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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
-
-
-
?
2,3-dihydroxybenzaldehyde + 2-oxoglutarate
(5R)-5-(2,3-dihydroxyphenyl)-5-hydroxy-4-oxopentanoic acid + CO2
-
assay at pH 8
-
-
?
2-bromobenzaldehyde + 2-oxoglutarate
(5R)-5-(2-bromophenyl)-5-hydroxy-4-oxopentanoic acid + CO2
-
assay at pH 8
-
-
?
2-chlorobenzaldehyde + 2-oxoglutarate
(5R)-5-(2-chlorophenyl)-5-hydroxy-4-oxopentanoic acid + CO2
-
assay at pH 8
-
-
?
2-fluorobenzaldehyde + 2-oxoglutarate
(5R)-5-(2-fluorophenyl)-5-hydroxy-4-oxopentanoic acid + CO2
-
assay at pH 8
-
-
?
2-fluorobenzaldehyde + oxaloacetate
(1R)-1-(2-fluorophenyl)-1-hydroxypropan-2-one + 2 CO2
-
assay at pH 8
-
-
?
2-fluorobenzaldehyde + pyruvate
(1R)-1-(2-fluorophenyl)-1-hydroxypropan-2-one + CO2
-
assay at pH 8
-
-
?
2-iodobenzaldehyde + 2-oxoglutarate
(5R)-5-hydroxy-5-(2-iodophenyl)-4-oxopentanoic acid + CO2
-
assay at pH 8
-
-
?
2-methylbenzaldehyde + 2-oxoglutarate
(5R)-5-hydroxy-5-(2-methylphenyl)-4-oxopentanoic acid + CO2
-
assay at pH 8
-
-
?
3,4-dihydroxybenzaldehyde + 2-oxoglutarate
(5R)-5-(3,4-dihydroxyphenyl)-5-hydroxy-4-oxopentanoic acid + CO2
-
assay at pH 8
-
-
?
3-fluorobenzaldehyde + 2-oxoglutarate
(5R)-5-(3-fluorophenyl)-5-hydroxy-4-oxopentanoic acid + CO2
-
assay at pH 8
-
-
?
3-iodobenzaldehyde + 2-oxoglutarate
(5R)-5-hydroxy-5-(3-iodophenyl)-4-oxopentanoic acid + CO2
-
assay at pH 8
-
-
?
3-methoxybenzaldehyde + 2-oxoglutarate
(5R)-5-hydroxy-5-(3-methoxyphenyl)-4-oxopentanoic acid + CO2
-
assay at pH 8
-
-
?
4-chlorbenzaldehyde + 2-oxoglutarate
(5R)-5-(4-chlorophenyl)-5-hydroxy-4-oxopentanoic acid + CO2
-
assay at pH 8
-
-
?
4-fluorobenzaldehyde + 2-oxoglutarate
(5R)-5-(4-fluorophenyl)-5-hydroxy-4-oxopentanoic acid + CO2
-
assay at pH 8
-
-
?
4-hydroxybenzaldehyde + 2-oxoglutarate
(5R)-5-hydroxy-5-(4-hydroxyphenyl)-4-oxopentanoic acid + CO2
-
assay at pH 8
-
-
?
acetaldehyde + 2-oxoglutarate
(5R)-5-hydroxy-4-oxohexanoic acid + CO2
-
assay at pH 8
-
-
?
benzaldehyde + 2-oxoglutarate
(5R)-5-hydroxy-4-oxo-5-phenylpentanoic acid + CO2
-
assay at pH 8
-
-
?
benzaldehyde + oxaloacetate
(1R)-1-hydroxy-1-phenylpropan-2-one + 2 CO2
-
assay at pH 8
-
-
?
benzaldehyde + pyruvate
(1R)-1-hydroxy-1-phenylpropan-2-one + 2 CO2
-
assay at pH 8
-
-
?
cyclohex-1-ene-1-carbaldehyde + 2-oxoglutarate
(5R)-5-cyclohex-1-en-1-yl-5-hydroxy-4-oxopentanoic acid + CO2
-
assay at pH 8
-
-
?
glyoxylate + 2-oxoglutarate
5-hydroxy-4-oxopentanoic acid + 2 CO2
-
assay at pH 8
-
-
?
hexanal + 2-oxoglutarate
(5R)-5-hydroxy-4-oxodecanoic acid + CO2
-
assay at pH 8
-
-
?
isochorismate + 2-oxoglutarate
(1R,2S,5S,6S)-5-[(1-carboxyethenyl)oxy]-2-(3-carboxypropanoyl)-6-hydroxycyclohex-3-ene-1-carboxylic acid + 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
pyruvate + 2-oxoglutarate
4-hydroxy-5-oxohexanoic acid + 2 CO2
-
assay at pH 8
-
-
?
undec-10-enal + 2-oxoglutarate
(5R)-5-hydroxy-4-oxopentadec-14-enoic acid + CO2
-
assay at pH 8
-
-
?
additional information
?
-
-
MenD participates in the menaquinone (vitamin K2) biosynthetic pathway
-
-
?
isochorismate + 2-oxoglutarate
(1R,2S,5S,6S)-5-[(1-carboxyethenyl)oxy]-2-(3-carboxypropanoyl)-6-hydroxycyclohex-3-ene-1-carboxylic acid + CO2
-
assay at pH 8
-
-
?
isochorismate + 2-oxoglutarate
(1R,2S,5S,6S)-5-[(1-carboxyethenyl)oxy]-2-(3-carboxypropanoyl)-6-hydroxycyclohex-3-ene-1-carboxylic acid + CO2
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
?
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-succinyl-cyclohex-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-succinyl-cyclohex-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
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
isochorismate + 2-oxoglutarate
5-enolpyruvoyl-6-hydroxy-2-succinyl-cyclohex-3-ene-1-carboxylate + CO2
-
-
-
?
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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
0.0077
2-oxoglutarate
mutant R106A, pH 7.8, 23°C
0.0091
2-oxoglutarate
-
mutant R293K, pH 7.4, temperature not specified in the publication
0.0099
2-oxoglutarate
-
wild-type, pH 7.4, 25°C
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, 25°C
0.013
2-oxoglutarate
-
mutant S391A, pH 7.4, temperature not specified in the publication
0.018
2-oxoglutarate
mutant L493A, pH 7.8, 23°C
0.022
2-oxoglutarate
mutant K299A, pH 7.8, 23°C
0.022
2-oxoglutarate
mutant R32A, pH 7.8, 23°C
0.022
2-oxoglutarate
wild-type, pH 7.8, 23°C
0.029
2-oxoglutarate
mutant enzyme R395A, at pH 7.0 and 21°C
0.045
2-oxoglutarate
-
mutant R395K, pH 7.4, 25°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
0.159
2-oxoglutarate
mutant R409A, pH 7.8, 23°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
0.274
2-oxoglutarate
mutant F490A, pH 7.8, 23°C
0.346
2-oxoglutarate
mutant I489A, pH 7.8, 23°C
0.514
2-oxoglutarate
mutant R428A, pH 7.8, 23°C
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
0.0053
isochorismate
-
mutant R395K, pH 7.4, 25°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 - 0.37
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
0.01
2-oxoglutarate
mutant R106A, pH 7.8, 23°C
0.018
2-oxoglutarate
mutant enzyme R395A, at pH 7.0 and 21°C
0.02
2-oxoglutarate
mutant F490A, pH 7.8, 23°C
0.043
2-oxoglutarate
mutant enzyme R413K, at pH 7.0 and 21°C
0.05
2-oxoglutarate
mutant R409A, pH 7.8, 23°C
0.06
2-oxoglutarate
mutant R428A, pH 7.8, 23°C
0.075
2-oxoglutarate
-
pH 7.8, 22°C
0.08
2-oxoglutarate
mutant R32A, pH 7.8, 23°C
0.1
2-oxoglutarate
mutant I489A, pH 7.8, 23°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
0.145
2-oxoglutarate
-
mutant R395K, pH 7.4, 25°C
0.17
2-oxoglutarate
mutant L493A, pH 7.8, 23°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
0.23
2-oxoglutarate
wild-type, pH 7.8, 23°C
0.28
2-oxoglutarate
-
wild-type, pH 7.4, 25°C
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, 25°C
0.3
2-oxoglutarate
-
mutant S391A, pH 7.4, temperature not specified in the publication
0.37
2-oxoglutarate
mutant K299A, pH 7.8, 23°C
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
0.07
2-oxoglutarate
mutant F490A, pH 7.8, 23°C
0.12
2-oxoglutarate
mutant R428A, pH 7.8, 23°C
0.27
2-oxoglutarate
mutant I489A, pH 7.8, 23°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
1.5
2-oxoglutarate
mutant R106A, pH 7.8, 23°C
2.2
2-oxoglutarate
mutant enzyme R395K, at pH 7.0 and 21°C
2.7
2-oxoglutarate
mutant R409A, pH 7.8, 23°C
3
2-oxoglutarate
-
mutant R395K, pH 7.4, temperature not specified in the publication
3.7
2-oxoglutarate
mutant R32A, pH 7.8, 23°C
8.3
2-oxoglutarate
mutant L493A, pH 7.8, 23°C
10.7
2-oxoglutarate
wild-type, pH 7.8, 23°C
16.7
2-oxoglutarate
mutant K299A, pH 7.8, 23°C
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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to 2.35 A resolution, in complex with thiamine diphosphate and Mn2+. basic residues Arg32, Arg106, Arg409, Arg428, and Lys299 interact with carboxylate and hydroxyl groups to align substrates for catalysis in combination with a cluster of the non-polar residues Ile489, Phe490, and Leu493 on one side of the active site. Arg409 plays a significant role in binding both substrates while Arg428 contributes mainly to binding of 2-oxoglutarate. Arg32 and in particular Arg106 are critical for recognition of isochorismate
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
sitting and hanging vapor diffusion method, hexagonal complex with thiamine diphosphate and Mn2+
apoenzyme and in complex with thiamine diphosphate and Mg2+, sitting drop vapor diffusion method
sitting drop vapor diffusion method, using 0.1 M MOPS/HEPES, pH 7.5, 20% (v/v) glycerol, 8% (w/v) PEG 4000, and a 0.02 M mixture of sodium formate, ammonium acetate, sodium citrate tribasic dihydrate, sodium oxamate, and potassium sodium tartrate tetrahydrate
-
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F490A
0.6% of wild-type activity
I489A
1% of wild-type activity
K299A
150% of wild-type activity
L493A
80% of wild-type activity
R106A
mutation in the second subunit forming the active site, 10% of wild-type activity
R32A
mutation in the second subunit forming the active site, 30% of wild-type activity
R409A
3% of wild-type activity
R428A
1% of wild-type activity
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
R277A
-
the mutant has 18% of the wild type enzyme activity
R303A
-
the mutant has 56% of the wild type enzyme activity
R395K
-
4fold increase in Km value, 50% decrease in kcat value
R97A
-
the mutant has 50% of the wild type enzyme activity
S391A
-
minor effect on activity
R277A
-
the mutant has 18% of the wild type enzyme activity
-
R303A
-
the mutant has 56% of the wild type enzyme activity
-
R97A
-
the mutant has 50% of the wild type enzyme activity
-
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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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
Priyadarshi, 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 affinity
Biochem. Biophys. Res. Commun.
380
797-801
2009
Escherichia coli K-12 (P17109)
brenda
Dawson, 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.
384
1353-1368
2008
Escherichia coli K-12 (P17109)
brenda
Kurutsch, A.; Richter, M.; Brecht, V.; Sprenger, G.; Mller, M.
MenD as a versatile catalyst for asymmetric synthesis
J. Mol. Catal. B
61
56-66
2009
Escherichia coli K-12
-
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
Dawson, A.; Chen, M.; Fyfe, P.K.; Guo, Z.; Hunter, W.N.
Structure and reactivity of Bacillus subtilis MenD catalyzing the first committed step in menaquinone biosynthesis
J. Mol. Biol.
401
253-264
2010
Bacillus subtilis (P23970), Bacillus subtilis
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)
brenda
Bashiri, G.; Nigon, L.V.; Jirgis, E.N.M.; Ho, N.A.T.; Stanborough, T.; Dawes, S.S.; Baker, E.N.; Bulloch, E.M.M.; Johnston, J.M.
Allosteric regulation of menaquinone (vitamin K2) biosynthesis in the human pathogen Mycobacterium tuberculosis
J. Biol. Chem.
295
3759-3770
2020
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
brenda
Xu, J.; Yan, W.; Zhang, W.
Enhancing menaquinone-7 production in recombinant Bacillus amyloliquefaciens by metabolic pathway engineering
RSC Adv.
7
28527-28534
2017
Bacillus amyloliquefaciens, Bacillus amyloliquefaciens W-21
-
brenda
Jirgis, E.N.; Bashiri, G.; Bulloch, E.M.; Johnston, J.M.; Baker, E.N.
Structural views along the Mycobacterium tuberculosis MenD reaction pathway illuminate key aspects of thiamin diphosphate-dependent enzyme mechanisms
Structure
24
1167-1177
2016
Mycobacterium tuberculosis (P9WK11), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WK11)
brenda