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1.3.1.6: fumarate reductase (NADH)

This is an abbreviated version!
For detailed information about fumarate reductase (NADH), go to the full flat file.

Word Map on EC 1.3.1.6

Reaction

succinate
+
NAD+
=
fumarate
 +
NADH
 +
H+

Synonyms

ABB37_00293, FRD, FRdABCD, FRDg, FRDm1, FRDm2, FRDS, Frds1p, fumarate reductase, KPA86010, KPK_2907, mitochondrial rhodoquinol-fumarate reductase, NADH-dependent fumarate reductase, NADH-FR, NADH-FRD, NADH-fumarate reductase, NFRD, QFR

ECTree

     1 Oxidoreductases
         1.3 Acting on the CH-CH group of donors
             1.3.1 With NAD+ or NADP+ as acceptor
                1.3.1.6 fumarate reductase (NADH)

Crystallization

Crystallization on EC 1.3.1.6 - fumarate reductase (NADH)

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystallized in the presence of octaethyleneglycol monododecyl ether and n-dodecyl-beta-D-maltopyranoside in a 3:2 weight ratio, crystals belongs to a orthorhombic space group with unit-cell parameters a=123.75 A, b= 29.08 A and c=221.12 A, diffracted to 2.8 A resolution using synchrotron radiation
-
mutant enzyme H505A and H505Y, hanging drop vapour diffusion method, protein solution: 6 mg/ml, 10 mM Tris-HCl, pH 8.5, well solution: 100 mM Tris-HCl, pH 7.4-8.2, 25°C, 80 mM NaCl, 16-19% PEG 8000, 10 mM fumarate, equal volume of 0.002 ml of protein solution and well solution, 10 days, cryoprotectant solution: 100 mM sodium acetate, pH 6.5, 20% PEG 8000, 10 mM fumarate, 80 mM NaCl, and 23% glycerol, X-ray diffraction structure determination and analysis at 1.8 A and 2.0 A resolution, respectively, molecular replacement
-
mutant enzyme H61A and H61M, hanging drop vapour diffusion method, protein solution: 6 mg/ml, 10 mM Tris-HCl, pH 8.5, well solution: 100 mM Tris-HCl, pH 7.4-8.5, 4°C, 80 mM NaCl, 16-19% PEG 8000, 10 mM fumarate, equal volume of 0.002 ml of protein solution and well solution, 10 days, cryoprotectant solution: 100 mM sodium acetate, pH 6.5, 20% PEG 8000, 10 mM fumarate, 80 mM NaCl, and 23% glycerol, X-ray diffraction structure determination and analysis at 2.1 A and 2.2 A resolution, respectively, molecular replacement
-