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o-succinylbenzoate synthase

Part of the Springer Handbook of Enzymes book series (HDBKENZYMES, volume S7)

Keywords

Escherichia Coli Source Organism UNIPROT Accession Thiamine Diphosphate Racemase Activity 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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References

  1. [1]
    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)CrossRefPubMedGoogle Scholar
  2. [2]
    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)CrossRefPubMedGoogle Scholar
  3. [3]
    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)CrossRefPubMedGoogle Scholar
  4. [4]
    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)CrossRefPubMedGoogle Scholar
  5. [5]
    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)CrossRefPubMedGoogle Scholar

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