Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(1R,6R)-2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate
4-(2-carboxyphenyl)-4-oxobutanoic acid + H2O
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
2-succinylbenzoate + H2O
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylic acid
4-(2-carboxyphenyl)-4-oxobutyrate + H2O
additional information
?
-
(1R,6R)-2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate
4-(2-carboxyphenyl)-4-oxobutanoic acid + H2O
-
-
-
-
?
(1R,6R)-2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate
4-(2-carboxyphenyl)-4-oxobutanoic acid + H2O
-
reaction in menaquinone biosynthetic pathway
-
-
?
(1R,6R)-2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate
4-(2-carboxyphenyl)-4-oxobutanoic acid + H2O
-
menaquinone pathway
-
-
?
(1R,6R)-2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate
4-(2-carboxyphenyl)-4-oxobutanoic acid + H2O
-
menaquinone pathway, presence in species lacking the menaquinone pathway suggests additional roles in amino acid racemization
-
-
?
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
2-succinylbenzoate + H2O
-
-
-
?
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
2-succinylbenzoate + H2O
-
-
-
?
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
2-succinylbenzoate + H2O
-
-
-
?
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
2-succinylbenzoate + H2O
-
-
-
-
?
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
2-succinylbenzoate + H2O
-
-
-
?
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
2-succinylbenzoate + H2O
-
-
-
-
?
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
2-succinylbenzoate + H2O
-
-
-
-
?
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
2-succinylbenzoate + H2O
-
-
-
-
?
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
2-succinylbenzoate + H2O
-
-
-
?
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
2-succinylbenzoate + H2O
the enzyme converts 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate (SHCHC) to 4-(2'-carboxyphenyl)-4-oxobutyrate via an elimination of water. The reaction likely proceeds by a mechanism similar to those employed by other members of the enolase superfamily with initial abstraction of the R-proton of the carboxylic acid and stabilization of the resulting enolic intermediate
-
-
?
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
2-succinylbenzoate + H2O
-
-
-
?
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
2-succinylbenzoate + H2O
the enzyme converts 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate (SHCHC) to 4-(2'-carboxyphenyl)-4-oxobutyrate via an elimination of water. The reaction likely proceeds by a mechanism similar to those employed by other members of the enolase superfamily with initial abstraction of the R-proton of the carboxylic acid and stabilization of the resulting enolic intermediate
-
-
?
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
2-succinylbenzoate + H2O
-
-
-
-
?
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
2-succinylbenzoate + H2O
-
-
-
?
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylic acid
4-(2-carboxyphenyl)-4-oxobutyrate + H2O
-
-
?
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylic acid
4-(2-carboxyphenyl)-4-oxobutyrate + H2O
-
-
?
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylic acid
4-(2-carboxyphenyl)-4-oxobutyrate + H2O
-
-
ir
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylic acid
4-(2-carboxyphenyl)-4-oxobutyrate + H2O
-
-
ir
additional information
?
-
-
the enzyme also shows N-acylamino acid racemase activity, with the optimal substrate being the enantiomers of N-acetyl methionine
-
-
?
additional information
?
-
the enzyme catalyzes not only the dehydration of (1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate but also catalyzes racemization of different acylamino acids, with N-succinyl-R-phenylglycine being the best substrate, molecular mechanisms for both reactions exploring the potential energy surface, and molecular dynamics simulations to obtain the free energy profiles and the averaged interaction energies of enzymatic residues with the reacting system, overview
-
-
?
additional information
?
-
involved in the menaquinone biosynthetic pathway
-
?
additional information
?
-
-
involved in the menaquinone biosynthetic pathway
-
?
additional information
?
-
involved in the menaquinone biosynthetic pathway
-
?
additional information
?
-
-
involved in the menaquinone biosynthetic pathway
-
?
additional information
?
-
-
the enzyme from Exiguobacterium sp. also shows N-succinylamino acid racemization activity, efficiency for the reaction is 0.041 mM/s. But the o-succinylbenzoate synthase activity is the only biologically relevant activity. Modeling of substrate and product binding, active site docking, overview
-
-
?
additional information
?
-
-
the enzyme from Exiguobacterium sp. also shows N-succinylamino acid racemization activity, efficiency for the reaction is 0.041 mM/s. But the o-succinylbenzoate synthase activity is the only biologically relevant activity. Modeling of substrate and product binding, active site docking, overview
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(1R,6R)-2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate
4-(2-carboxyphenyl)-4-oxobutanoic acid + H2O
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
2-succinylbenzoate + H2O
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylic acid
4-(2-carboxyphenyl)-4-oxobutyrate + H2O
additional information
?
-
(1R,6R)-2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate
4-(2-carboxyphenyl)-4-oxobutanoic acid + H2O
-
reaction in menaquinone biosynthetic pathway
-
-
?
(1R,6R)-2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate
4-(2-carboxyphenyl)-4-oxobutanoic acid + H2O
-
menaquinone pathway
-
-
?
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
2-succinylbenzoate + H2O
-
-
-
?
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
2-succinylbenzoate + H2O
-
-
-
?
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
2-succinylbenzoate + H2O
-
-
-
?
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
2-succinylbenzoate + H2O
-
-
-
-
?
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
2-succinylbenzoate + H2O
-
-
-
?
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
2-succinylbenzoate + H2O
-
-
-
-
?
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
2-succinylbenzoate + H2O
-
-
-
-
?
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
2-succinylbenzoate + H2O
-
-
-
-
?
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
2-succinylbenzoate + H2O
-
-
-
?
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
2-succinylbenzoate + H2O
-
-
-
?
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
2-succinylbenzoate + H2O
-
-
-
-
?
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
2-succinylbenzoate + H2O
-
-
-
?
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylic acid
4-(2-carboxyphenyl)-4-oxobutyrate + H2O
-
-
ir
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylic acid
4-(2-carboxyphenyl)-4-oxobutyrate + H2O
-
-
ir
additional information
?
-
involved in the menaquinone biosynthetic pathway
-
?
additional information
?
-
-
involved in the menaquinone biosynthetic pathway
-
?
additional information
?
-
involved in the menaquinone biosynthetic pathway
-
?
additional information
?
-
-
involved in the menaquinone biosynthetic pathway
-
?
additional information
?
-
-
the enzyme from Exiguobacterium sp. also shows N-succinylamino acid racemization activity, efficiency for the reaction is 0.041 mM/s. But the o-succinylbenzoate synthase activity is the only biologically relevant activity. Modeling of substrate and product binding, active site docking, overview
-
-
?
additional information
?
-
-
the enzyme from Exiguobacterium sp. also shows N-succinylamino acid racemization activity, efficiency for the reaction is 0.041 mM/s. But the o-succinylbenzoate synthase activity is the only biologically relevant activity. Modeling of substrate and product binding, active site docking, overview
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.48
(1R,6R)-2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate
-
-
0.007 - 0.668
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
additional information
additional information
-
substrate affinity is as much as 40fold higher for Escherichia coli OSBS than for OSBS of Amycolatopsis, also stated by analysis on phylogeny, structure, sequence conservation
-
0.007
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
pH 8.0, 25°C, recombinant mutant R17A
0.0096
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
-
pH 8.0, 25°C, recombinant mutant G16P/V17F/V18R/L19T/R20S/D21F/R22G/R23T/L24QL48A
0.01
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
-
pH 8.0, 25°C, recombinant mutant I265A
0.012
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
-
pH 8.0, 25°C, recombinant wild-type enzyme
0.013
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
-
pH 8.0, 25°C, recombinant mutant L19A
0.02
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
-
pH 8.0, 25°C, recombinant enzyme
0.021
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
-
pH 8.0, 25°C, recombinant mutant S262G
0.029
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
-
pH 8.0, 25°C, recombinant mutant S264A
0.036
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
pH 8.0, 25°C, recombinant mutant F16A
0.036
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
-
pH 8.0, 25°C, recombinant mutant L109A
0.038
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
pH 8.0, 25°C, recombinant mutant R17A/Y42A
0.048
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
pH 8.0, 25°C, recombinant mutant R17A/F39A
0.051
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
-
pH 8.0, 25°C, recombinant mutant F51Y
0.051
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
-
pH 8.0, 25°C, recombinant mutant S262A/S263A/S264A/I265A
0.052
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
-
pH 8.0, 25°C, recombinant mutant L48M
0.054
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
pH 8.0, 25°C, recombinant mutant R15G/F16G/R17G/G18G/I19G
0.057
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
pH 8.0, 25°C, recombinant mutant T75L
0.073
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
-
pH 8.0, 25°C, recombinant mutant L48M/F51Y
0.078
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
pH 8.0, 25°C, recombinant wild-type enzyme
0.08
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
-
pH 8.0, 25°C, recombinant mutant R159M
0.086
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
pH 8.0, 25°C, recombinant mutant G254A
0.089
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
-
pH 8.0, 25°C, recombinant mutant L48A/F51A
0.099
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
-
pH 8.0, 25°C, recombinant mutant V233N
0.111
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
-
pH 8.0, 25°C, recombinant mutant L48A
0.122
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
-
pH 8.0, 25°C, recombinant mutant F51A
0.145
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
pH 8.0, 25°C, recombinant mutant V230L
0.154
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
pH 8.0, 25°C, recombinant mutant T75A
0.158
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
-
pH 8.0, 25°C, recombinant mutant S263G
0.182
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
pH 8.0, 25°C, recombinant wild-type enzyme
0.206
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
-
pH 8.0, 25°C, recombinant mutant T291S
0.256
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
pH 8.0, 25°C, recombinant mutant N73A/T75L
0.3
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
pH 8.0, 25°C, recombinant mutant N73L/T75V
0.304
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
pH 8.0, 25°C, recombinant mutant G295A
0.322
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
pH 8.0, 25°C, recombinant mutant N73A
0.343
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
-
pH 8.0, 25°C, recombinant mutant S262T
0.47
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
pH 8.0, 25°C, recombinant mutant R128M
0.588
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
pH 8.0, 25°C, recombinant mutant Y42A
0.666
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
pH 8.0, 25°C, recombinant mutant F39A
0.668
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
pH 8.0, 25°C, recombinant mutant G254T
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
120
(1R,6R)-2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate
-
-
0.1 - 210
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
0.1
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
pH 8.0, 25°C, recombinant mutant R15G/F16G/R17G/G18G/I19G
0.18
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
pH 8.0, 25°C, recombinant mutant N73L/T75V
0.2
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
pH 8.0, 25°C, recombinant mutant R17A/F39A
0.36
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
pH 8.0, 25°C, recombinant mutant R17A/Y42A
0.4
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
-
pH 8.0, 25°C, recombinant mutant G16P/V17F/V18R/L19T/R20S/D21F/R22G/R23T/L24QL48A
0.6
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
pH 8.0, 25°C, recombinant mutant R17A
0.9
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
-
pH 8.0, 25°C, recombinant mutant R159M
2.7
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
-
pH 8.0, 25°C, recombinant mutant S262A/S263A/S264A/I265A
2.9
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
-
pH 8.0, 25°C, recombinant mutant L109A
3.9
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
-
pH 8.0, 25°C, recombinant mutant L19A
4
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
pH 8.0, 25°C, recombinant mutant G295A
4.4
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
pH 8.0, 25°C, recombinant mutant F16A
5.1
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
pH 8.0, 25°C, recombinant mutant N73A/T75L
6
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
-
pH 8.0, 25°C, recombinant mutant I265A
10
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
pH 8.0, 25°C, recombinant mutant N73A
10
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
-
pH 8.0, 25°C, recombinant mutant S262G
11
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
-
pH 8.0, 25°C, recombinant mutant L48A/F51A
12
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
-
pH 8.0, 25°C, recombinant mutant S264A
13
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
pH 8.0, 25°C, recombinant mutant G254T
14
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
-
pH 8.0, 25°C, recombinant mutant L48A
16
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
pH 8.0, 25°C, recombinant mutant G254A
18
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
-
pH 8.0, 25°C, recombinant mutant F51Y
18
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
pH 8.0, 25°C, recombinant mutant T75L
24
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
-
pH 8.0, 25°C, recombinant wild-type enzyme
27
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
-
pH 8.0, 25°C, recombinant mutant L48M/F51Y
29
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
-
pH 8.0, 25°C, recombinant mutant L48M
29
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
pH 8.0, 25°C, recombinant mutant V230L
49
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
-
pH 8.0, 25°C, recombinant mutant F51A
51
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
-
pH 8.0, 25°C, recombinant enzyme
55
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
pH 8.0, 25°C, recombinant mutant T75A
65
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
-
pH 8.0, 25°C, recombinant mutant S262T
67
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
-
pH 8.0, 25°C, recombinant mutant T291S
73
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
-
pH 8.0, 25°C, recombinant mutant S263G
80
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
pH 8.0, 25°C, recombinant wild-type enzyme
94
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
-
pH 8.0, 25°C, recombinant mutant V233N
104
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
pH 8.0, 25°C, recombinant mutant R128M
122
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
pH 8.0, 25°C, recombinant wild-type enzyme
163
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
pH 8.0, 25°C, recombinant mutant F39A
210
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
pH 8.0, 25°C, recombinant mutant Y42A
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.61 - 2600
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
additional information
additional information
-
catalytic efficiency for the N-succinylamino acid racemization reaction is 0.041 mM/s
-
0.61
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
pH 8.0, 25°C, recombinant mutant N73L/T75V
3.8
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
-
pH 8.0, 25°C, recombinant mutant G288A
4.2
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
pH 8.0, 25°C, recombinant mutant R17A/F39A
9.5
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
pH 8.0, 25°C, recombinant mutant R17A/Y42A
11
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
-
pH 8.0, 25°C, recombinant mutant R159M
13
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
pH 8.0, 25°C, recombinant mutant G295A
19
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
pH 8.0, 25°C, recombinant mutant G254T
20
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
pH 8.0, 25°C, recombinant mutant N73A/T75L
31
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
pH 8.0, 25°C, recombinant mutant N73A
43
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
-
pH 8.0, 25°C, recombinant mutant G16P/V17F/V18R/L19T/R20S/D21F/R22G/R23T/L24QL48A
53
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
-
pH 8.0, 25°C, recombinant mutant S262A/S263A/S264A/I265A
80
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
-
pH 8.0, 25°C, recombinant mutant L109A
86
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
pH 8.0, 25°C, recombinant mutant R17A
120
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
pH 8.0, 25°C, recombinant mutant F16A
122
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
pH 8.0, 25°C, recombinant wild-type enzyme
130
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
-
pH 8.0, 25°C, recombinant mutant L48A
130
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
-
pH 8.0, 25°C, recombinant mutant L48A/F51A
190
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
pH 8.0, 25°C, recombinant mutant G254A
190
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
-
pH 8.0, 25°C, recombinant mutant S262T
200
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
pH 8.0, 25°C, recombinant mutant V230L
220
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
pH 8.0, 25°C, recombinant mutant R128M
250
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
pH 8.0, 25°C, recombinant mutant F39A
300
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
-
pH 8.0, 25°C, recombinant mutant L19A
320
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
pH 8.0, 25°C, recombinant mutant T75L
330
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
-
pH 8.0, 25°C, recombinant mutant T291S
350
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
-
pH 8.0, 25°C, recombinant mutant F51Y
360
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
pH 8.0, 25°C, recombinant mutant T75A
360
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
pH 8.0, 25°C, recombinant mutant Y42A
370
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
-
pH 8.0, 25°C, recombinant mutant L48M/F51Y
400
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
-
pH 8.0, 25°C, recombinant mutant F51A
410
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
-
pH 8.0, 25°C, recombinant mutant S264A
460
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
-
pH 8.0, 25°C, recombinant mutant S263G
480
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
-
pH 8.0, 25°C, recombinant mutant S262G
570
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
-
pH 8.0, 25°C, recombinant mutant L48M
580
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
-
pH 8.0, 25°C, recombinant mutant I265A
670
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
pH 8.0, 25°C, recombinant mutant R15G/F16G/R17G/G18G/I19G
960
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
-
pH 8.0, 25°C, recombinant mutant V233N
1000
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
pH 8.0, 25°C, recombinant wild-type enzyme
2000
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
-
pH 8.0, 25°C, recombinant wild-type enzyme
2600
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
-
pH 8.0, 25°C, recombinant enzyme
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
evolution
o-succinylbenzoate synthase is a member of the enolase superfamily
evolution
o-succinylbenzoate synthase is a member of the enolase superfamily, there are significant differences in structure and conformational flexibility between Thermobifida fusca OSBS and other members of the enolase superfamily. The 20s loop, a flexible loop in the active site that permits ligand binding and release in most enolase superfamily proteins, has a four-amino acid deletion and is well-ordered in Thermobifida fusca OSBS. The flexibility of a different region allows the substrate to enter from the other side of the active site
evolution
-
the enzyme belongs to the NSAR/OSBS subfamily of enzymes, the enzyme from Exiguobacterium sp. shows both o-succinylbenzoate synthase and N-succinylamino acid racemization activities. The N-succinylamino acid racemization activity originates as a promiscuous activity in an ancestor of the NSAR/OSBS subfamily. ExiOSBS diverged from the NSAR/OSBS subfamily before NSAR emerged as a biologically relevant activity
evolution
-
the enzyme belongs to the o-succinylbenzoate synthase (OSBS) family, which is part of the enolase superfamily. Some enzymes in the OSBS family catalyze another reaction, N-succinylamino acid racemization (NSAR). NSARs cannot be segregated into a separate family because their sequences are highly similar to those of known OSBSs, and many of them have both OSBS and NSAR activities. Phylogenetic and sequence analysis
evolution
the evolution of catalytically promiscuous enzymes like those from the N-succinylamino acid racemase/o-succinylbenzoate synthase (NSAR/OSBS) subfamily can reveal mechanisms by which new functions evolve. Additional sites influence the evolution of NSAR reaction specificity in the NSAR/OSBS subfamily
evolution
-
the evolution of catalytically promiscuous enzymes like those from the N-succinylamino acid racemase/o-succinylbenzoate synthase (NSAR/OSBS) subfamily can reveal mechanisms by which new functions evolve. Additional sites influence the evolution of NSAR reaction specificity in the NSAR/OSBS subfamily
-
evolution
-
the enzyme belongs to the NSAR/OSBS subfamily of enzymes, the enzyme from Exiguobacterium sp. shows both o-succinylbenzoate synthase and N-succinylamino acid racemization activities. The N-succinylamino acid racemization activity originates as a promiscuous activity in an ancestor of the NSAR/OSBS subfamily. ExiOSBS diverged from the NSAR/OSBS subfamily before NSAR emerged as a biologically relevant activity
-
metabolism
o-succinylbenzoate synthase catalyzes a step in menaquinone biosynthesis
metabolism
o-succinylbenzoate synthase catalyzes a step in menaquinone biosynthesis
metabolism
-
the enzyme is important in the menaquinone biosynthesis
metabolism
-
the enzyme is involved in menaquinone synthesis
metabolism
-
the enzyme is required for menaquinone biosynthesis
metabolism
O-succinylbenzoate synthase plays a major role in the shikimate pathway
metabolism
-
the enzyme is involved in menaquinone synthesis
-
metabolism
-
O-succinylbenzoate synthase plays a major role in the shikimate pathway
-
metabolism
-
the enzyme is important in the menaquinone biosynthesis
-
physiological function
O-succinylbenzoate synthase is an important enzyme in the biosynthesis of menaquinone, ubiquinone, and terpenoid quinone in Mycobacterium tuberculosis
physiological function
-
O-succinylbenzoate synthase is an important enzyme in the biosynthesis of menaquinone, ubiquinone, and terpenoid quinone in Mycobacterium tuberculosis
-
additional information
-
Lys108, Asn140, Asp138, Lys110, Glu189, Ser236, Asp188, Arg27, Tyr52, and Ser237 are highly conserved and may play a vital role as active residues
additional information
the 20s loop, a flexible loop in the active site that permits ligand binding and release in most enolase superfamily proteins, has a four-amino acid deletion and is well-ordered in Thermobifida fusca OSBS. The flexibility of a different region allows the substrate to enter from the other side of the active site, active site structure, overview. Comparison of apo and ligand-bound structures of the Mycobacterium tuberculosis enzyme with the Escherichia coli enzyme
additional information
-
the 20s loop, a flexible loop in the active site that permits ligand binding and release in most enolase superfamily proteins, has a four-amino acid deletion and is well-ordered in Thermobifida fusca OSBS. The flexibility of a different region allows the substrate to enter from the other side of the active site, active site structure, overview. Comparison of apo and ligand-bound structures of the Mycobacterium tuberculosis enzyme with the Escherichia coli enzyme
additional information
competitive inhibition and molecular modeling show that AaOSBS binds N-succinylphenylglycine with moderate affinity in a site that overlaps its normal substrate
additional information
enzyme promiscuity in enolase superfamily is analyzed by using quantum mechanics/molecular mechanics (QM/MM) methods, using both density functional theory and semiempirical Hamiltonians. Presence of flexible loops in the active site and the selection of structural modifications in the substrate seem to be key elements to promote the promiscuity of this enzyme, role played by the different residues in each of the two possible reactions, overview
additional information
molecular modeling and docking study of O-succinylbenzoate synthase of Mycobacterium tuberculosis, overview. A three-dimensional structure model of Mtb-OSBS is built using structure coordinates of Thermobifida fusca. Residues Lys108, Asn140, Asp138, Lys110, Glu189, Ser236, Asp188, Arg27, Tyr52, and Ser237 are highly conserved and may play a vital role as active residues
additional information
-
molecular modeling and docking study of O-succinylbenzoate synthase of Mycobacterium tuberculosis, overview. A three-dimensional structure model of Mtb-OSBS is built using structure coordinates of Thermobifida fusca. Residues Lys108, Asn140, Asp138, Lys110, Glu189, Ser236, Asp188, Arg27, Tyr52, and Ser237 are highly conserved and may play a vital role as active residues
additional information
-
competitive inhibition and molecular modeling show that AaOSBS binds N-succinylphenylglycine with moderate affinity in a site that overlaps its normal substrate
-
additional information
-
molecular modeling and docking study of O-succinylbenzoate synthase of Mycobacterium tuberculosis, overview. A three-dimensional structure model of Mtb-OSBS is built using structure coordinates of Thermobifida fusca. Residues Lys108, Asn140, Asp138, Lys110, Glu189, Ser236, Asp188, Arg27, Tyr52, and Ser237 are highly conserved and may play a vital role as active residues
-
additional information
-
Lys108, Asn140, Asp138, Lys110, Glu189, Ser236, Asp188, Arg27, Tyr52, and Ser237 are highly conserved and may play a vital role as active residues
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Y299I
naturally occuring mutation, identified by molecular modeling and sequence conservation within the NSAR/OSBS subfamily, the mutation increases NSAR activity from without affecting OSBS activity. The mutation does not appear to affect binding affinity but instead affects kcat, by reorienting the substrate or modifying conformational changes to allow both catalytic lysines to access the proton that is moved during the reaction
Y299I/M18F
site-directed mutagenesis, while the Y299I mutation increases NSAR activity, the second mutation M18F obliterates this gain of activity, epistatic interference by M18F
Y299I
-
naturally occuring mutation, identified by molecular modeling and sequence conservation within the NSAR/OSBS subfamily, the mutation increases NSAR activity from without affecting OSBS activity. The mutation does not appear to affect binding affinity but instead affects kcat, by reorienting the substrate or modifying conformational changes to allow both catalytic lysines to access the proton that is moved during the reaction
-
Y299I/M18F
-
site-directed mutagenesis, while the Y299I mutation increases NSAR activity, the second mutation M18F obliterates this gain of activity, epistatic interference by M18F
-
K163R
-
no o-succinylbenzoate synthase activity and no N-acylamino acid racemase activity, mutant enzyme catalyzes the stereospecific exchange of the alpha-hydrogen of N-succinyl-(S)-phenylglycine with solvent hydrogen
K163S
-
no o-succinylbenzoate synthase activity and no N-acylamino acid racemase activity, mutant enzyme catalyzes the stereospecific exchange of the alpha-hydrogen of N-succinyl-(S)-phenylglycine with solvent hydrogen
K263R
-
no o-succinylbenzoate synthase activity and no N-acylamino acid racemase activity, mutant enzyme catalyzes the stereospecific exchange of the alpha-hydrogen of N-succinyl-(R)-phenylglycine with solvent hydrogen
K263S
-
no o-succinylbenzoate synthase activity and no N-acylamino acid racemase activity, mutant enzyme catalyzes the stereospecific exchange of the alpha-hydrogen of N-succinyl-(R)-phenylglycine with solvent hydrogen
F51A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
F51Y
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
G16P/V17F/V18R/L19T/R20S/D21F/R22G/R23T/L24QL48A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
G288A
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme, G288A introduces a steric clash with the substrate, reducing kcat/KM over 500fold
G295A
site-directed mutagenesis, the mutant enzyme activity is reduced compared to the wild-type enzyme
I265A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
L109A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
L19A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
L48A/F51A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
L48M
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
L48M/F51Y
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
R159M
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
S262A/S263A/S264A/I265A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
S262G
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
S262T
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
S263G
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
S264A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
T291S
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
V233N
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
F16A
site-directed mutagenesis, the mutant enzyme activity is reduced compared to the wild-type enzyme
F39A
site-directed mutagenesis, the mutant enzyme activity is reduced compared to the wild-type enzyme
G254A
site-directed mutagenesis, the mutant enzyme activity is reduced compared to the wild-type enzyme
G254T
site-directed mutagenesis, the mutant enzyme activity is reduced compared to the wild-type enzyme
N73A
site-directed mutagenesis, the mutant enzyme activity is reduced compared to the wild-type enzyme
N73A/T75A
site-directed mutagenesis, the mutant is inactive
N73A/T75L
site-directed mutagenesis, the mutant enzyme activity is reduced compared to the wild-type enzyme
N73L/T75V
site-directed mutagenesis, the mutant enzyme activity is reduced compared to the wild-type enzyme
R128M
site-directed mutagenesis, the mutant enzyme activity is reduced compared to the wild-type enzyme
R15G/F16G/R17G/G18G/I19G
site-directed mutagenesis, the mutant enzyme activity is reduced compared to the wild-type enzyme
R17A
site-directed mutagenesis, the mutant enzyme activity is reduced compared to the wild-type enzyme
R17A/F39A
site-directed mutagenesis, the mutant enzyme activity is reduced compared to the wild-type enzyme
R17A/Y42A
site-directed mutagenesis, the mutant enzyme activity is reduced compared to the wild-type enzyme
T75A
site-directed mutagenesis, the mutant enzyme activity is reduced compared to the wild-type enzyme
T75L
site-directed mutagenesis, the mutant enzyme activity is reduced compared to the wild-type enzyme
V230L
site-directed mutagenesis, the mutant enzyme activity is reduced compared to the wild-type enzyme
Y42A
site-directed mutagenesis, the mutant enzyme activity is reduced compared to the wild-type enzyme
additional information
-
20s loop is truncated by deleting residues V17, V18, L19, R20, D21, R22, R23, and L24 resulting in a mutant with highly reduced activity compared to the wild-type enzyme
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Thompson, T.B.; Garrett, J.B.; Taylor, E.A.; Meganathan, R.; Gerlt, J.A.; Rayment, I.
Evolution of enzymatic activity in the enolase superfamily: structure of o-succinylbenzoate synthase from Escherichia coli in complex with Mg2+ and o-succinylbenzoate
Biochemistry
39
10662-10676
2000
Escherichia coli (P29208), Escherichia coli
brenda
Klenchin, V.A.; Taylor Ringia, E.A.; Gerlt, J.A.; Rayment, I.
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
Biochemistry
42
14427-14433
2003
Escherichia coli (P29208), Escherichia coli
brenda
Weische, A.; Garvert, W.; Leistner, E.
Biosynthesis of o-succinylbenzoic acid. II.: Properties of o-succinylbenzoic acid synthase, an enzyme involved in vitamin K2 biosynthesis
Arch. Biochem. Biophys.
256
223-231
1987
Escherichia coli, Escherichia coli AN 154
brenda
Taylor Ringia, E.A.; Garrett, J.B.; Thoden, J.B.; Holden, H.M.; Rayment, I.; Gerlt, J.A.
Evolution of enzymatic activity in the enolase superfamily: functional studies of the promiscuous o-succinylbenzoate synthase from Amycolatopsis
Biochemistry
43
224-229
2004
Amycolatopsis sp.
brenda
Thoden, J.B.; Taylor Ringia, E.A.; Garrett, J.B.; Gerlt, J.A.; Holden, H.M.; Rayment, I.
Evolution of enzymatic activity in the enolase superfamily: structural studies of the promiscuous o-succinylbenzoate synthase from Amycolatopsis
Biochemistry
43
5716-5727
2004
Amycolatopsis sp., Amycolatopsis sp. T-1-60
brenda
Glasner, M.E.; Fayazmanesh, N.; Chiang, R.A.; Sakai, A.; Jacobson, M.P.; Gerlt, J.A.; Babbitt, P.C.
Evolution of structure and function in the o-succinylbenzoate synthase/N-acylamino acid racemase family of the enolase superfamily
J. Mol. Biol.
360
228-250
2006
Amycolatopsis sp.
brenda
Pulaganti, M.; Banaganapalli, B.; Mulakayala, C.; Chitta, S.K.; C M, A.
Molecular modeling and docking studies of O-succinylbenzoate synthase of M. tuberculosis - a potential target for antituberculosis drug design
Appl. Biochem. Biotechnol.
172
1407-1432
2014
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
brenda
Brizendine, A.M.; Odokonyero, D.; McMillan, A.W.; Zhu, M.; Hull, K.; Romo, D.; Glasner, M.E.
Promiscuity of Exiguobacterium sp. AT1b o-succinylbenzoate synthase illustrates evolutionary transitions in the OSBS family
Biochem. Biophys. Res. Commun.
450
679-684
2014
Exiguobacterium sp., Exiguobacterium sp. AT1b
brenda
Zhu, W.W.; Wang, C.; Jipp, J.; Ferguson, L.; Lucas, S.N.; Hicks, M.A.; Glasner, M.E.
Residues required for activity in Escherichia coli o-succinylbenzoate synthase (OSBS) are not conserved in all OSBS enzymes
Biochemistry
51
6171-6181
2012
Escherichia coli
brenda
Odokonyero, D.; Ragumani, S.; Lopez, M.S.; Bonanno, J.B.; Ozerova, N.D.; Woodard, D.R.; Machala, B.W.; Swaminathan, S.; Burley, S.K.; Almo, S.C.; Glasner, M.E.
Divergent evolution of ligand binding in the o-succinylbenzoate synthase family
Biochemistry
52
7512-7521
2013
Escherichia coli (P29208), Escherichia coli, Thermobifida fusca (Q47Q21), Thermobifida fusca
brenda
Pulaganti, M.; Banaganapalli, B.; Mulakayala, C.; Chitta, S.; Anuradha, C.
Molecular modeling and docking studies of O-succinylbenzoate synthase of M. tuberculosis - a potential target for antituberculosis drug design
Appl. Biochem. Biotechnol.
172
1407-1432
2014
Mycobacterium tuberculosis (P9WJP3), Mycobacterium tuberculosis, Mycobacterium tuberculosis ATCC 25618 / H37Rv (P9WJP3)
brenda
Odokonyero, D.; McMillan, A.W.; Ramagopal, U.A.; Toro, R.; Truong, D.P.; Zhu, M.; Lopez, M.S.; Somiari, B.; Herman, M.; Aziz, A.; Bonanno, J.B.; Hull, K.G.; Burley, S.K.; Romo, D.; Almo, S.C.; Glasner, M.E.
Comparison of Alicyclobacillus acidocaldarius o-succinylbenzoate synthase to its promiscuous N-succinylamino acid racemase/o-succinylbenzoate synthase relatives
Biochemistry
57
3676-3689
2018
Alicyclobacillus acidocaldarius subsp. acidocaldarius (C8WS29), Alicyclobacillus acidocaldarius subsp. acidocaldarius ATCC 27009 / DSM 446 / JCM 5260 / NBRC 15652 / NCIMB 11725 / NRRL B-14509 / 104-1A (C8WS29)
brenda
Sanchez-Tarin, M.; Swiderek, K.; Roca, M.; Tunon, I.
Enzyme promiscuity in enolase superfamily. Theoretical study of o-succinylbenzoate synthase using QM/MM methods
J. Phys. Chem. B
119
1899-1911
2015
Amycolatopsis sp. (Q44244)
brenda