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Literature summary 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

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.1.1.86 hanging drop vapor diffusion method, using 0.1 M bis-Tris, pH 5.0, 20% (w/v) w/v polyethylene glycol 1500 uncultured archaeon
1.1.1.86 hanging drop vapor diffusion method, using 0.1 M bis-Tris, pH 6.0, 22% (w/v) polyethylene glycol monomethylether 5000 Ignisphaera aggregans
1.1.1.86 hanging drop vapor diffusion method, using 0.25 M NaCl, 28% (w/v) polyethylene glycol 3350 and 0.1 M bis-Tris, pH 5.5 Azotobacter vinelandii
1.1.1.86 hanging drop vapor diffusion method, using 1 M sodium potassium tartrate, 200 mM sodium chloride, 100 mM imidazole pH 8.0 Alicyclobacillus acidocaldarius subsp. acidocaldarius
1.1.1.86 in complex with NADPH and the transition state analogue N-isopropyloxamate and apo-form. The enzyme has a seven-residue specificity loop Ignisphaera aggregans
1.1.1.382 apo-enzyme, to 1.39 A resolution, and in complex with NADP+. Enzyme accepts both cofactors NADH and NADPH. Insertions near the N-terminus of the specificity loop probably determine cofactor specificity, the laboratory engineering of NADH preference involved specific loop substitution Ignisphaera aggregans
1.1.1.382 in complex with NADH, to 1.54 A resolution. The specificity loop differs significantly from any other crystallized ketol-acid reductoisomerases. Glu46, the first residue of the beta2alphaB-loop, lies along the N3 edge of the adenine moiety and forms a bi-dentate interaction with the O2' hydroxy of the ribose. The position of this glutamate is stabilized by a hydrogen bond interaction with Asn55 uncultured archaeon
1.1.1.382 in complex with substrate analog L-tartaric acid, to 2.5 A resolution. The enzyme displays a six-member specificity loop, with residues Arg48 and Ser52 forming hydrogen bonds to the NAD(H) phosphate Alicyclobacillus acidocaldarius subsp. acidocaldarius
1.1.1.382 to 1.54 A resolution. Structure contains 2 Mg2+ ions and NADH. Glu46, the first residue of the beta2alphaB-loop, lies along the N3 edge of the adenine moiety and forms a bi-dentate interaction with the O2 hydroxy of the ribose. The position of this glutamate is stabilized by a hydrogen bond interaction with Asn55 uncultured archaeon GZfos26G2
1.1.1.383 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

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.1.1.86 Mg2+ required Ignisphaera aggregans
1.1.1.86 Mg2+ required Azotobacter vinelandii
1.1.1.86 Mg2+ required Alicyclobacillus acidocaldarius subsp. acidocaldarius
1.1.1.86 Mg2+ required uncultured archaeon

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.1.86 (S)-2-acetolactate + NADH + H+ Ignisphaera aggregans
-
 (R)-2,3-dihydroxyisovalerate + NAD+
-
 r
1.1.1.86 (S)-2-acetolactate + NADH + H+ Azotobacter vinelandii
-
 (R)-2,3-dihydroxyisovalerate + NAD+
-
 r
1.1.1.86 (S)-2-acetolactate + NADH + H+ Alicyclobacillus acidocaldarius subsp. acidocaldarius
-
 (R)-2,3-dihydroxyisovalerate + NAD+
-
 r
1.1.1.86 (S)-2-acetolactate + NADH + H+ uncultured archaeon
-
 (R)-2,3-dihydroxyisovalerate + NAD+
-
 r
1.1.1.86 (S)-2-acetolactate + NADH + H+ Ignisphaera aggregans DSM 17230
-
 (R)-2,3-dihydroxyisovalerate + NAD+
-
 r
1.1.1.86 (S)-2-acetolactate + NADH + H+ Azotobacter vinelandii ATCC BAA-1303
-
 (R)-2,3-dihydroxyisovalerate + NAD+
-
 r
1.1.1.86 (S)-2-acetolactate + NADPH + H+ Ignisphaera aggregans
-
 (R)-2,3-dihydroxyisovalerate + NADP+
-
 r
1.1.1.86 (S)-2-acetolactate + NADPH + H+ Azotobacter vinelandii
-
 (R)-2,3-dihydroxyisovalerate + NADP+
-
 r
1.1.1.86 (S)-2-acetolactate + NADPH + H+ Alicyclobacillus acidocaldarius subsp. acidocaldarius
-
 (R)-2,3-dihydroxyisovalerate + NADP+
-
 r
1.1.1.86 (S)-2-acetolactate + NADPH + H+ uncultured archaeon
-
 (R)-2,3-dihydroxyisovalerate + NADP+
-
 r
1.1.1.86 (S)-2-acetolactate + NADPH + H+ Ignisphaera aggregans DSM 17230
-
 (R)-2,3-dihydroxyisovalerate + NADP+
-
 r
1.1.1.86 (S)-2-acetolactate + NADPH + H+ Azotobacter vinelandii ATCC BAA-1303
-
 (R)-2,3-dihydroxyisovalerate + NADP+
-
 r

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.86 Alicyclobacillus acidocaldarius subsp. acidocaldarius C8WR67
-
-
1.1.1.86 Azotobacter vinelandii C1DFH7
-
-
1.1.1.86 Azotobacter vinelandii ATCC BAA-1303 C1DFH7
-
-
1.1.1.86 Ignisphaera aggregans E0SRA9
-
-
1.1.1.86 Ignisphaera aggregans DSM 17230 E0SRA9
-
-
1.1.1.86 uncultured archaeon Q64BR7
-
-
1.1.1.382 Alicyclobacillus acidocaldarius subsp. acidocaldarius C8WR67 cf. EC 1.1.1.86
-
1.1.1.382 Ignisphaera aggregans E0SRA9
-
-
1.1.1.382 Ignisphaera aggregans DSM 17230 E0SRA9
-
-
1.1.1.382 uncultured archaeon Q64BR7 cf. 1.1.1.86
-
1.1.1.382 uncultured archaeon GZfos26G2 Q64BR7
-
-
1.1.1.383 Azotobacter vinelandii C1DFH7 cf. EC 1.1.1.86
-
1.1.1.383 Azotobacter vinelandii ATCC BAA-1303 C1DFH7 cf. EC 1.1.1.86
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.86 (S)-2-acetolactate + NADH + H+
-
 Ignisphaera aggregans (R)-2,3-dihydroxyisovalerate + NAD+
-
 r
1.1.1.86 (S)-2-acetolactate + NADH + H+
-
 Azotobacter vinelandii (R)-2,3-dihydroxyisovalerate + NAD+
-
 r
1.1.1.86 (S)-2-acetolactate + NADH + H+
-
 Alicyclobacillus acidocaldarius subsp. acidocaldarius (R)-2,3-dihydroxyisovalerate + NAD+
-
 r
1.1.1.86 (S)-2-acetolactate + NADH + H+
-
 uncultured archaeon (R)-2,3-dihydroxyisovalerate + NAD+
-
 r
1.1.1.86 (S)-2-acetolactate + NADH + H+
-
 Ignisphaera aggregans DSM 17230 (R)-2,3-dihydroxyisovalerate + NAD+
-
 r
1.1.1.86 (S)-2-acetolactate + NADH + H+
-
 Azotobacter vinelandii ATCC BAA-1303 (R)-2,3-dihydroxyisovalerate + NAD+
-
 r
1.1.1.86 (S)-2-acetolactate + NADPH + H+
-
 Ignisphaera aggregans (R)-2,3-dihydroxyisovalerate + NADP+
-
 r
1.1.1.86 (S)-2-acetolactate + NADPH + H+
-
 Azotobacter vinelandii (R)-2,3-dihydroxyisovalerate + NADP+
-
 r
1.1.1.86 (S)-2-acetolactate + NADPH + H+
-
 Alicyclobacillus acidocaldarius subsp. acidocaldarius (R)-2,3-dihydroxyisovalerate + NADP+
-
 r
1.1.1.86 (S)-2-acetolactate + NADPH + H+
-
 uncultured archaeon (R)-2,3-dihydroxyisovalerate + NADP+
-
 r
1.1.1.86 (S)-2-acetolactate + NADPH + H+
-
 Ignisphaera aggregans DSM 17230 (R)-2,3-dihydroxyisovalerate + NADP+
-
 r
1.1.1.86 (S)-2-acetolactate + NADPH + H+
-
 Azotobacter vinelandii ATCC BAA-1303 (R)-2,3-dihydroxyisovalerate + NADP+
-
 r

Synonyms

EC Number Synonyms Comment Organism
1.1.1.86 acetohydroxyacid isomeroreductase
-
 Ignisphaera aggregans
1.1.1.86 acetohydroxyacid isomeroreductase
-
 Azotobacter vinelandii
1.1.1.86 acetohydroxyacid isomeroreductase
-
 Alicyclobacillus acidocaldarius subsp. acidocaldarius
1.1.1.86 acetohydroxyacid isomeroreductase
-
 uncultured archaeon
1.1.1.86 AHAIR
-
 Ignisphaera aggregans
1.1.1.86 AHAIR
-
 Azotobacter vinelandii
1.1.1.86 AHAIR
-
 Alicyclobacillus acidocaldarius subsp. acidocaldarius
1.1.1.86 AHAIR
-
 uncultured archaeon
1.1.1.86 AHIR
-
 Ignisphaera aggregans
1.1.1.86 AHIR
-
 Azotobacter vinelandii
1.1.1.86 AHIR
-
 Alicyclobacillus acidocaldarius subsp. acidocaldarius
1.1.1.86 AHIR
-
 uncultured archaeon
1.1.1.86 ilvC
-
 Ignisphaera aggregans
1.1.1.86 KARI
-
 Ignisphaera aggregans
1.1.1.86 KARI
-
 Azotobacter vinelandii
1.1.1.86 KARI
-
 Alicyclobacillus acidocaldarius subsp. acidocaldarius
1.1.1.86 KARI
-
 uncultured archaeon
1.1.1.382 ilvC
-
 uncultured archaeon GZfos26G2
1.1.1.382 ilvC
-
 Ignisphaera aggregans
1.1.1.382 ilvC
-
 Alicyclobacillus acidocaldarius subsp. acidocaldarius
1.1.1.382 ilvC
-
 uncultured archaeon
1.1.1.383 ilvC
-
 Azotobacter vinelandii

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
1.1.1.86 95
-
 half-maximal residual activity at 95°C Ignisphaera aggregans
1.1.1.383 95
-
 half-maximal residual activity at 95°C Azotobacter vinelandii

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.1.1.86 95
-
 the enzyme is highly thermostable with half-maximal residual activity at 95°C Ignisphaera aggregans

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.86 NADH
-
 Ignisphaera aggregans
1.1.1.86 NADH
-
 Azotobacter vinelandii
1.1.1.86 NADH
-
 Alicyclobacillus acidocaldarius subsp. acidocaldarius
1.1.1.86 NADH
-
 uncultured archaeon
1.1.1.86 NADPH
-
 Ignisphaera aggregans
1.1.1.86 NADPH
-
 Azotobacter vinelandii
1.1.1.86 NADPH
-
 Alicyclobacillus acidocaldarius subsp. acidocaldarius
1.1.1.86 NADPH
-
 uncultured archaeon