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4.2.1.11: phosphopyruvate hydratase

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

Word Map on EC 4.2.1.11

Reaction

2-phospho-D-glycerate
=
phosphoenolpyruvate
 +
H2O

Synonyms

14-3-2 protein, 2-phospho-D-glycerate hydro-lyase, 2-phospho-D-glycerate hydrolase, 2-phospho-D-glycerate hydrolyase, 2-phospho-D-glyceratehydrolyase, 2-phosphoglycerate dehydratase, 2-phosphoglycerate enolase, 2-phosphoglycerate hydrolase, 2-phosphoglycerate hydrolyase, 2-phosphoglyceric dehydratase, 2-phosphopyruvate hydrolyase, alpha,alpha-enolase, alpha-enolase, alpha-enolase 1, alpha-enolase 2, Alt a XI, beta,beta-enolase, beta-enolase, Cla h VI, Csenolase, cytotoxin B, EhENO, ENO, ENO-1, Eno-alpha, ENO-S, ENO1, Eno1p, Eno2, ENOA, EnoA I, EnoA1, ENOL, Enol-1, enolase, enolase 1, enolase 2, enolase alpha, enolase gamma, enolase S, enolase-1, enolase-alpha, enolase-beta, Enolase-phosphatase E1, enolase2p, Err2p, Err3p, gamma,gamma-enolase, gamma-enolase, hENO1, HLE1, human alpha-enolase, human neuron-specific enolase, hydratase, phosphoenolpyruvate, Laminin binding protein, Major allergen Alt a 11, MASA, MSE, Neural enolase, neuron specific enolase, neuron-specific enolase, neuronal enolase, NNE, Non-neural enolase, NSE, OSE1, p45, P46, Pfen, Pfeno, phosphoenolpyruvate enolase, phosphoenolpyruvate hydratase, Phosphopyruvate hydratase, plasminogen-binding alpha-enolase, R-NSE, r-Pfen, rBaEn, rSsEno, SEN, SjENO, Skeletal muscle enolase, SPM2, SsEno, SSO0913, streptococcal surface enolase, Tau-crystallin, tv-ENO1, tv-rENO1, XEP, yeast enolase

ECTree

     4 Lyases
         4.2 Carbon-oxygen lyases
             4.2.1 Hydro-lyases
                4.2.1.11 phosphopyruvate hydratase

Crystallization

Crystallization on EC 4.2.1.11 - phosphopyruvate hydratase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
to 2.0 A resolution, space group R32. Enzyme forms a homodimer with conserved residues in the dimer interface
purified recombinant EhENO with two 2-phospho-D-glycerate substrate molecules bound at the two active sites, the protein solution contains 7.5 mg/ml protein in 100 mM Tris-HCl pH 7.5, 100 mM NaCl, 5 mM MgCl2, sitting-drop vapour-diffusion, 20°C, mixing of equal volumes of precipitant solution, contraining 100 mM Bis-Tris, pH 5.5, 25% w/v PEG 3350, 200 mM ammonium sulfate, and protein solution, X-ray diffractrion structure determination and analysis at 1.9 A resolution, molecular replacement
using the hanging drop method followed by recrystallization under the same conditions, X-ray structure solved by molecular replacement
1.6 A resolution, co-crystallization of enolase with a synthetic peptide corresponding to residues 833 to 850 from RNase E determined, asymmetric binding of a single molecule of RNase E to a conserved cleft at the interface of the enolase dimer
using the sitting drop method, co-crystallized with Mg2+
-
hanging drop method, 17 A resolution, X-ray coordinates and structure factors determined, complexes with phosphate, with Mg2+, with Mg2+ and HCO3-, with Mg2+ and the alternate substrate 2,3-diketohexane 1-phosphate identified, activated enolase carboxylated on Lys173, conserved Lys98 in the N-terminal domain determined for C1 proton abstraction
1.7 A resolution by multiwavelength anomalous diffraction and molecular replacement techniques
-
asymmetric complex NSE*Mg2SO4/NSE*MgCl, pH 7.0, large orthorhombic plates, structure by molecular replacement
-
at room temperature using the hanging-drop vapour-diffusion method for structure analysis by X-ray diffraction
enolase fluoride/phosphate inhibitory complex and enolase phosphate inhibitory complex
hanging drop vapor diffusion method, using 0.1 M ammonium acetate, 0.1 M bis-tris pH 5.5, 20% (w/v) polyethylene glycol monomethyl ether 2000
hanging drop vapor diffusion method, using 20% (w/v) PEG 550, 100 mM bicine pH 9.0, 100 mM sodium chloride
hanging drop method, from preparations of purified dextransucrase
co-crystallization of the S39A mutant with Mg2+ and phosphonoacetohydroxamate, the active-site flap is opened
-
crystal structure of asymmetric dimer enolase-2-phospho-D-glycerate/enolase-phosphoenolpyruvate at 2.0 A resolution
engineered K345A/N80D/N126D heterodimer in complex with substrate/product, 1.85A resolution, batch method
mutant E211Q complexed with Mg2+ and phosphoenolpyruvate, mutant E168Q complexed with Mg2+ and 2-phospho-D-glycerate
structure of enolase-Zn2+/Mn2+ complex formation with phosphonoacetohydroxamate solved to 1.54 A resolution by X-ray crystallography, replacement of native Mg2+ ions with Mn2+/Zn2+ introduces only minor atom displacements in the binding site, crystallographic data refined, simulations reveal a model of the enolase active site chosen for the study indicating sites MI and MII either occupied with Mn2+ at site MI and Zn2+ at site MII or vice versa, stereo view of the coordination of the two metal ions in the enolase-inhibitor-complex and of key active site residues presented, rotation patterns shown
2.0 A resolution, molecular replacement, hanging-drop vapor-diffusion
hanging drop vapor diffusion method, using 0.1 M MES (pH 6.5) and 10% (w/v) PEG 20000
to 2.75 A resolution. Residue Glu164 in catalytic loop 2 may account for the comparatively lower activity of this isozyme
hanging drop method
hanging drop method, six novel crystal structures with various ligation states and conformations identified, high structural diversity of loops near the catalytic site determined, novel metal-binding site within the catalytic site identified