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EC Tree
IUBMB Comments 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 .
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
shchc, 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase, (1r,6r)-2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase,
more
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(1R,6R)-2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase
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EC 2.5.1.64
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formerly, part transferred
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MenH
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SHCHC synthase
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5-enolpyruvoyl-6-hydroxy-2-succinylcyclohex-3-ene-1-carboxylate = (1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate + pyruvate
5-enolpyruvoyl-6-hydroxy-2-succinylcyclohex-3-ene-1-carboxylate = (1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate + pyruvate
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-
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5-enolpyruvoyl-6-hydroxy-2-succinylcyclohex-3-ene-1-carboxylate = (1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate + pyruvate
the nucleophilicity of the catalyitc serine-histidine-aspartate triad is shielded and its catalytic role is limited to being a specific general base by an open-closed conformational change. The enzyme adopts an open conformation without a functional triad in its ligand-free form and a closed conformation with a fully functional catalytic triad in the presence of its reaction product. The open-to-closed conformational transition involves movement of half of the alpha-helical cap domain, which causes extensive structural changes in the apha/beta-domain and forces the side chainof the triad histidine to adopt an energetically disfavored gauche conformation to form the functional triad. The inactive open conformation without a triad prevails in ligand-free solution and is converted to the closed conformation with a properly formed triad by the reaction product
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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].
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(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
2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate
(1R,6R)-2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate + pyruvate
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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
(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
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-
-
-
?
(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
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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
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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
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step in menaquinone biosynthesis
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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
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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
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the enzyme is involved in biosynthesis of vitamin K2 (manoquinone). Under basic conditions, the product can spontaneously lose pyruvate to form (1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
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?
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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
5-enolpyruvoyl-6-hydroxy-2-succinyl-cyclohex-3-ene-1-carboxylate
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate + pyruvate
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step in menaquinone biosynthesis
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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
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the enzyme is involved in biosynthesis of vitamin K2 (manoquinone). Under basic conditions, the product can spontaneously lose pyruvate to form (1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
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-
?
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additional information
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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+)
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Dehydration
Evolution of enzymatic activity in the enolase superfamily: structural and mutagenic studies of the mechanism of the reaction catalyzed by o-succinylbenzoate synthase from Escherichia coli.
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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
0.0086
(1R,2S,5S,6S)-2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate
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H232A mutant protein
0.01
(1R,2S,5S,6S)-2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate
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wild-type protein
0.013
(1R,2S,5S,6S)-2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate
wild-type, pH 7.0, temperature not specified in the publication
0.014
(1R,2S,5S,6S)-2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate
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Y85F mutant protein
0.0194
(1R,2S,5S,6S)-2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate
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K212A mutant protein
0.0237
(1R,2S,5S,6S)-2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate
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W147A mutant protein
0.028
(1R,2S,5S,6S)-2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate
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S86A mutant protein
0.036
(1R,2S,5S,6S)-2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate
mutant Y148F, pH 7.0, temperature not specified in the publication
0.05
(1R,2S,5S,6S)-2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate
mutant Y148A, pH 7.0, temperature not specified in the publication
0.07
(1R,2S,5S,6S)-2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate
mutant F153A, pH 7.0, temperature not specified in the publication
0.074
(1R,2S,5S,6S)-2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate
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W147F mutant protein
0.084
(1R,2S,5S,6S)-2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate
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R124A mutant protein
0.085
(1R,2S,5S,6S)-2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate
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D128A mutant protein
0.118
(1R,2S,5S,6S)-2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate
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D210A mutant protein
0.134
(1R,2S,5S,6S)-2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate
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R168A mutant protein
0.159
(1R,2S,5S,6S)-2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate
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R90A mutant protein
0.16
(1R,2S,5S,6S)-2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate
mutant V152G, pH 7.0, temperature not specified in the publication
0.3
(1R,2S,5S,6S)-2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate
mutant V152A, pH 7.0, temperature not specified in the publication
0.532
(1R,2S,5S,6S)-2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate
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H232K mutant protein
0.0083
2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate
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wild-type at 37°C
0.0086
2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate
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mutant H232A
0.0101
2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate
-
wild-type at 25°C
0.028
2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate
-
mutant S86A at 25°C
0.118
2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate
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mutant D210A at 25°C
0.0083
5-enolpyruvoyl-6-hydroxy-2-succinyl-cyclohex-3-ene-1-carboxylate
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pH 7.0, 37°C
0.0086
5-enolpyruvoyl-6-hydroxy-2-succinyl-cyclohex-3-ene-1-carboxylate
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25°C, mutant enzyme H232A
0.0191
5-enolpyruvoyl-6-hydroxy-2-succinyl-cyclohex-3-ene-1-carboxylate
-
25°C, wild-type enzyme
0.028
5-enolpyruvoyl-6-hydroxy-2-succinyl-cyclohex-3-ene-1-carboxylate
-
25°C, mutant enzyme S86A
0.118
5-enolpyruvoyl-6-hydroxy-2-succinyl-cyclohex-3-ene-1-carboxylate
-
25°C, mutant enzyme D210A
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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
0.00058
(1R,2S,5S,6S)-2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate
-
H232A mutant protein
0.021
(1R,2S,5S,6S)-2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate
-
H232K mutant protein
0.047
(1R,2S,5S,6S)-2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate
-
R90A mutant protein
0.056
(1R,2S,5S,6S)-2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate
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W147A mutant protein
0.13
(1R,2S,5S,6S)-2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate
mutant V152A, pH 7.0, temperature not specified in the publication
0.13
(1R,2S,5S,6S)-2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate
mutant Y148A, pH 7.0, temperature not specified in the publication
0.18
(1R,2S,5S,6S)-2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate
-
D210A mutant protein
0.2
(1R,2S,5S,6S)-2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate
mutant V152G, pH 7.0, temperature not specified in the publication
0.29
(1R,2S,5S,6S)-2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate
-
S86A mutant protein
0.51
(1R,2S,5S,6S)-2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate
-
R124A mutant protein
0.58
(1R,2S,5S,6S)-2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate
mutant Y148F, pH 7.0, temperature not specified in the publication
2.58
(1R,2S,5S,6S)-2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate
-
Y85F mutant protein
2.9
(1R,2S,5S,6S)-2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate
-
R168A mutant protein
3.33
(1R,2S,5S,6S)-2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate
mutant F153A, pH 7.0, temperature not specified in the publication
8.5
(1R,2S,5S,6S)-2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate
wild-type, pH 7.0, temperature not specified in the publication
15.4
(1R,2S,5S,6S)-2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate
-
W147F mutant protein
41.5
(1R,2S,5S,6S)-2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate
-
K212A mutant protein
115
(1R,2S,5S,6S)-2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate
-
D128A mutant protein
147
(1R,2S,5S,6S)-2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate
-
wild-type protein
0.18
5-enolpyruvoyl-6-hydroxy-2-succinyl-cyclohex-3-ene-1-carboxylate
-
25°C, mutant enzyme D210A
0.29
5-enolpyruvoyl-6-hydroxy-2-succinyl-cyclohex-3-ene-1-carboxylate
-
25°C, mutant enzyme S86A
5.8
5-enolpyruvoyl-6-hydroxy-2-succinyl-cyclohex-3-ene-1-carboxylate
-
25°C, mutant enzyme H232A
147
5-enolpyruvoyl-6-hydroxy-2-succinyl-cyclohex-3-ene-1-carboxylate
-
25°C, wild-type enzyme
167
5-enolpyruvoyl-6-hydroxy-2-succinyl-cyclohex-3-ene-1-carboxylate
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pH 7.0, 37°C
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0.0392 - 14000
(1R,2S,5S,6S)-2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate
67 - 20000000
2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate
0.0392
(1R,2S,5S,6S)-2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate
-
H232K mutant protein
0.067
(1R,2S,5S,6S)-2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate
-
H232A mutant protein
0.295
(1R,2S,5S,6S)-2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate
-
R90A mutant protein
0.43
(1R,2S,5S,6S)-2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate
mutant V152A, pH 7.0, temperature not specified in the publication
1.2
(1R,2S,5S,6S)-2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate
mutant V152G, pH 7.0, temperature not specified in the publication
1.5
(1R,2S,5S,6S)-2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate
-
D210A mutant protein
2.4
(1R,2S,5S,6S)-2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate
-
W147A mutant protein
2.7
(1R,2S,5S,6S)-2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate
mutant Y148A, pH 7.0, temperature not specified in the publication
6.1
(1R,2S,5S,6S)-2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate
-
R124A mutant protein
10
(1R,2S,5S,6S)-2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate
-
S86A mutant protein
15
(1R,2S,5S,6S)-2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate
-
R168A mutant protein
16.3
(1R,2S,5S,6S)-2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate
mutant Y148F, pH 7.0, temperature not specified in the publication
48
(1R,2S,5S,6S)-2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate
mutant F153A, pH 7.0, temperature not specified in the publication
180
(1R,2S,5S,6S)-2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate
-
Y85F mutant protein
220
(1R,2S,5S,6S)-2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate
-
W147F mutant protein
533
(1R,2S,5S,6S)-2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate
wild-type, pH 7.0, temperature not specified in the publication
1400
(1R,2S,5S,6S)-2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate
-
D128A mutant protein
2200
(1R,2S,5S,6S)-2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate
-
K212A mutant protein
14000
(1R,2S,5S,6S)-2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate
-
wild-type protein
67
2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate
-
mutant H232A
1500
2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate
-
mutant D210A at 25°C
10000
2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate
-
mutant S86A at 25°C
14000000
2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate
-
wild-type at 25°C
20000000
2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate
-
wild-type at 37°C
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brenda
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UniProt
brenda
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brenda
-
SwissProt
brenda
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physiological function
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involved in menaquinone biosynthesis
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monomer
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-
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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
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
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
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D128A
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conserved among MenH proteins
F153A
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
-
conserved among MenH proteins
R124A
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conserved among MenH proteins
R168A
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conserved among MenH proteins
R90A
-
conserved among MenH proteins
V152A
residue involved in open-closed transition, mutation leads to large decrease in enzymatic activity
V152G
residue involved in open-closed transition, mutation leads to large decrease in enzymatic activity
W147A
-
conserved among MenH proteins
W147F
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conserved among MenH proteins
Y148A
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
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conserved among MenH proteins
D210A
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decreased activity
D210A
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kcat/Km is 9091fold lower than wild-type value
D210A
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part of the catalytically essential triad
H232A
-
decreased activity
H232A
-
kcat/Km is 208333fold lower than wild-type value
H232A
-
part of the catalytically essential triad
S86A
-
decreased activity
S86A
-
kcat/Km is 1498fold lower than wild-type value
S86A
-
part of the catalytically essential triad
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combination of Ni2+-affinity chromatography and size-exclusion chromatography
-
immobilized metal ion affinity chromatography, gel filtration
-
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expressed in Escherichia coli BL21(DE3)
-
expression in Escherichia coli
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Jiang, 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 activity
Biochemistry
46
10979-10989
2007
Escherichia coli K-12
brenda
Jiang, M.; Chen, X.; Guo, Z.F.; Cao, Y.; Chen, M.; Guo, Z.
Identification and characterization of (1R,6R)-2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase in the menaquinone biosynthesis of Escherichia coli
Biochemistry
47
3426-3434
2008
Escherichia coli
brenda
Jiang, M.; Chen, X.; Wu, X.H.; Chen, M.; Wu, Y.D.; Guo, Z.
Catalytic mechanism of SHCHC synthase in the menaquinone biosynthesis of Escherichia coli: identification and mutational analysis of the active site residues
Biochemistry
48
6921-6931
2009
Escherichia coli
brenda
Dawson, A.; Fyfe, P.; Gillet, F.; Hunter, W.
Exploiting the high-resolution crystal structure of Staphylococcus aureus MenH to gain insight into enzyme activity
BMC Struct. Biol.
11
19
2011
Staphylococcus aureus (A0A0H2WW38)
brenda
Sun, Y.; Yin, S.; Feng, Y.; Li, J.; Zhou, J.; Liu, C.; Zhu, G.; Guo, Z.
Molecular basis of the general base catalysis of an alpha/beta-hydrolase catalytic triad
J. Biol. Chem.
289
15867-15879
2014
Escherichia coli (P37355)
brenda
Johnston, J.M.; Jiang, M.; Guo, Z.; Baker, E.N.
Crystal structures of E. coli native MenH and two active site mutants
PLoS ONE
8
e61325
2013
Escherichia coli (P37355), Escherichia coli
brenda
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