Information on EC 1.1.1.383 - ketol-acid reductoisomerase [NAD(P)+]

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The expected taxonomic range for this enzyme is: Bacteria, Archaea

EC NUMBER
COMMENTARY hide
1.1.1.383
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RECOMMENDED NAME
GeneOntology No.
ketol-acid reductoisomerase [NAD(P)+]
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(2R)-2,3-dihydroxy-3-methylbutanoate + NAD(P)+ = (2S)-2-hydroxy-2-methyl-3-oxobutanoate + NAD(P)H + H+
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
L-isoleucine biosynthesis II
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L-isoleucine biosynthesis IV
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SYSTEMATIC NAME
IUBMB Comments
(2R)-2,3-dihydroxy-3-methylbutanoate:NAD(P)+ oxidoreductase (isomerizing)
The enzyme, characterized from the bacteria Hydrogenobaculum sp. and Syntrophomonas wolfei subsp. wolfei and from the archaea Metallosphaera sedula and Ignisphaera aggregans, can use both NADH and NADPH with similar efficiency [cf. EC 1.1.1.86, ketol-acid reductoisomerase (NADP+) and EC 1.1.1.382, ketol-acid reductoisomerase (NAD+)].
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
cf. EC 1.1.1.86
SwissProt
Manually annotated by BRENDA team
cf. EC 1.1.1.86
SwissProt
Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(2S)-2-hydroxy-2-methyl-3-oxobutanoate + NADH + H+
(2R)-2,3-dihydroxy-3-methylbutanoate + NAD+
show the reaction diagram
(2S)-2-hydroxy-2-methyl-3-oxobutanoate + NADPH + H+
(2R)-2,3-dihydroxy-3-methylbutanoate + NADP+
show the reaction diagram
(S)-2-acetolactate + NADH + H+
2,3-dihydroxy-3-methylbutanoate + NAD+
show the reaction diagram
(S)-2-acetolactate + NADPH + H+
2,3-dihydroxy-3-methylbutanoate + NADP+
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADPH
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.015 - 1.08
NADH
0.001 - 1.4
NADPH
additional information
NADH
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.02 - 4.3
NADH
0.03 - 7.2
NADPH
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.3 - 165
NADH
8
0.05 - 4500
NADPH
5
additional information
NADH
8
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
95
half-maximal residual activity at 95°C
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A71S
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mutant engineered to use NADH instead of NADPH
A71S/R76D/S78D/Q110A
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mutant engineered to use NADH instead of NADPH
A71S/R76D/S78D/Q110V
A71S/R76D/S78D/Q110V/D146G/G185R/K433E
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mutant engineered for reversal in cofactor specificity for NADH over NADPH
Q110A
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mutant engineered to use NADH instead of NADPH
Q110V
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mutant engineered to use NADH instead of NADPH
R76D
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mutant engineered to use NADH instead of NADPH
S78D
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mutant engineered to use NADH instead of NADPH
S78D/Q110V
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mutant engineered to use NADH instead of NADPH
V48L/R49P/K52E/S53D
mutant engineered for reversal in cofactor specificity for NADH over NADPH
V48L/R49P/K52L/S53D
mutant engineered for reversal in cofactor specificity for NADH over NADPH
V48L/R49P/K52L/S53D/E59K/T182S/E320K
mutant engineered for reversal in cofactor specificity for NADH over NADPH
V48L/R49P/K52E/S53D
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mutant engineered for reversal in cofactor specificity for NADH over NADPH
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V48L/R49P/K52L/S53D
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mutant engineered for reversal in cofactor specificity for NADH over NADPH
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V48L/R49P/K52L/S53D/E59K/T182S/E320K
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mutant engineered for reversal in cofactor specificity for NADH over NADPH
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A71S/R76D/S78AD/Q110V
mutant engineered for reversal in cofactor specificity for NADH over NADPH
R76D/Ser78D
mutant engineered for reversal in cofactor specificity for NADH over NADPH
A71S/R76D/S78AD/Q110V
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mutant engineered for reversal in cofactor specificity for NADH over NADPH
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R76D/Ser78D
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mutant engineered for reversal in cofactor specificity for NADH over NADPH
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S61D/S63D
mutant engineered for reversal in cofactor specificity for NADH over NADPH
S61D/S63D/I95V
mutant engineered for reversal in cofactor specificity for NADH over NADPH
S61D/S63D
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mutant engineered for reversal in cofactor specificity for NADH over NADPH
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S61D/S63D/I95V
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mutant engineered for reversal in cofactor specificity for NADH over NADPH
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additional information
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recipe for altering the cofactor specificity of the ketol-acid reductoisomerases (KARIs). Combining results for an engineered NADH-dependent variant of Escherichia coli KARI with available KARI crystal structures and a comprehensive KARI-sequence alignment, key cofactor specificity determinants are identified and used to construct KARIs with reversed cofactor preference
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
biofuel production