EC Number | Cloned (Comment) | Organism |
---|---|---|
4.2.1.113 | ExiOSBS is encoded in the menaquinone synthesis operon, phylogenetic analysis and tree of the NSAR/OSBS subfamily, expression of N-terminally His-tagged enzyme in Escherichia coli strain BW25113 menC- | Exiguobacterium sp. |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
4.2.1.113 | 0.02 | - |
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate | pH 8.0, 25°C, recombinant enzyme | Exiguobacterium sp. |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
4.2.1.113 | Mn2+ | required | Exiguobacterium sp. |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
4.2.1.113 | (1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate | Exiguobacterium sp. | - |
2-succinylbenzoate + H2O | - |
? | |
4.2.1.113 | (1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate | Exiguobacterium sp. AT1b | - |
2-succinylbenzoate + H2O | - |
? | |
4.2.1.113 | additional information | Exiguobacterium sp. | 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 | ? | - |
? | |
4.2.1.113 | additional information | Exiguobacterium sp. AT1b | 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 | ? | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
4.2.1.113 | Exiguobacterium sp. | - |
- |
- |
4.2.1.113 | Exiguobacterium sp. AT1b | - |
- |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
4.2.1.113 | recombinant N-terminally His-tagged enzyme from Escherichia coli strain BW25113 menC- by metal affinity chromatography | Exiguobacterium sp. |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
4.2.1.113 | (1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate | - |
Exiguobacterium sp. | 2-succinylbenzoate + H2O | - |
? | |
4.2.1.113 | (1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate | - |
Exiguobacterium sp. AT1b | 2-succinylbenzoate + H2O | - |
? | |
4.2.1.113 | 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 | Exiguobacterium sp. | ? | - |
? | |
4.2.1.113 | 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 | Exiguobacterium sp. AT1b | ? | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
4.2.1.113 | ExiOSBS | - |
Exiguobacterium sp. |
4.2.1.113 | OSBS | - |
Exiguobacterium sp. |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
4.2.1.113 | 25 | - |
assay at | Exiguobacterium sp. |
EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
4.2.1.113 | 51 | - |
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate | pH 8.0, 25°C, recombinant enzyme | Exiguobacterium sp. |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
4.2.1.113 | 8 | - |
assay at | Exiguobacterium sp. |
EC Number | General Information | Comment | Organism |
---|---|---|---|
4.2.1.113 | 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 | Exiguobacterium sp. |
4.2.1.113 | metabolism | the enzyme is involved in menaquinone synthesis | Exiguobacterium sp. |
EC Number | kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
4.2.1.113 | additional information | - |
additional information | catalytic efficiency for the N-succinylamino acid racemization reaction is 0.041 mM/s | Exiguobacterium sp. | |
4.2.1.113 | 2600 | - |
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate | pH 8.0, 25°C, recombinant enzyme | Exiguobacterium sp. |