Activating Compound | Comment | Organism | Structure |
---|---|---|---|
CoA | CoA, the last substrate to bind, strongly activates the first half-reaction after the first round of turnover, by CoA stabilizing conformations of the enzyme in the F form, which slowly isomerize back to the E form | Bacillus anthracis |
Application | Comment | Organism |
---|---|---|
drug development | the enzyme is a potential target for the discovery of antibiotics | Bacillus anthracis |
Cloned (Comment) | Organism |
---|---|
gene menE, DNA and amino acid sequence determination and analysis, expression of the His6-tagged enzyme in Escherichia coli strain BL21(DE3) | Bacillus anthracis |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
5'-O-{N-[2-(trifluoromethyl)phenyl]-4-oxobutyl}adenosine sulfonamide | i.e. TFMP-butyl-AMS, a reaction intermediate analogue of 2-succinylbenzoate-AMP, uncompetitive versus CoA and a mixed-type versus ATP and 2-succinylbenzoate | Bacillus anthracis | |
AMP | competitive versus ATP, mixed-type versus 2-succinylbenzoate | Bacillus anthracis | |
benzoyl-CoA | competitive versus CoA | Bacillus anthracis | |
additional information | inhibitor design studies, overvew | Bacillus anthracis |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | pre-steady-state and steady-state kinetic studies, overview | Bacillus anthracis | |
0.0219 | - |
2-succinylbenzoate | pH 7.5, 21°C, recombinant His-tagged enzyme | Bacillus anthracis | |
0.0268 | - |
ATP | pH 7.5, 21°C, recombinant His-tagged enzyme | Bacillus anthracis | |
0.304 | - |
CoA | pH 7.5, 21°C, recombinant His-tagged enzyme | Bacillus anthracis |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | - |
Bacillus anthracis |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + 2-succinylbenzoate + CoA | Bacillus anthracis | ATP-dependent condensation of o-succinylbenzoate, and CoA to form o-succinylbenzoyl-CoA, the fourth step of the menaquinone biosynthetic pathway in Bacillus anthracis | AMP + diphosphate + 2-succinylbenzoyl-CoA | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Bacillus anthracis | Q81K97 | gene menE | - |
Purification (Comment) | Organism |
---|---|
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity and hydrophobic interaction chromatography | Bacillus anthracis |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
ATP + 2-succinylbenzoate + CoA = AMP + diphosphate + 4-(2-carboxyphenyl)-4-oxobutanoyl-CoA | kinetic ordered bi uni uni bi ping-pong mechanism | Bacillus anthracis |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
additional information | - |
- |
Bacillus anthracis |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
4-[2-(trifluoromethyl)phenyl]-4-oxobutyric acid + CoA | a substrate analogue, 100fold less active than 2-succinylbenzoate | Bacillus anthracis | AMP + diphosphate + 4-[2-(trifluoromethyl)phenyl]-4-oxobutyryl-CoA | - |
? | |
ATP + 2-succinylbenzoate + CoA | ATP-dependent condensation of o-succinylbenzoate, and CoA to form o-succinylbenzoyl-CoA, the fourth step of the menaquinone biosynthetic pathway in Bacillus anthracis | Bacillus anthracis | AMP + diphosphate + 2-succinylbenzoyl-CoA | - |
? | |
ATP + 2-succinylbenzoate + CoA | substrate specificity and binding structure, overview | Bacillus anthracis | AMP + diphosphate + 2-succinylbenzoyl-CoA | - |
? |
Synonyms | Comment | Organism |
---|---|---|
o-succinylbenzoyl-CoA synthetase | - |
Bacillus anthracis |
OSB-CoA synthetase | - |
Bacillus anthracis |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
21 | - |
assay at | Bacillus anthracis |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
2.62 | - |
ATP | pH 7.5, 21°C, recombinant His-tagged enzyme | Bacillus anthracis | |
2.62 | - |
CoA | pH 7.5, 21°C, recombinant His-tagged enzyme | Bacillus anthracis | |
2.62 | - |
2-succinylbenzoate | pH 7.5, 21°C, recombinant His-tagged enzyme | Bacillus anthracis |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.5 | - |
assay at | Bacillus anthracis |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
ATP | - |
Bacillus anthracis |
Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|
0.0052 | - |
5'-O-(N-[2-(trifluoromethyl)phenyl]-4-oxobutyl)adenosine sulfonamide | pH 7.5, 21°C, versus ATP, recombinant enzyme | Bacillus anthracis | |
0.0056 | - |
5'-O-(N-[2-(trifluoromethyl)phenyl]-4-oxobutyl)adenosine sulfonamide | pH 7.5, 21°C, versus 2-succinylbenzoate, recombinant enzyme | Bacillus anthracis | |
0.0089 | - |
5'-O-(N-[2-(trifluoromethyl)phenyl]-4-oxobutyl)adenosine sulfonamide | pH 7.5, 21°C, versus CoA, recombinant enzyme | Bacillus anthracis | |
3 | - |
benzoyl-CoA | pH 7.5, 21°C, versus CoA, recombinant enzyme | Bacillus anthracis | |
3.6 | - |
AMP | pH 7.5, 21°C, versus ATP, recombinant enzyme | Bacillus anthracis | |
4.6 | - |
AMP | pH 7.5, 21°C, versus 2-succinylbenzoate, recombinant enzyme | Bacillus anthracis |