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1.2.7.11: 2-oxoacid oxidoreductase (ferredoxin)

This is an abbreviated version!
For detailed information about 2-oxoacid oxidoreductase (ferredoxin), go to the full flat file.

Word Map on EC 1.2.7.11

Reaction

a 2-oxocarboxylate
+
CoA
 + 2 oxidized ferredoxin =
an acyl-CoA
 +
CO2
 + 2 reduced ferredoxin + 2 H+

Synonyms

2-ketoacid:ferredoxin oxidoreductase, 2-oxoacid: ferredoxin oxidoreductase, 2-oxoacid:ferredoxin oxidoreductase, 2-oxoacid:ferredoxin oxidoreductases, Ape1473/1472, KOR, OFOR, OFOR1, OFOR2, PFOR, Saci_2306, Saci_2307, StOFOR, StOFOR1, StOFOR2

ECTree

     1 Oxidoreductases
         1.2 Acting on the aldehyde or oxo group of donors
             1.2.7 With an iron-sulfur protein as acceptor
                1.2.7.11 2-oxoacid oxidoreductase (ferredoxin)

Crystallization

Crystallization on EC 1.2.7.11 - 2-oxoacid oxidoreductase (ferredoxin)

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystals are grown at 20°C using sitting drop vapor diffusion. The structure of the recombinant enzyme StOFOR2 by the single-wavelength anomalous dispersion method is solved using a selenomethionine(SeMet)-labeled protein crystal, and the structures of the ligand-free (2.1 Å resolution) and pyruvate-complexed (2.2 Å) forms are determined. In the structure of the recombinant enzyme StOFOR2 in unreacted pyruvate complex form, the carboxylate group of pyruvate is recognized by Arg344 and Thr257 from the alpha-subunit. The binding pockets of the 2-oxoacid oxidoreductase enzymes from Sulfolobus tokodaii surrounding the methyl or propyl group of the ligands are wider than that of 2-oxoacid oxidoreductase enzymes from Desulfovbrio africanus. A possible complex structural model is constructed by placing a Zn2+-containing dicluster ferredoxin of Sulfolobus tokodaii into the large pocket of the recombinant StOFOR2 enzyme, providing insight into the electron transfer between the two redox proteins
crystals of the StOFOR1 enzyme are prepared by co-crystallization with 50 mM 2-oxobutyrate and 1 mM CoA. Crystals are grown at 25°C using sitting drop vapor diffusion. In the structure of StOFOR1 co-crystallized with 2-oxobutyrate, electron density corresponding to a 1-hydroxypropyl group (post-decarboxylation state) is observed at the thiazole ring of thiamine diphosphate. The binding pockets of the 2-oxoacid oxidoreductase enzymes from Sulfolobus tokodaii surrounding the methyl or propyl group of the ligands are wider than that of 2-oxoacid oxidoreductase enzymes from Desulfovbrio africanus
sitting drop vapor diffusion method, using 0.7 M ammonium tartrate dibasic and 0.1 M Tris-HCl (pH 8.5)
sitting drop vapor diffusion method, using 15% (w/v) PEG3350, 0.1 M Tris-HCl (pH 8.5) and 0.1 M NaBr