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Literature summary for 4.2.1.113 extracted from

  • 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 (2004), Biochemistry, 43, 5716-5727.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
hanging-drop vapor diffusion method, the best crystals are observed growing at room temperature from poly(ethylene glycol) 8000 at pH 8.0, space group R32 with unit cell dimensions of a = b = 216.0 A and c = 261.0 A and contains 4 subunits in the asymmetric unit. Three-dimensional structures of liganded complexes of the enzyme with o-succinylbenzoate, N-acetylmethionine, N-succinylmethionine, succinylphenylglycine to 2.2, 2.3, 2.1, and 1.9 A resolution, respectively Amycolatopsis sp.

Organism

Organism UniProt Comment Textmining
Amycolatopsis sp.
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Amycolatopsis sp. T-1-60
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Purification (Commentary)

Purification (Comment) Organism
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Amycolatopsis sp.