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1.1.1.86: ketol-acid reductoisomerase (NADP+)

This is an abbreviated version!
For detailed information about ketol-acid reductoisomerase (NADP+), go to the full flat file.

Word Map on EC 1.1.1.86

Reaction

(2R)-2,3-dihydroxy-3-methylbutanoate
+
NADP+
=
(2S)-2-hydroxy-2-methyl-3-oxobutanoate
+
NADPH
+
H+

Synonyms

2-hydroxy-3-keto acid reductoisomerase, acetohydroxy acid isomeroreductase, acetohydroxy acid reductoisomerase, acetohydroxy-acid isomeroreductase , acetohydroxy-acid reductoisomerase , acetohydroxyacid isomeroreductase, acetolactate reductoisomerase, AHAIR, AHIR, alpha-keto-beta-hydroxylacil reductoisomerase, alpha-keto-beta-hydroxylacyl reductoisomerase, class II ketol-acid reductoisomerase, dehydrogenase, dihydroxyisovalerate (isomerizing), dihydroxyisovalerate dehydrogenase (isomerizing), EC 1.1.1.89, Icl1p, Ilv5p, ilvC, IlvC-PanE, IlvC1, IlvC2, isomerase, ketol acid reducto-, isomeroreductase, KARI, ketol-acid reductoisomerase, reductoisomerase

ECTree

     1 Oxidoreductases
         1.1 Acting on the CH-OH group of donors
             1.1.1 With NAD+ or NADP+ as acceptor
                1.1.1.86 ketol-acid reductoisomerase (NADP+)

Engineering

Engineering on EC 1.1.1.86 - ketol-acid reductoisomerase (NADP+)

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
R48P/S51L/S52D
mutant engineered for reversal in cofactor specificity for NADH over NADPH
R48P/S51L/S52D/R84A
mutant engineered for reversal in cofactor specificity for NADH over NADPH
D217E
-
less than 4% reductoisomerase activity in comparison to wild-type enzyme
D217N
-
less than 4% reductoisomerase activity in comparison to wild-type enzyme
E213D
-
75% reductoisomerase activity in comparison of wild-type enzyme
E213Q
-
less than 4% reductoisomerase activity in comparison of wild-type enzyme
E221D
-
less than 4% reductoisomerase activity in comparison to wild-type enzyme
E221Q
-
less than 4% reductoisomerase activity in comparison to wild-type enzyme
E389D
-
less than 4% reductoisomerase activity in comparison to wild-type enzyme
E389Q
-
less than 4% reductoisomerase activity in comparison to wild-type enzyme
E393D
-
less than 4% reductoisomerase activity in comparison to wild-type enzyme
E393Q
-
the mutant is insoluble, a soluble form is obtained only after denaturation
H132K
-
less than 4% reductoisomerase activity in comparison of wild-type enzyme
H132Q
-
less than 4% reductoisomerase activity in comparison of wild-type enzyme
K155E
-
less than 4% reductoisomerase activity in comparison of wild-type enzyme
K155Q
-
less than 4% reductoisomerase activity in comparison of wild-type enzyme
K155R
-
less than 4% reductoisomerase activity in comparison of wild-type enzyme
K69L
-
Km-value for NADP+ in the reaction with 2,3-dihydroxy-3-methylbutanoate is 2.1fold higher than the Km-value of the wild-type enzyme, the turnover-number for the reaction with NADP+ and 2,3-dihydroxy-3-methylbutanoate is lower by a factor 163 compared to wild-type enzyme. Km-value for NADPH in the reaction with acetolactate is comparable to that of the wild-type emzyme, the turnover-number for the reaction with NADP+ and 2,3-dihydroxy-3-methylbutanoate is 1.8fold higher than that of the wild-type enzyme
K75Q
-
Km-value for NADP+ in the reaction with 2,3-dihydroxy-3-methylbutanoate is 2.7fold higher than the Km-value of the wild-type enzyme, the turnover-number for the reaction with NADP+ and 2,3-dihydroxy-3-methylbutanoate is lower by a factor 77.5 compared to wild-type enzyme. Km-value for NADPH in the reaction with acetolactate is lower by a factor 2.9 compared to the Km-value of the wild-type enzyme, the turnover-number for the reaction with NADP+ and 2,3-dihydroxy-3-methylbutanoate is lower by a factor 12.9 compared to wild-type enzyme
R68D/K69L/K75V/R76D
-
turnover-number for reaction with NADH and acetolactate is 48fold higher compared to wild-type enzyme, turnover-number for reaction with NADPH and acetolactate is lower by factor 3.7 compared to wild-type enzyme, Km-value for NADH in the reaction with NADH and acetolactate is lower by a factor 10.8 compared to wild-type enzyme, Km-value for NADH in the reaction with NADPH and acetolactate is 30fold higher compared to wild-type enzyme
R68Q
-
Km-value for NADP+ in the reaction with 2,3-dihydroxy-3-methylbutanoate is 6.9fold higher than the Km-value of the wild-type enzyme, the turnover-number for the reaction with NADP+ and 2,3-dihydroxy-3-methylbutanoate is lower by a factor 345 compared to wild-type enzyme. Km-value for NADPH in the reaction with acetolactate is 3.4fold higher thahn that of the wild-type enzyme, the turnover-number for the reaction with NADP+ and 2,3-dihydroxy-3-methylbutanoate is lower by a factor 18 compared to wild-type enzyme
R76D
-
turnover-number for reaction with NADH and acetolactate is 48fold higher compared to wild-type enzyme, turnover-number for reaction with NADPH and acetolactate is lower by factor 4 compared to wild-type enzyme, Km-value for NADH in the reaction with NADH and acetolactate is lower by a factor 2.5 compared to wild-type enzyme, Km-value for NADPH in the reaction with NADPH and acetolactate is 55fold higher compared to wild-type enzyme
R76Q
-
Km-value for NADP+ in the reaction with 2,3-dihydroxy-3-methylbutanoate is 17.1fold higher than the Km-value of the wild-type enzyme, the turnover-number for the reaction with NADP+ and 2,3-dihydroxy-3-methylbutanoate is lower by a factor 258 compared to wild-type enzyme. Km-value for NADPH in the reaction with acetolactate is 5fold higher than that of the wild-type enzyme, the turnover-number for the reaction with NADP+ and 2,3-dihydroxy-3-methylbutanoate is lower by a factor 19.5 compared to wild-type enzyme
R76Q/R68A
-
turnover-number for reaction with NADH and acetolactate is 20fold higher compared to wild-type enzyme, turnover-number for reaction with NADPH and acetolactate is lower by factor 28 compared to wild-type enzyme, Km-value for NADH in the reaction with NADH and acetolactate is comparable to that of wild-type enzyme, Km-value for NADPH in the reaction with NADPH and acetolactate is 22fold higher compared to wild-type enzyme
S414A
-
less than 4% reductoisomerase activity in comparison to wild-type enzyme
S414T
-
less than 4% reductoisomerase activity in comparison to wild-type enzyme
G50D/S52D
DELTA1-17
-
mutant with N-terminal 17-residue deletion: cellular localisation similar to wild-type, introduction into an ilv5DELTA strain, lacking the ilv5 gene, complements isoleucine and valine synthesis
DELTA1-33
-
mutant with N-terminal 33-residue deletion: cellular localisation predominatly in the cytosol rather than in mitochondria. Deletion of the N-terminal 33 residues is sufficient to largely impair the protein's targeting to mitochondria. Introduction into an ilv5DELTA strain, lacking the ilv5 gene, complements isoleucine and valine synthesis
DELTA1-40
-
mutant with N-terminal 40-residue deletion: cellular localisation throughout the cytosol rather than in mitochondria
DELTA1-46
-
mutant with N-terminal 46-residue deletion: cellular localisation throughout the cytosol rather than in mitochondria. This mutant shows the largest steady-state protein level. Introduction into an ilv5DELTA strain, lacking the ilv5 gene, does not complements isoleucine and valine synthesis. Introduction into an industrial lager brewing strain, a robust expression of DELTA46 is as effective as that of a wild-type Ilv5p in lowering the total Vicinal diketones production in a 2l scale fermentation trial. Additional expression of DELTA46 does not alter the quality of the resultant beer in terms of contents of aromatic compounds and organic acids
DELTA1-53
-
mutant with N-terminal 53-residue deletion: cellular localisation throughout the cytosol rather than in mitochondria
DELTA1-66
-
mutant with N-terminal 66-residue deletion: weaker cytosolic localisation compared to other mutants. Mutant shows only a small amount of steady-state protein content
DELTA1-83
-
mutant with N-terminal 83-residue deletion: weaker cytosolic localisation compared to other mutants. Mutant shows only a small amount of steady-state protein content
DELTA1-99
-
mutant with N-terminal 99-residue deletion: weaker cytosolic localisation compared to other mutants. Mutant shows only a small amount of steady-state protein content
DELTA423-430/F431S
-
mutant enzyme behaves as an active monomer with reduced thermal stability, KM-value for NADPH does not differ considerably from that for the wild-type enzyme, magnesium affinity is dramatically altered by monomerization
D191G
crystal structure of the mutants (R49E, D83G, D191G and E195S) reveals local conformational changes only in the NADP(H) binding site. Mutant enzyme exhibits significantly reduced activities compared to wild-type enzyme
D191K
mutant enzyme exhibits significantly reduced activities compared to wild-type enzyme
D83G
crystal structure of the mutants (R49E, D83G, D191G and E195S) reveals local conformational changes only in the NADP(H) binding site. Mutant enzyme exhibits significantly reduced activities compared to wild-type enzyme
E195A
mutant enzyme exhibits significantly reduced activities compared to wild-type enzyme
E195K
mutant enzyme exhibits significantly reduced activities compared to wild-type enzyme
E195S
crystal structure of the mutants (R49E, D83G, D191G and E195S) reveals local conformational changes only in the NADP(H) binding site. Mutant enzyme exhibits significantly reduced activities compared to wild-type enzyme
R49A
mutant enzyme exhibits significantly reduced activities compared to wild-type enzyme
R49E
crystal structure of the mutants (R49E, D83G, D191G and E195S) reveals local conformational changes only in the NADP(H) binding site. Mutant enzyme exhibits significantly reduced activities compared to wild-type enzyme
R49G
mutant enzyme exhibits significantly reduced activities compared to wild-type enzyme
S53A
mutant enzyme exhibits significantly reduced activities compared to wild-type enzyme
S53G
mutant enzyme exhibits significantly reduced activities compared to wild-type enzyme
S53K
mutant enzyme exhibits significantly reduced activities compared to wild-type enzyme
S53T
mutant enzyme exhibits significantly reduced activities compared to wild-type enzyme