14940
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
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assay at
PDB
SCOP
CATH
ORGANISM
UNIPROT
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Staphylococcus aureus (strain COL)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25400
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
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; 1 * 25400
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
native enzyme to 2.75 A resolution, together with the structures of the active site mutant proteins Tyr85Phe and Arg124Ala, both at 2.5 A resolution. The enzyme has the predicted alpha/beta hydrolase fold with its core alpha/beta domain capped by a helical lid. The active site, a long groove beneath the cap, contains a number of conserved basic residues and is found to bind exogeneous anions, modeled as sulfate and chloride, in all three crystal structures. The bound anions may mark the binding sites for anionic groups on the substrate
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to 1.45 A resolution. The nucleophilicity of the catalytic serine-histidine-aspartate triad is shielded and its catalytic role is limited to being a specific general base by an open-closed conformational change
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to 2 A resolution. The overall basic active site displays pronounced hydrophobic character on one side and these properties complement those of the substrate. A complex network of hydrogen bonds involving well-ordered water molecules serves to position key residues participating in the recognition of substrate and subsequent catalysis. Proton shuttle mechanism, reliant on a catalytic triad consisting of Ser89, Asp216 and His243. The reaction is initiated by proton abstraction from the substrate by an activated Ser89. The propensity to form a conjugated system provides the driving force for pyruvate elimination. During the elimination, a methylene group is converted to a methyl and probybly His243 provides a proton, previously acquired from Ser89 for reduction. A conformational change of the protonated His243 may be encouraged by the presence of an anionic intermediate in the active site
Q5HH39
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
; combination of Ni2+-affinity chromatography and size-exclusion chromatography
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immobilized metal ion affinity chromatography, gel filtration
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3)
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expression in Escherichia coli
Q5HH39
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D128A
-
conserved among MenH proteins
F153A
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residue involved in open-closed transition, mutation leads to large decrease in enzymatic activity
H232K
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part of the catalytically essential triad
K212A
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conserved among MenH proteins
R124A
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conserved among MenH proteins
R168A
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conserved among MenH proteins
R90A
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conserved among MenH proteins
V152A
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residue involved in open-closed transition, mutation leads to large decrease in enzymatic activity
V152G
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residue involved in open-closed transition, mutation leads to large decrease in enzymatic activity
V152G/F153A
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inactive
W147A
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conserved among MenH proteins
W147A/Y148A
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inactive
W147F
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conserved among MenH proteins
Y148A
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residue involved in open-closed transition, mutation leads to large decrease in enzymatic activity
Y148F
-
residue involved in open-closed transition, mutation leads to large decrease in enzymatic activity
Y85F
-
conserved among MenH proteins
Show AA Sequence (2667 entries)
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