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Literature summary for 5.4.99.5 extracted from

  • Asojo, O.; Subramanian, S.; Abendroth, J.; Exley, I.; Lorimer, D.; Edwards, T.; Myler, P.
    Crystal structure of chorismate mutase from Burkholderia phymatum (2018), Acta Crystallogr. Sect. F, 74, 187-192 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 5.4.99.5

Cloned(Commentary)

Cloned (Comment) Organism
gene Bphy_7813, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)-R3 Rosetta Paraburkholderia phymatum

Crystallization (Commentary)

Crystallization (Comment) Organism
purified recombinant enzyme, sitting drop vapor diffusion method, mixing of 400 nl of 22.4 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 formate, pH 6.6, and equilibration against 0.08 ml of reservoir solution, X-ray diffraction structure determination and analysis at 1.95 A resolution Paraburkholderia phymatum

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
Chorismate Paraburkholderia phymatum
-
 Prephenate
-
 ?
Chorismate Paraburkholderia phymatum DSM 17167 / CIP 108236 / LMG 21445 / STM815
-
 Prephenate
-
 ?

Organism

Organism UniProt Comment Textmining
Paraburkholderia phymatum B2JYH9 i.e. Paraburkholderia phymatum, identified from root-nodule isolates from tropical legumes and is capable of symbiotic nitrogen fixation with the legumes Machaerium lunatum and Mimosa pudica
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Paraburkholderia phymatum DSM 17167 / CIP 108236 / LMG 21445 / STM815 B2JYH9 i.e. Paraburkholderia phymatum, identified from root-nodule isolates from tropical legumes and is capable of symbiotic nitrogen fixation with the legumes Machaerium lunatum and Mimosa pudica
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3)-R3 Rosetta by nickel affinity chromatography, gel filtration, and ultrafiltration Paraburkholderia phymatum

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Chorismate
-
 Paraburkholderia phymatum Prephenate
-
 ?
Chorismate
-
 Paraburkholderia phymatum DSM 17167 / CIP 108236 / LMG 21445 / STM815 Prephenate
-
 ?

Subunits

Subunits Comment Organism
More the enzyme is a chorismate mutases with AroQgamma topology Paraburkholderia phymatum

Synonyms

Synonyms Comment Organism
AroQ
-
 Paraburkholderia phymatum
Bphy_7813
-
 Paraburkholderia phymatum

General Information

General Information Comment Organism
evolution there are two classes of chorismate mutase: AroQ and AroH. The bacterial subclass AroQgamma has reported roles in virulence. Chorismate mutase from Burkholderia phymatum has the prototypical AroQgamma topology and retains the characteristic chorismate mutase active site Paraburkholderia phymatum
additional information the enzyme is a chorismate mutase with AroQgamma topology, enzyme structure analysis, enzyme topology, and conserved residues in the substrate-binding sites of chorismate mutase, overview Paraburkholderia phymatum