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Literature summary for 1.1.1.383 extracted from

  • Cahn, J.K.; Brinkmann-Chen, S.; Spatzal, T.; Wiig, J.A.; Buller, A.R.; Einsle, O.; Hu, Y.; Ribbe, M.W.; Arnold, F.H.
    Cofactor specificity motifs and the induced fit mechanism in Class I ketol-acid reductoisomerases (2015), Biochem. J., 468, 475-484.
    View publication on PubMedView publication on EuropePMC
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Crystallization (Commentary)

Crystallization (Comment) Organism
with metal ions (Mg2+ and Fe2+) bound in the active site, but without a cofactor or a substrate analogue. The enzyme has a seven-residue NADPH-dependent beta2alphaB specificity loop. Residues Lys130, Asp190 and Glu226' undergo rotamer changes upon metal binding Azotobacter vinelandii

Organism

Organism UniProt Comment Textmining
Azotobacter vinelandii C1DFH7 cf. EC 1.1.1.86
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Azotobacter vinelandii ATCC BAA-1303 C1DFH7 cf. EC 1.1.1.86
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Synonyms

Synonyms Comment Organism
ilvC
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 Azotobacter vinelandii

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
95
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 half-maximal residual activity at 95°C Azotobacter vinelandii