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5.1.2.2: mandelate racemase

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

Word Map on EC 5.1.2.2

Reaction

(S)-Mandelate
=
(R)-mandelate

Synonyms

mandelate racemase, mandelic acid racemase, mdlA, MR, racemase, mandelate

ECTree

     5 Isomerases
         5.1 Racemases and epimerases
             5.1.2 Acting on hydroxy acids and derivatives
                5.1.2.2 mandelate racemase

Crystallization

Crystallization on EC 5.1.2.2 - mandelate racemase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystallographic evidence for stereospecific alkylation by (R)-alpha-phenylglycidate
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identification of the active site and possible catalytic residues at 2.5 A resolution
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mutant E317Q
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of mutant K166R
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purified recombinant homooctameric wild-type enzyme complexed with two analogues of the putative aci-carboxylate intermediate, benzohydroxamate and Cupferron, X-ray diffraction structure at 2.2 A resolution
wild-type and C92S/C264S/K166C mutant enzymes in complex with inhibitors benzilate, 3,3,3-trifluoro-2-hydroxy-2-(trifluoromethyl)-propanoate and tratronate, hanging drop vapor diffusion method, mixing of 0.002 ml of each protein and reservoir solution, the protein solution contains for 3,3,3-trifluoro-2-hydroxy-2-(trifluoromethyl)-propanoate-enzyme crystals 3.3 mM MgCl2, 1 mM inhibitor, and HEPES, 50 mM, pH 7.5, and for the reservoir solution 20% w/v, 120 mM glycine, 70 mM KNO3, and 0.1 M Tris-HCl, pH 8.0, for tartronate-enzyme crystals , 6.0 mg/ml protein, 3.3 mM MgCl2, 20 mM sodium tartronate, and 50 mM HEPES, pH 7.5, and 14% w/v PEG 1500 , 100 mM glycine, and 0.1 M triethanolamin, pH 8.5, as reservoir solution, and for mutant enzyme-benzilate crystals, mutant protein in 3.3 mM MgCl2, 20 mM benzilate, and 50 mM HEPES, pH 7.5, reservoir solution containing 15% w/v PEG 1500, 150 mM glycine, 50 mM NaCl, and 0.1 M HEPES, pH 7.5, equilibration against 0.5 ml reservoir solution, 21°C, and 50% humidity, X-ray diffraction structure determination and analysis at 1.68-1.89 A resolution
X-ray crystal structure of mandelate racemase solved at 2.5 A resolution, reveals that the sescondary, tertiary and quarternary structures of mandelate racemase and muconate lactonizing enzyme are remarkably similar
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