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Literature summary extracted from

  • Domagalski, M.J.; Tkaczuk, K.L.; Chruszcz, M.; Skarina, T.; Onopriyenko, O.; Cymborowski, M.; Grabowski, M.; Savchenko, A.; Minor, W.
    Structure of isochorismate synthase DhbC from Bacillus anthracis (2013), Acta Crystallogr. Sect. F, 69, 956-961.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
5.4.4.2 gene dhbC, overexpression in Escherichia coli strain BL21-CodonPlus(DE3)-RIPL as His-tagged enzyme from vector pMCSG19c in fusion N-terminally with maltose binding protein and a Tobacco vein mottling virus protease cleaving site, the His-tag is cleavable by Tobacco etch virus protease, in M9 SeMET High-Yield growth medium Bacillus anthracis

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
5.4.4.2 purified recombinant detagged selenomethionine-labeled enzyme, hanging drop vapor diffusion method, mixing of 0.002 ml of protein solution containing 16 mg/ml protein in 300 mM NaCl, 10 mM HEPES, pH 7.5, 0.5 mM TCEP, with 0.002 ml of well solution containing 2 M ammonium sulfate, 2% v/v PEG 400, 100 mM HEPES. pH 7.5, 50 mM Bis-Tris, pH 5.5, X-ray diffraction structure determination and analysis at 2.4 A resolution, single-wavelength anomalous diffraction Bacillus anthracis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
5.4.4.2 Mg2+ Mg2+-dependent catalytic mechanism Bacillus anthracis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
5.4.4.2 Chorismate Bacillus anthracis
-
 Isochorismate
-
 r
5.4.4.2 Chorismate Bacillus anthracis Ames
-
 Isochorismate
-
 r

Organism

EC Number Organism UniProt Comment Textmining
5.4.4.2 Bacillus anthracis Q81QQ0 gene dhbC
-
5.4.4.2 Bacillus anthracis Ames Q81QQ0 gene dhbC
-

Purification (Commentary)

EC Number Purification (Comment) Organism
5.4.4.2 recombinant selenomethionine-substituted, His-tagged enzyme from Escherichia coli strain BL21-CodonPlus(DE3)-RIPL by nickel affinity chromatography, His-tag cleavage, and a second step of nickel affinity chromatography Bacillus anthracis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5.4.4.2 Chorismate
-
 Bacillus anthracis Isochorismate
-
 r
5.4.4.2 Chorismate
-
 Bacillus anthracis Ames Isochorismate
-
 r

Subunits

EC Number Subunits Comment Organism
5.4.4.2 More enzyme structure comparisons and analysis, overview Bacillus anthracis

Synonyms

EC Number Synonyms Comment Organism
5.4.4.2 DhbC
-
 Bacillus anthracis

General Information

EC Number General Information Comment Organism
5.4.4.2 additional information enzyme structure comparisons and analysis, active site structure, overview. Ala304 plays an important role in positioning the peptide-bond carbonyl, enabling the formation of a proper hydrogen bond to the isochorismate C2 hydroxyl Bacillus anthracis
5.4.4.2 physiological function the enzyme is essential for the biosynthesis of the siderophore bacillibactin by the pathogenic bacterium Bacillus anthracis