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EC Tree
IUBMB Comments 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.
The taxonomic range for the selected organisms is: Escherichia coli The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
shchc synthase, 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexadiene-1-carboxylate synthase, ecmend, sephchc synthase, 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase,
more
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(1R,2S,5S,6S)-2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase
-
(1R,2S,5S,6S)-2-succinyl-5-enolpyruvyl-6-hydroxycyclohex-3-ene-1-carboxylate synthase
-
2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase
-
MenD
-
-
SEPHCHC synthase
-
-
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isochorismate + 2-oxoglutarate = 5-enolpyruvoyl-6-hydroxy-2-succinyl-cyclohex-3-ene-1-carboxylate + CO2
isochorismate + 2-oxoglutarate = 5-enolpyruvoyl-6-hydroxy-2-succinyl-cyclohex-3-ene-1-carboxylate + CO2
reaction follows a ping-pong bi-bi mechanism
-
isochorismate + 2-oxoglutarate = 5-enolpyruvoyl-6-hydroxy-2-succinyl-cyclohex-3-ene-1-carboxylate + CO2
proposed mechanism for formation of the tetrahedral intermediate in MenD catalysis. The strong interaction at the terminal carboxylate is proposed to restrict the rotation around C2-C2alpha so that no hydrogen bond is formed between C2alpha-OH and N4' of the cofactor throughout the reaction process. This disables the formation of the enamine intermediate and enables the formation of the tetrahedral intermediate. Modeling, overview
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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.
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(+)-5-(carboxymethoxy)-6-hydroxycyclohexa-2,4-diene-1-carboxylic acid + 2-oxoglutarate
? + CO2
-
analogue of isochorismate, weaker binding to enzyme. Only the (+)-enantiomer is a substrate
-
-
?
(5S,6S)-5,6-dihydroxycyclohexa-1,3-diene-1-carboxylate + 2-oxoglutarate
(1R,2S,5S,6S)-2-succinyl-5,6-dihydroxycyclohex-3-ene-1-carboxylate + CO2
-
-
-
?
(5S,6S)-6-amino-5-hydroxycyclohexa-1,3-diene-1-carboxylate + 2-oxoglutarate
2-succinyl-6-amino-5-hydroxycyclohex-3-ene-1-carboxylate + CO2
-
-
-
?
isochorismate + 2-oxoglutarate
5-enolpyruvoyl-6-hydroxy-2-succinyl-cyclohex-3-ene-1-carboxylate + CO2
isochorismate + 2-oxoglutarate
5-enolpyruvoyl-6-hydroxy-2-succinylcyclohex-3-ene-1-carboxylate + CO2
additional information
?
-
-
MenD participates in the menaquinone (vitamin K2) biosynthetic pathway
-
-
?
isochorismate + 2-oxoglutarate
5-enolpyruvoyl-6-hydroxy-2-succinyl-cyclohex-3-ene-1-carboxylate + CO2
-
-
-
?
isochorismate + 2-oxoglutarate
5-enolpyruvoyl-6-hydroxy-2-succinyl-cyclohex-3-ene-1-carboxylate + CO2
-
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
-
-
?
isochorismate + 2-oxoglutarate
5-enolpyruvoyl-6-hydroxy-2-succinyl-cyclohex-3-ene-1-carboxylate + CO2
-
under basic conditions, the product can spontaneously lose pyruvate to form (1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
-
-
?
isochorismate + 2-oxoglutarate
5-enolpyruvoyl-6-hydroxy-2-succinylcyclohex-3-ene-1-carboxylate + CO2
-
-
-
?
isochorismate + 2-oxoglutarate
5-enolpyruvoyl-6-hydroxy-2-succinylcyclohex-3-ene-1-carboxylate + CO2
via a tetrahedral enamine/acyl anion intermediate, overview
-
-
?
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isochorismate + 2-oxoglutarate
5-enolpyruvoyl-6-hydroxy-2-succinyl-cyclohex-3-ene-1-carboxylate + CO2
isochorismate + 2-oxoglutarate
5-enolpyruvoyl-6-hydroxy-2-succinylcyclohex-3-ene-1-carboxylate + CO2
-
-
-
?
additional information
?
-
-
MenD participates in the menaquinone (vitamin K2) biosynthetic pathway
-
-
?
isochorismate + 2-oxoglutarate
5-enolpyruvoyl-6-hydroxy-2-succinyl-cyclohex-3-ene-1-carboxylate + CO2
-
-
-
?
isochorismate + 2-oxoglutarate
5-enolpyruvoyl-6-hydroxy-2-succinyl-cyclohex-3-ene-1-carboxylate + CO2
-
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
-
-
?
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thiamine diphosphate
-
thiamine diphosphate
-
Km value 0.008 mM
thiamine diphosphate
ThDP-dependent enzyme
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Mg2+
required
Mg2+
-
required, Km: 0.08 mM
Mg2+
5 mM used in assay conditions
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4-[hydroxy(methoxy)phosphoryl]-4-oxobutanoic acid
-
competitive with respect to 2-oxoglutarate, uncompetitive with respect to (+)-5-(carboxymethoxy)-6-hydroxycyclohexa-2,4-diene-1-carboxylic acid. Compound is proposed to bind to the active site and react with thiamine diphosphate but not proceed forward to products by cleavage of the C-P bond
methyl succinylphosphonate
-
dead-end inhibitor
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thiamine diphosphate
-
required, Km: 0.0024 mM
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0.0042 - 0.109
(+)-5-(carboxymethoxy)-6-hydroxycyclohexa-2,4-diene-1-carboxylic acid
0.0026 - 1.5
2-oxoglutarate
0.00008 - 0.053
isochorismate
0.0042
(+)-5-(carboxymethoxy)-6-hydroxycyclohexa-2,4-diene-1-carboxylic acid
-
mutant R293K, pH 7.4, temperature not specified in the publication
0.01
(+)-5-(carboxymethoxy)-6-hydroxycyclohexa-2,4-diene-1-carboxylic acid
-
mutant R413K, pH 7.4, temperature not specified in the publication
0.012
(+)-5-(carboxymethoxy)-6-hydroxycyclohexa-2,4-diene-1-carboxylic acid
-
wild-type, pH 7.4, temperature not specified in the publication
0.027
(+)-5-(carboxymethoxy)-6-hydroxycyclohexa-2,4-diene-1-carboxylic acid
-
mutant I418L, pH 7.4, temperature not specified in the publication
0.036
(+)-5-(carboxymethoxy)-6-hydroxycyclohexa-2,4-diene-1-carboxylic acid
-
mutant S391A, pH 7.4, temperature not specified in the publication
0.042
(+)-5-(carboxymethoxy)-6-hydroxycyclohexa-2,4-diene-1-carboxylic acid
-
mutant S32A, pH 7.4, temperature not specified in the publication
0.05
(+)-5-(carboxymethoxy)-6-hydroxycyclohexa-2,4-diene-1-carboxylic acid
-
mutant R292Q, pH 7.4, temperature not specified in the publication
0.091
(+)-5-(carboxymethoxy)-6-hydroxycyclohexa-2,4-diene-1-carboxylic acid
-
mutant R107K, pH 7.4, temperature not specified in the publication
0.109
(+)-5-(carboxymethoxy)-6-hydroxycyclohexa-2,4-diene-1-carboxylic acid
-
mutant R395K, pH 7.4, temperature not specified in the publication
0.0026
2-oxoglutarate
-
mutant K292Q, pH 7.4, temperature not specified in the publication
0.0029
2-oxoglutarate
wild type enzyme, at pH 7.0 and 21°C
0.0053
2-oxoglutarate
-
mutant R107K, pH 7.4, temperature not specified in the publication
0.0091
2-oxoglutarate
-
mutant R293K, pH 7.4, temperature not specified in the publication
0.0099
2-oxoglutarate
-
wild-type, pH 7.4, temperature not specified in the publication
0.0099
2-oxoglutarate
-
mutant S32A, pH 7.4, temperature not specified in the publication
0.012
2-oxoglutarate
-
mutant E55D, pH 7.4, temperature not specified in the publication
0.013
2-oxoglutarate
-
mutant S391A, pH 7.4, temperature not specified in the publication
0.029
2-oxoglutarate
mutant enzyme R395A, at pH 7.0 and 21°C
0.045
2-oxoglutarate
-
mutant R395K, pH 7.4, temperature not specified in the publication
0.067
2-oxoglutarate
mutant enzyme R395K, at pH 7.0 and 21°C
0.115
2-oxoglutarate
mutant enzyme R413K, at pH 7.0 and 21°C
0.172
2-oxoglutarate
mutant enzyme R395K/R413K, at pH 7.0 and 21°C
0.2
2-oxoglutarate
-
mutant I418L, pH 7.4, temperature not specified in the publication
0.22
2-oxoglutarate
-
mutant R413K, pH 7.4, temperature not specified in the publication
1.5
2-oxoglutarate
-
pH 7.8, 22°C
0.00008
isochorismate
wild type enzyme, at pH 7.0 and 21°C
0.00035
isochorismate
mutant enzyme R413K, at pH 7.0 and 21°C
0.00082
isochorismate
mutant enzyme R395K/R413K, at pH 7.0 and 21°C
0.0022
isochorismate
mutant enzyme R395K, at pH 7.0 and 21°C
0.016
isochorismate
mutant enzyme R395A, at pH 7.0 and 21°C
0.053
isochorismate
-
pH 7.8, 22°C
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0.12 - 0.4
(+)-5-(carboxymethoxy)-6-hydroxycyclohexa-2,4-diene-1-carboxylic acid
0.0027 - 0.3
2-oxoglutarate
0.0025 - 0.337
isochorismate
0.12
(+)-5-(carboxymethoxy)-6-hydroxycyclohexa-2,4-diene-1-carboxylic acid
-
mutant R107K, pH 7.4, temperature not specified in the publication
0.18
(+)-5-(carboxymethoxy)-6-hydroxycyclohexa-2,4-diene-1-carboxylic acid
-
mutant R395K, pH 7.4, temperature not specified in the publication
0.22
(+)-5-(carboxymethoxy)-6-hydroxycyclohexa-2,4-diene-1-carboxylic acid
-
mutant S391A, pH 7.4, temperature not specified in the publication
0.25
(+)-5-(carboxymethoxy)-6-hydroxycyclohexa-2,4-diene-1-carboxylic acid
-
mutant S32A, pH 7.4, temperature not specified in the publication
0.28
(+)-5-(carboxymethoxy)-6-hydroxycyclohexa-2,4-diene-1-carboxylic acid
-
mutant K292Q, pH 7.4, temperature not specified in the publication
0.38
(+)-5-(carboxymethoxy)-6-hydroxycyclohexa-2,4-diene-1-carboxylic acid
-
mutant I418L, pH 7.4, temperature not specified in the publication
0.4
(+)-5-(carboxymethoxy)-6-hydroxycyclohexa-2,4-diene-1-carboxylic acid
-
wild-type, pH 7.4, temperature not specified in the publication
0.4
(+)-5-(carboxymethoxy)-6-hydroxycyclohexa-2,4-diene-1-carboxylic acid
-
mutant R293K, pH 7.4, temperature not specified in the publication
0.0027
2-oxoglutarate
mutant enzyme R395K/R413K, at pH 7.0 and 21°C
0.018
2-oxoglutarate
mutant enzyme R395A, at pH 7.0 and 21°C
0.043
2-oxoglutarate
mutant enzyme R413K, at pH 7.0 and 21°C
0.075
2-oxoglutarate
-
pH 7.8, 22°C
0.1
2-oxoglutarate
-
mutant R413K, pH 7.4, temperature not specified in the publication
0.13
2-oxoglutarate
-
mutant R395K, pH 7.4, temperature not specified in the publication
0.143
2-oxoglutarate
mutant enzyme R395K, at pH 7.0 and 21°C
0.17
2-oxoglutarate
-
mutant R107K, pH 7.4, temperature not specified in the publication
0.2
2-oxoglutarate
-
mutant K292Q, pH 7.4, temperature not specified in the publication
0.22
2-oxoglutarate
-
mutant I418L, pH 7.4, temperature not specified in the publication
0.23
2-oxoglutarate
-
mutant S32A, pH 7.4, temperature not specified in the publication
0.28
2-oxoglutarate
-
wild-type, pH 7.4, temperature not specified in the publication
0.287
2-oxoglutarate
wild type enzyme, at pH 7.0 and 21°C
0.3
2-oxoglutarate
-
mutant R293K, pH 7.4, temperature not specified in the publication
0.3
2-oxoglutarate
-
mutant S391A, pH 7.4, temperature not specified in the publication
0.0025
isochorismate
mutant enzyme R395K/R413K, at pH 7.0 and 21°C
0.038
isochorismate
mutant enzyme R413K, at pH 7.0 and 21°C
0.05
isochorismate
-
pH 7.8, 22°C
0.065
isochorismate
mutant enzyme R395A, at pH 7.0 and 21°C
0.135
isochorismate
mutant enzyme R395K, at pH 7.0 and 21°C
0.337
isochorismate
wild type enzyme, at pH 7.0 and 21°C
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1 - 1417
(+)-5-(carboxymethoxy)-6-hydroxycyclohexa-2,4-diene-1-carboxylic acid
0.016 - 98.3
2-oxoglutarate
1
(+)-5-(carboxymethoxy)-6-hydroxycyclohexa-2,4-diene-1-carboxylic acid
-
mutant R107K, pH 7.4, temperature not specified in the publication
2
(+)-5-(carboxymethoxy)-6-hydroxycyclohexa-2,4-diene-1-carboxylic acid
-
mutant R395K, pH 7.4, temperature not specified in the publication
6
(+)-5-(carboxymethoxy)-6-hydroxycyclohexa-2,4-diene-1-carboxylic acid
-
mutant K292Q, pH 7.4, temperature not specified in the publication
6
(+)-5-(carboxymethoxy)-6-hydroxycyclohexa-2,4-diene-1-carboxylic acid
-
mutant S32A, pH 7.4, temperature not specified in the publication
6
(+)-5-(carboxymethoxy)-6-hydroxycyclohexa-2,4-diene-1-carboxylic acid
-
mutant S391A, pH 7.4, temperature not specified in the publication
33
(+)-5-(carboxymethoxy)-6-hydroxycyclohexa-2,4-diene-1-carboxylic acid
-
wild-type, pH 7.4, temperature not specified in the publication
95
(+)-5-(carboxymethoxy)-6-hydroxycyclohexa-2,4-diene-1-carboxylic acid
-
mutant R293K, pH 7.4, temperature not specified in the publication
1417
(+)-5-(carboxymethoxy)-6-hydroxycyclohexa-2,4-diene-1-carboxylic acid
-
mutant I418L, pH 7.4, temperature not specified in the publication
0.016
2-oxoglutarate
mutant enzyme R395K/R413K, at pH 7.0 and 21°C
0.28
2-oxoglutarate
-
wild-type, pH 7.4, temperature not specified in the publication
0.37
2-oxoglutarate
mutant enzyme R413K, at pH 7.0 and 21°C
0.62
2-oxoglutarate
mutant enzyme R395A, at pH 7.0 and 21°C
1
2-oxoglutarate
-
mutant I418L, pH 7.4, temperature not specified in the publication
2.2
2-oxoglutarate
mutant enzyme R395K, at pH 7.0 and 21°C
3
2-oxoglutarate
-
mutant R395K, pH 7.4, temperature not specified in the publication
18
2-oxoglutarate
-
mutant E55D, pH 7.4, temperature not specified in the publication
23
2-oxoglutarate
-
mutant S32A, pH 7.4, temperature not specified in the publication
23
2-oxoglutarate
-
mutant S391A, pH 7.4, temperature not specified in the publication
28
2-oxoglutarate
-
wild-type, pH 7.4, temperature not specified in the publication
32
2-oxoglutarate
-
mutant R107K, pH 7.4, temperature not specified in the publication
33
2-oxoglutarate
-
mutant R293K, pH 7.4, temperature not specified in the publication
77
2-oxoglutarate
-
mutant K292Q, pH 7.4, temperature not specified in the publication
98.3
2-oxoglutarate
wild type enzyme, at pH 7.0 and 21°C
0.3
isochorismate
mutant enzyme R395K/R413K, at pH 7.0 and 21°C
4
isochorismate
mutant enzyme R395A, at pH 7.0 and 21°C
6.2
isochorismate
mutant enzyme R395K, at pH 7.0 and 21°C
110
isochorismate
mutant enzyme R413K, at pH 7.0 and 21°C
400
isochorismate
wild type enzyme, at pH 7.0 and 21°C
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0.00013
4-[hydroxy(methoxy)phosphoryl]-4-oxobutanoic acid
-
pH 7.4, temperature not specified in the publication
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-
UniProt
brenda
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evolution
the enzyme Men D is not significantly different from other ThDP-dependent enzymes in active-site architecture, cofactor binding, or overall three-dimensional structure, suggesting the use of the canonical enamine intermediate in its catalysis
physiological function
-
enzyme is essential for menaquinone biosynthesis
additional information
in the covalent tetrahedral enamine intermediate, all of the bond lengths and angles of its planar thiazolium ring are comparable to those of a similar enzyme-free thiamine diphosphate adduct, complex crystal structure determination and analysis, NMR structure analysis and modeling, overview
metabolism
MenD is a thiamine diphosphate-dependent enzyme that catalyzes a distinctive Stetterlike 1,4-addition reaction in bacterial biosynthesis of vitamin K2
metabolism
the enzyme catalyzes an essential Stetter reaction in menaquinone (vitamin K2) biosynthesis via thiamine diphosphate (ThDP)-bound tetrahedral postdecarboxylation intermediates
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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 A
-
mutant enzyme R395K bound to thiamine diphosphate, hanging drop vapor diffusion method, using 0.2 M ammonium acetate, 0.06 M magnesium formate, 3% (w/v) polyethylene glycol 3350, and 12% (w/v) polyethylene glycol 10000 in 0.1 M Tris-HCl (pH 7.5). Mutant enzyme R395A bound to thiamine diphosphate, hanging drop vapor diffusion method, using 30% (v/v) Jeffamine M-600 (pH 7.0), 11.2% (w/v) polyethylene glycol 3350 and 0.16 M magnesium formate in 0.1 M HEPES (pH 7.5). Mutant enzyme R413A bound to thiamine diphosphate, hanging drop vapor diffusion method, using 0.16 M magnesium formate, 1% (w/v) tacsimate (pH 7.0), 14% (w/v) polyethylene glycol 3350, and 2% (w/v) polyethylene glycol MME 5000 in 0.02 M HEPES (pH 7.0)
purified recombinant enzyme complexed with its tetrahedral reaction intermediate, X-ray diffraction structure determination and analysis
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E55D
-
about 30% decrease in catalytic efficiency
I148L
-
strong decrease in catalytic efficiency
K292Q
-
150% increase in catalytic efficiency
N117R/L478T
the mutant preferentially converts (5S,6S)-5,6-dihydroxycyclohexa-1,3-diene-1-carboxylate with a more than 70fold higher ratio than that for the wild type enzyme
Q118A
the mutant is completely inactive
R107I
the mutant uses (5S,6S)-6-amino-5-hydroxycyclohexa-1,3-diene-1-carboxylate as substrate with more than 6fold conversion compared to the wild type enzyme
R107K
-
no decrease in catalytic efficiency
R293K
-
slight increase in catalytic efficiency
R395A
the mutant shows a 160 and 1000fold decrease in kcat/Km value with respect to 2-oxoglutarate and isochorismate, respectively, compared to the wild type enzyme
R395K/R413K
the mutant shows a 6300 and 1300fold decrease in kcat/Km value with respect to 2-oxoglutarate and isochorismate, respectively, compared to the wild type enzyme
R413A
the mutant is completely inactive
S32A
-
slight decrease in catalytic efficiency
S391A
-
slight decrease in catalytic efficiency
R395K
-
90% decrease in catalytic efficiency
R395K
the mutant shows a 45 and 66fold decrease in kcat/Km value with respect to 2-oxoglutarate and isochorismate, respectively, compared to the wild type enzyme
R413K
-
strong decrease in catalytic efficiency
R413K
the mutant shows a 270 and 37fold decrease in kcat/Km value with respect to 2-oxoglutarate and isochorismate, respectively, compared to the wild type enzyme
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DEAE column chromatography and Sephacryl S-200 gel filtration
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expressed in Escherichia coli BL21(DE3) cells
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Sieminska, 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 coli
Acta Crystallogr. Sect. F
61
489-492
2005
Escherichia coli
brenda
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
brenda
Fang, M.; Macova, A.; Hanson, K.L.; Kos, J.; Palmer, D.R.
Using substrate analogues to probe the kinetic mechanism and active site of Escherichia coli MenD
Biochemistry
50
8712-8721
2011
Escherichia coli, Mycobacterium tuberculosis
brenda
Song, H.; Dong, C.; Qin, M.; Chen, Y.; Sun, Y.; Liu, J.; Chan, W.; Guo, Z.
A thiamine-dependent enzyme utilizes an active tetrahedral intermediate in vitamin K biosynthesis
J. Am. Chem. Soc.
138
7244-7247
2016
Escherichia coli (P17109)
brenda
Qin, M.; Song, H.; Dai, X.; Chen, Y.; Guo, Z.
Two active site arginines are critical determinants of substrate binding and catalysis in MenD a thiamine-dependent enzyme in menaquinone biosynthesis
Biochem. J.
475
3651-3667
2018
Escherichia coli (P17109)
brenda
Fries, A.; Mazzaferro, L.S.; Gruening, B.; Bisel, P.; Stibal, K.; Buchholz, P.C.F.; Pleiss, J.; Sprenger, G.A.; Mueller, M.
Alteration of the route to menaquinone towards isochorismate-derived metabolites
ChemBioChem
20
1672-1677
2019
Escherichia coli (P17109)
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