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Literature summary extracted from

  • Tyagi, R.; Duquerroy, S.; Navaza, J.; Guddat, L.W.; Duggleby, R.G.
    The crystal structure of a bacterial class II ketol-acid reductoisomerase: domain conservation and evolution (2005), Protein Sci., 14, 3089-3100.
    View publication on PubMedView publication on EuropePMC


EC Number Cloned (Comment) Organism expression as His6-tagged enzyme Escherichia coli

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism purified recombinant His-tagged enzyme, 9 mg/ml protein in 20 mM sodium HEPES, pH 7.5, and NADPH in a ratio of 10 mol NADPH per mol of enzyme, hanging drop vapour diffusion method, equal volumes of 0.003 ml of protein and reservoir solution, the latter containing 1.6 M ammonium sulfate, and 0.1 M sodium bicine, pH 9.0, 17°C, 6 months, X-ray diffraction structure determination and analysis at 2.6 A resolution Escherichia coli


EC Number Organism UniProt Comment Textmining Escherichia coli

Purification (Commentary)

EC Number Purification (Comment) Organism recombinant His6-tagged enzyme Escherichia coli


EC Number Reaction Comment Organism Reaction ID (2R)-2,3-dihydroxy-3-methylbutanoate + NADP+ = (2S)-2-hydroxy-2-methyl-3-oxobutanoate + NADPH + H+ active site structure Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac. (R)-2,3-dihydroxy-3-methylbutanoate + NADP+ the enzyme is involved in biosynthesis of the branched chain amino acids valine and leucine, pathway overview Escherichia coli (S)-2-hydroxy-2-methyl-3-oxobutanoate + NADPH


EC Number Subunits Comment Organism tetramer three-dimensional enzyme structure, subunit domain structures, surface contact and interlock, crystal structure analysis, overview Escherichia coli


EC Number Synonyms Comment Organism class II ketol-acid reductoisomerase
Escherichia coli KARI
Escherichia coli


EC Number Cofactor Comment Organism Structure NADP+
Escherichia coli