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Literature summary extracted from

  • Burschowsky, D.; van Eerde, A.; Oekvist, M.; Kienhoefer, A.; Kast, P.; Hilvert, D.; Krengel, U.
    Electrostatic transition state stabilization rather than reactant destabilization provides the chemical basis for efficient chorismate mutase catalysis (2014), Proc. Natl. Acad. Sci. USA, 111, 17516-17521 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
5.4.99.5 recombinant expression of enzyme BsCM in Escherichia coli strain KA13 Bacillus subtilis

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
5.4.99.5 purified recombinant wild-type enzyme, hanging drop vapor diffusion technique, mixing of 0.001 ml of 3 mM protein in 10 mM Tris buffer, pH 7.5, 2 mM DTT, and 0.125 mM EDTA with 0.001 ml of reservoir solution containing 100 mM malic acid, Mes, Tris (MMT buffer) (in molar ratios of 1:2:2, respectively), pH 6.0, 100-150 mM MgCl2, 25% w/v PEG 1000, and 0.3 mM NaN3, at 20°C, 4-5 days, X-ray diffraction structure determination and analysis at resolution at 1.59 A resolution, molecular replacement using crystal structure PDB ID 1DBF as search model. Purified recombinant mutant enzyme Arg90Cit free or complexed with either substrate, product, or a transition state analogue, hanging drop vapor diffusion technique, mixing of 750 nl of 3 mM protein in 20 mM Tris, pH 8.0, 0.6 mM PMSF, 0.3 mM NaN3 with 750 nl of reservoir solution 100 mM MMT buffer pH 6.0, 50-150 mM CaCl2, 24-26% w/v PEG 1000, and 0.3 mM NaN3, at 20°C, 3-4 days, X-ray diffraction structure determination and analysis at resolution at 1.61-1.80 A resolution, modeling Bacillus subtilis

Protein Variants

EC Number Protein Variants Comment Organism
5.4.99.5 additional information mutant Arg90Cit, a sluggish variant of Bacillus subtilis chorismate mutase, in which a cationic active-site arginine is replaced by a neutral citrulline, is a poor catalyst even though it effectively preorganizes chorismate for the reaction Bacillus subtilis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
5.4.99.5 Chorismate Bacillus subtilis
-
 Prephenate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
5.4.99.5 Bacillus subtilis P19080
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
5.4.99.5 recombinant enzyme BsCM from Escherichia coli strain KA13 Bacillus subtilis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5.4.99.5 Chorismate
-
 Bacillus subtilis Prephenate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
5.4.99.5 BsCM
-
 Bacillus subtilis

General Information

EC Number General Information Comment Organism
5.4.99.5 malfunction mutant Arg90Cit, a sluggish variant of Bacillus subtilis chorismate mutase, in which a cationic active-site arginine is replaced by a neutral citrulline, is a poor catalyst even though it effectively preorganizes chorismate for the reaction Bacillus subtilis
5.4.99.5 physiological function the enzyme catalyzes the rearrangement of chorismate to prephenate. Calculations have predicted the decisive factor in chorismate mutase catalysis to be ground state destabilization rather than transition state stabilization Bacillus subtilis