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2.2.1.9: 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid synthase

This is an abbreviated version!
For detailed information about 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid synthase, go to the full flat file.

Word Map on EC 2.2.1.9

Reaction

isochorismate
+
2-oxoglutarate
=
5-enolpyruvoyl-6-hydroxy-2-succinyl-cyclohex-3-ene-1-carboxylate
 +
CO2

Synonyms

(1R,2S,5S,6S)-2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase, (1R,2S,5S,6S)-2-succinyl-5-enolpyruvyl-6-hydroxycyclohex-3-ene-1-carboxylate synthase, 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexadiene-1-carboxylate synthase, 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase, 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic acid synthase, EC 2.5.1.64, EcMenD, MenD, Rv0555, SEPHCHC synthase, SHCHC synthase

ECTree

     2 Transferases
         2.2 Transferring aldehyde or ketonic groups
             2.2.1 Transketolases and transaldolases
                2.2.1.9 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid synthase

Crystallization

Crystallization on EC 2.2.1.9 - 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid synthase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
to 2.35 A resolution, in complex with thiamine diphosphate and Mn2+. basic residues Arg32, Arg106, Arg409, Arg428, and Lys299 interact with carboxylate and hydroxyl groups to align substrates for catalysis in combination with a cluster of the non-polar residues Ile489, Phe490, and Leu493 on one side of the active site. Arg409 plays a significant role in binding both substrates while Arg428 contributes mainly to binding of 2-oxoglutarate. Arg32 and in particular Arg106 are critical for recognition of isochorismate
crystallization of the apoenzyme and holoenzyme forms of MenD. The apoenzyme crystals are obtained by sitting-drop vapour diffusion with 70% MPD. The crystals are too small to collect diffraction data and a search for better conditions is not successful. Single crystals of the holoenzyme with thiamin diphosphate and Mn2+ as cofactors are obtained by the hanging-drop vapour-diffusion method with 35% ethylene glycol as precipitant. Diffraction data are collected on a cryocooled crystal to a resolution of 2.0 A
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mutant enzyme R395K bound to thiamine diphosphate, hanging drop vapor diffusion method, using 0.2 M ammonium acetate, 0.06 M magnesium formate, 3% (w/v) polyethylene glycol 3350, and 12% (w/v) polyethylene glycol 10000 in 0.1 M Tris-HCl (pH 7.5). Mutant enzyme R395A bound to thiamine diphosphate, hanging drop vapor diffusion method, using 30% (v/v) Jeffamine M-600 (pH 7.0), 11.2% (w/v) polyethylene glycol 3350 and 0.16 M magnesium formate in 0.1 M HEPES (pH 7.5). Mutant enzyme R413A bound to thiamine diphosphate, hanging drop vapor diffusion method, using 0.16 M magnesium formate, 1% (w/v) tacsimate (pH 7.0), 14% (w/v) polyethylene glycol 3350, and 2% (w/v) polyethylene glycol MME 5000 in 0.02 M HEPES (pH 7.0)
purified recombinant enzyme complexed with its tetrahedral reaction intermediate, X-ray diffraction structure determination and analysis
sitting and hanging vapor diffusion method, hexagonal complex with thiamine diphosphate and Mn2+
tetragonal crystal form
apoenzyme and in complex with thiamine diphosphate and Mg2+, sitting drop vapor diffusion method
sitting drop vapor diffusion method, using 0.1 M MOPS/HEPES, pH 7.5, 20% (v/v) glycerol, 8% (w/v) PEG 4000, and a 0.02 M mixture of sodium formate, ammonium acetate, sodium citrate tribasic dihydrate, sodium oxamate, and potassium sodium tartrate tetrahydrate
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