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2.7.1.71: shikimate kinase

This is an abbreviated version!
For detailed information about shikimate kinase, go to the full flat file.

Word Map on EC 2.7.1.71

Reaction

ATP
+
shikimate
=
ADP
+
3-phosphoshikimate

Synonyms

adenosine triphosphate: shikimate-3-phosphotransferase, AroK, AroL, AtSK1, AtSK2, kinase (phosphorylating), shikimate, kinase, shikimate (phosphorylating), MtSK, OsSK1, OsSK2, OsSK3, Rv2539c, shikimate kinase II, shikimate kinase-like 1, SK I, SK II, SK1, SK2, SKI, SKII, SKL1, type I shikimate kinase, aroK-encoded, type II shikimate kinase

ECTree

     2 Transferases
         2.7 Transferring phosphorus-containing groups
             2.7.1 Phosphotransferases with an alcohol group as acceptor
                2.7.1.71 shikimate kinase

Crystallization

Crystallization on EC 2.7.1.71 - shikimate kinase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
in complex with shikimate, microbatch-under-oil method and sitting-drop vapor diffusion method using 0.1 M HEPES pH 7.5, 1.5 M lithium sulfate
heat-stable isozyme AtSK2, X-ray diffraction structure determinaion and analysis at 2.35 A resolution
structural model based on structure of Mycobacterium tuberculosis enzyme. Molecular modeling and molecular dynamics simulation. Substrate shikimate binds to a pocket formed by the conserved residues Asp33, Arg57, Gly78 and Gly79, and Arg135
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mutant enzyme K15M, sitting-drop vapor diffusion
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vapor-diffusion method using NaCl as precipitant
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hanging drop vapour diffusion method using containing 0.2 M lithium sulfate, 30% (wt/vol) PEG 8000, and 0.1 M sodium acetate buffer (pH 6.5), at 20°C
hanging-drop vapor diffusion method. 1.8 A crystal structure of shikimate kinase. The crystal structure shows a three-layer alpha/beta fold consisting of a central sheet of five parallel beta-strands flanked by seven alpha-helices. An HpSK-shikimate-PO4 complex is also determined and refined to 2.3 A, revealing induced-fit movement from an open to a closed form on substrate binding
molecular modeling and docking of inhibitors. The active site is rather roomy and deep, forming an L-shape channel on the surface of the protein, and compound 3-methoxy-4-[[2-([2-methoxy-4-[(4-oxo-2-thioxo-1,3-thiazolidin-5-ylidene)methyl]phenoxy]methyl)benzyl]oxy]benzaldehyde prefers the corner area of L-shape channel, while compound 5-bromo-2-(5-[[1-(3,4-dichlorophenyl)-3,5-dioxo-4-pyrazolidinylidene]methyl]-2-furyl)benzoic acid binds the short arm of the channel in the binding interactions
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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
crystal structure of the enzyme complexed with MgADP and shikimic acid, determined at 2.3 A resolution, hanging-drop vapor-diffusion method
crystal structure of the enzyme in complex with MgADP- determined at 1.8 A resolution
hanging drop vapour diffusion method
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hanging drop vapour diffusion method, enzyme in complex with ADP and shikimate in the absence of Mg2+ using 0.1 M Tris-HCl buffer pH 8.0, 17% PEG 1500 and 0.5-0.7 M LiCl, or enzyme in complex with ADP and Mg2+ in the absence of shikimate using 0.1 M Tris-HCl buffer pH 8.0, 20% PEG 3350 and 0.1 M MgCl2*6H2O
hanging-drop vapour-diffusion method. Crystal structure of shikimate kinase complexed with MgADP and shikimate determined at 2.3 A resolution
-
in complex with ADP and inhibitor, sitting drop vapor diffusion method, using 20% (w/v) poly(ethyleneglycol) 3350, 0.5 M LiCl, and 100 mM Tris-HCl pH 7.8
in complex with ADP-shikimate and with MgADP-, at 1.93 A and 2.8 A resolution, respectively. Presence of Mg2+ influences the conformation of the shikimate hydroxyl groups and the position of the side chains of some of the residues of the activesite. Presence of Cl- seems to influence the affinity of ADP and its position in the active site and the opening length of the LID domain. Shikimate binding causes a closing of the LID domain and also seems to influence the crystallographic packing
sitting drop vapour diffusion method using 0.2 M ammonium sulfate and 30% (w/v) poly(ethylene glycol) monomethyl ether 5000 in 0.1 M MES (pH 6.5) buffer
X-ray crystal structure of shikimate kinase with bound shikimate and adenosine diphosphate determined to a resolution of 2.15 A, sitting drop vapor diffusion method
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