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1.1.1.379: (R)-mandelate dehydrogenase

This is an abbreviated version!
For detailed information about (R)-mandelate dehydrogenase, go to the full flat file.

Word Map on EC 1.1.1.379

Reaction

(R)-mandelate
+
NAD+
=
phenylglyoxylate
+
NADH
+
H+

Synonyms

D(-)-mandelate dehydrogenase, D-mandelate dehydrogenase, D-ManDH, D-ManDH2, DMDH, LhDMDH, ManDH2, NAD+-dependent D-mandelate dehydrogenase, NAD-dependent D-mandelate dehydrogenase

ECTree

     1 Oxidoreductases
         1.1 Acting on the CH-OH group of donors
             1.1.1 With NAD+ or NADP+ as acceptor
                1.1.1.379 (R)-mandelate dehydrogenase

Crystallization

Crystallization on EC 1.1.1.379 - (R)-mandelate dehydrogenase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified enzyme in complex with substrates NADH and anilino(oxo)acetate (AOA), hanging-drop vapor diffusion method, mixing of 10 mg/ml protein in 5 mM sodium MOPS, pH 7.5, 2 mM NADH, and 20 mM AOA with reservoir solution containing 0.1 M cacodylate-Na, pH 5.0, 0.17 M ammonium sulfate, and 22.5% PEG 8000, in a 1:1 ratio, at 25°C, X-ray diffraction structure determination and analysis at 2.4 A resolution, molecular replacement using the crystal structure of unliganded D-ManDH2 (PDB ID 3WFI) as a search model, modeling. The ternary complex of D-ManDH2 forms a 2fold symmetric homodimer in a crystallographic asymmetric unit, as in the cases of the apo and binary complex structures
-
the enzyme is crystallized in three different forms using the hanging drop vapour diffusion method at 15-20°C. Type I crystals belong to space group P222(1), P22(1)2(1) or P2(1)2(1)2(1) with a = 100.3 A, b = 117.4 A, c = 80.4 A and are likely to contain a dimer in the crystallographic asymmetric unit