BRENDA - Enzyme Database
show all sequences of 1.1.1.382

Cofactor specificity motifs and the induced fit mechanism in Class I ketol-acid reductoisomerases

Cahn, J.K.; Brinkmann-Chen, S.; Spatzal, T.; Wiig, J.A.; Buller, A.R.; Einsle, O.; Hu, Y.; Ribbe, M.W.; Arnold, F.H.; Biochem. J. 468, 475-484 (2015)

Data extracted from this reference:

Crystallization (Commentary)
Crystallization (Commentary)
Organism
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
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
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
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
Organism
Organism
UniProt
Commentary
Textmining
Alicyclobacillus acidocaldarius subsp. acidocaldarius
C8WR67
cf. EC 1.1.1.86
-
Alicyclobacillus acidocaldarius subsp. acidocaldarius DSM 446
C8WR67
cf. EC 1.1.1.86
-
Ignisphaera aggregans
E0SRA9
-
-
Ignisphaera aggregans DSM 17230
E0SRA9
-
-
uncultured archaeon
Q64BR7
cf. 1.1.1.86
-
uncultured archaeon GZfos26G2
Q64BR7
-
-
Synonyms
Synonyms
Commentary
Organism
ilvC
-
uncultured archaeon GZfos26G2
ilvC
-
Ignisphaera aggregans
ilvC
-
Alicyclobacillus acidocaldarius subsp. acidocaldarius
ilvC
-
uncultured archaeon
Crystallization (Commentary) (protein specific)
Crystallization
Organism
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
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
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
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
Other publictions for EC 1.1.1.382
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Synonyms
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
731279
Cahn
Cofactor specificity motifs an ...
Alicyclobacillus acidocaldarius subsp. acidocaldarius, Ignisphaera aggregans, uncultured archaeon, uncultured archaeon GZfos26G2, Alicyclobacillus acidocaldarius subsp. acidocaldarius DSM 446, Ignisphaera aggregans DSM 17230
Biochem. J.
468
475-484
2015
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732457
Brinkmann-Chen
Uncovering rare NADH-preferrin ...
Thermacetogenium phaeum, uncultured archaeon, Desulfococcus oleovorans, Archaeoglobus fulgidus
Metab. Eng.
26C
17-22
2014
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