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Literature summary extracted from

  • Asojo, O.; Dranow, D.; Serbzhinskiy, D.; Subramanian, S.; Staker, B.; Edwards, T.; Myler, P.
    Crystal structure of chorismate mutase from Burkholderia thailandensis (2018), Acta Crystallogr. Sect. F, 74, 294-299 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
5.4.99.5 gene BTH_I1596, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)R3 Rosetta Burkholderia thailandensis

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
5.4.99.5 purified recombinant enzyme, sitting drop vapor diffusion method, mixing of 400 nl of 20 mg/ml protein in 20 mM HEPES, pH 7.0, 300 mM NaCl, 5% glycerol, and 1 mM TCEP, with 400 nl reservoir solution containing 20% w/v PEG 3350, 200 mM ammonium nitrate, and equilibration against 0.08 ml of reservoir solution, 17°C, X-ray diffraction structure determination and analysis at 2.15 A resolution Burkholderia thailandensis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
5.4.99.5 Chorismate Burkholderia thailandensis
-
 Prephenate
-
 ?
5.4.99.5 Chorismate Burkholderia thailandensis ATCC 700388 / DSM 13276 / CIP 106301 / E264
-
 Prephenate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
5.4.99.5 Burkholderia thailandensis Q2SY64
-
-
5.4.99.5 Burkholderia thailandensis ATCC 700388 / DSM 13276 / CIP 106301 / E264 Q2SY64
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
5.4.99.5 recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3)R3 Rosetta by nickel affinity chromatography, gel filtration, and ultrafiltration Burkholderia thailandensis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5.4.99.5 Chorismate
-
 Burkholderia thailandensis Prephenate
-
 ?
5.4.99.5 Chorismate
-
 Burkholderia thailandensis ATCC 700388 / DSM 13276 / CIP 106301 / E264 Prephenate
-
 ?

Subunits

EC Number Subunits Comment Organism
5.4.99.5 More the high-resolution structure of chorismate mutase is determined in the monoclinic space group P21 with three homodimers per asymmetric unit. The overall structure of each protomer has the prototypical AroQgamma topology and shares conserved binding-cavity residues with other chorismate mutases. The AroQgamma topology is composed entirely of helices connected by short loops Burkholderia thailandensis

Synonyms

EC Number Synonyms Comment Organism
5.4.99.5 AroQ
-
 Burkholderia thailandensis
5.4.99.5 BTH_I1596
-
 Burkholderia thailandensis

General Information

EC Number General Information Comment Organism
5.4.99.5 additional information enzyme structure analysis, enzyme topology, and conserved residues in the substrate-binding sites of chorismate mutase, overview Burkholderia thailandensis