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Literature summary extracted from

  • Cheng, W.C.; Chen, Y.F.; Wang, H.J.; Hsu, K.C.; Lin, S.C.; Chen, T.J.; Yang, J.M.; Wang, W.C.
    Structures of Helicobacter pylori shikimate kinase reveal a selective inhibitor-induced-fit mechanism (2012), PLoS ONE, 7, e33481.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.7.1.71 wild-type dimeric enzyme, wild-type enzyme in complex with products ADP and shikimate 3-phosphate, enzyme mutant R57A, and enzyme mutant E114A in complex with selective inhibitor NSC162535, hanging drop vapour ddiffusion metho, 50 mg/ml protein in 40 mM Tris-HCl, pH 7.0, containing 100 mM NaCl mixed with an equal volume of reservoir solution and equilibrated against 0.06 ml of reservoir solution, containing 0.2 M Li2SO4, 30% w/v PEG 8000, and 0.1 M sodium acetate, pH 6.5 for the apo-enzyme, or containing 0.1 M HEPES sodium salt, pH 7.5, 0.1 M sodium acetate, 18% w/v PEG 8000, 2% w/v 2-propanol, and 5 mM shikimate and 5 mM MgATP for the product complex enzyme, or containing 0.1 M HEPES sodium salt, pH 8.0, 8% w/v 2-propanol and 18% w/v PEG 4000 for enzyme mutant R57A, or containing 0.1 M HEPES sodium salt, pH 6.7, and 1.2 M potassium sodium tartrate tetrahydrate for the enzyme mutant E114A with inhibitor, X-ray diffraction structure determination and analysis at 1.8 A, 2.3 A, 2.4 A, and 2.53 A resolution, respectively, molecular replacement Helicobacter pylori

Protein Variants

EC Number Protein Variants Comment Organism
2.7.1.71 D33A site-directed mutagensis, inactive mutant Helicobacter pylori
2.7.1.71 D33E site-directed mutagensis, inactive mutant Helicobacter pylori
2.7.1.71 E114A site-directed mutagensis, the mutant shows 82% of wlld-type activity Helicobacter pylori
2.7.1.71 F48A site-directed mutagensis, inactive mutant Helicobacter pylori
2.7.1.71 F48Y site-directed mutagensis, the mutant shows 40% of wlld-type activity Helicobacter pylori
2.7.1.71 M10A site-directed mutagensis, the mutant shows 38% of wlld-type activity Helicobacter pylori
2.7.1.71 R116A site-directed mutagensis, inactive mutant Helicobacter pylori
2.7.1.71 R116K site-directed mutagensis, inactive mutant Helicobacter pylori
2.7.1.71 R132A site-directed mutagensis, the mutant shows 5% of wlld-type activity Helicobacter pylori
2.7.1.71 R132K site-directed mutagensis, inactive mutant Helicobacter pylori
2.7.1.71 R57A site-directed mutagensis, the mutant shows 2% of wlld-type activity Helicobacter pylori
2.7.1.71 R57K site-directed mutagensis, the mutant shows 2% of wlld-type activity Helicobacter pylori

General Stability

EC Number General Stability Organism
2.7.1.71 differential scanning calorimetry experiments for evaluaton of the stability and unfolding of each of the enzyme mutants, overview Helicobacter pylori

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.7.1.71 NSC162535 selective inhibitor, identification and binding analysis with enzyme mutant E144A by virtual docking analysis, isothermal titration calorimetry, and crystals structure analysis revealing an induced-fit mechanism, inactivation mechanism, detailed overview. Binding kinetics of wild-type and mutant enzymes Helicobacter pylori

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.7.1.71 0.039
-
 shikimate enzyme mutant E114A, pH 7.5, 25°C Helicobacter pylori
2.7.1.71 0.06
-
 shikimate wild-type enzyme, pH 7.5, 25°C Helicobacter pylori
2.7.1.71 0.101
-
 ATP wild-type enzyme, pH 7.5, 25°C Helicobacter pylori
2.7.1.71 0.101
-
 ATP enzyme mutant M10A, pH 7.5, 25°C Helicobacter pylori
2.7.1.71 0.135
-
 shikimate enzyme mutant M10A, pH 7.5, 25°C Helicobacter pylori
2.7.1.71 0.143
-
 ATP enzyme mutant E114A, pH 7.5, 25°C Helicobacter pylori
2.7.1.71 0.231
-
 ATP enzyme mutant F48Y, pH 7.5, 25°C Helicobacter pylori
2.7.1.71 0.291
-
 shikimate enzyme mutant F48Y, pH 7.5, 25°C Helicobacter pylori

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.1.71 Mg2+ required Helicobacter pylori

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.1.71 ATP + shikimate Helicobacter pylori
-
 ADP + 3-phosphoshikimate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.7.1.71 Helicobacter pylori P56073
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.1.71 ATP + shikimate
-
 Helicobacter pylori ADP + 3-phosphoshikimate
-
 ?

Subunits

EC Number Subunits Comment Organism
2.7.1.71 dimer detailed structure-activity relationship analysis, overview Helicobacter pylori

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.7.1.71 25
-
 assay at Helicobacter pylori

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.7.1.71 7.5
-
 assay at Helicobacter pylori

Cofactor

EC Number Cofactor Comment Organism Structure
2.7.1.71 ATP
-
 Helicobacter pylori

IC50 Value

EC Number IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
2.7.1.71 0.0049
-
 pH 7.5, 25°C Helicobacter pylori NSC162535

General Information

EC Number General Information Comment Organism
2.7.1.71 metabolism shikimate kinase catalyzes the fifth step of the shikimate pathway for biosynthesis of aromatic amino acids Helicobacter pylori
2.7.1.71 additional information detailed structure-activity relationship analysis, overview. The critical conserved residues D33, F48, R57, R116, and R132 interact with shikimate. A characteristic three-layer architecture and a conformationally elastic region consisting of F48, R57, R116, and R132 are occupied by shikimate Helicobacter pylori