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Literature summary for 4.2.1.113 extracted from

  • 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 (2014), Biochem. Biophys. Res. Commun., 450, 679-684.
    View publication on PubMed
Search for more literature for 4.2.1.113

Cloned(Commentary)

Cloned (Comment) Organism
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.

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.02
-
 (1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate pH 8.0, 25°C, recombinant enzyme Exiguobacterium sp.

Metals/Ions

Metals/Ions Comment Organism Structure
Mn2+ required Exiguobacterium sp.

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate Exiguobacterium sp.
-
 2-succinylbenzoate + H2O
-
 ?
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate Exiguobacterium sp. AT1b
-
 2-succinylbenzoate + H2O
-
 ?
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 ?
-
 ?
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 ?
-
 ?

Organism

Organism UniProt Comment Textmining
Exiguobacterium sp.
-
-
-
Exiguobacterium sp. AT1b
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant N-terminally His-tagged enzyme from Escherichia coli strain BW25113 menC- by metal affinity chromatography Exiguobacterium sp.

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
-
 Exiguobacterium sp. 2-succinylbenzoate + H2O
-
 ?
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
-
 Exiguobacterium sp. AT1b 2-succinylbenzoate + H2O
-
 ?
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. ?
-
 ?
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 ?
-
 ?

Synonyms

Synonyms Comment Organism
ExiOSBS
-
 Exiguobacterium sp.
OSBS
-
 Exiguobacterium sp.

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
 assay at Exiguobacterium sp.

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
51
-
 (1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate pH 8.0, 25°C, recombinant enzyme Exiguobacterium sp.

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
 assay at Exiguobacterium sp.

General Information

General Information Comment Organism
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.
metabolism the enzyme is involved in menaquinone synthesis Exiguobacterium sp.

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
additional information
-
 additional information catalytic efficiency for the N-succinylamino acid racemization reaction is 0.041 mM/s Exiguobacterium sp.
2600
-
 (1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate pH 8.0, 25°C, recombinant enzyme Exiguobacterium sp.