Literature summary for 5.4.4.2 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.

Cloned(Commentary)

Cloned (Comment)	Organism
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)

Crystallization (Comment)	Organism
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

Crystallization (Comment)

Organism

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

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

Natural Substrates/ Products (Substrates)

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

Organism

Organism	UniProt	Comment	Textmining
Bacillus anthracis	Q81QQ0	gene dhbC	-
Bacillus anthracis Ames	Q81QQ0	gene dhbC	-

Purification (Commentary)

Purification (Comment)	Organism
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)

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

Subunits

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

Synonyms

Synonyms	Comment	Organism
DhbC	-	Bacillus anthracis

General Information

General Information	Comment	Organism
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
physiological function	the enzyme is essential for the biosynthesis of the siderophore bacillibactin by the pathogenic bacterium	Bacillus anthracis