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1.1.1.267: 1-deoxy-D-xylulose-5-phosphate reductoisomerase

This is an abbreviated version!
For detailed information about 1-deoxy-D-xylulose-5-phosphate reductoisomerase, go to the full flat file.

Word Map on EC 1.1.1.267

Reaction

2-C-methyl-D-erythritol 4-phosphate
+
NADP+
=
1-deoxy-D-xylulose 5-phosphate
+
NADPH
+
H+

Synonyms

1-deoxy-D-xylulose 5-phosphate isomeroreductase, 1-deoxy-D-xylulose 5-phosphate reductoisomerase, 1-deoxy-D-xylulose-5-phosphate, 1-deoxy-D-xylulose-5-phosphate reductoisomerase, 1-deoxy-D-xylulose-5-phosphate synthase, 1-deoxyxylulose 5-phosphate reductoisomerase, 1-deoxyxylulose-5-phosphate reductoisomerase, 2-C-methyl-D-erythritol 4-phosphate synthase, 2C-methyl-D-erythritol 4-phosphate synthase, 2C-methyl-D-erythritol-4-phosphate synthase, AaDXR, CaDXR, deoxyxylulose 5-phosphate reductoisomerase, deoxyxylulosephosphate reductoisomerase, DOXP reductoisomerase, DOXP-reductoisomerase, DXP reductoisomerase, DXP-reductoisomerase, DXR, DXR1, DzDXR, EcDXR, FtIspC, IspC, MEP synthase, meps, methylerythritol phosphate synthase, MtbIspC, MtDXR, Os01g01710, OsDXR, PdDXR, PfDXR, PtDXR, Rv2870c, SaDXR, VvDxr, YpIspC

ECTree

     1 Oxidoreductases
         1.1 Acting on the CH-OH group of donors
             1.1.1 With NAD+ or NADP+ as acceptor
                1.1.1.267 1-deoxy-D-xylulose-5-phosphate reductoisomerase

Engineering

Engineering on EC 1.1.1.267 - 1-deoxy-D-xylulose-5-phosphate reductoisomerase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E231K
less than 0.24% wild type kcat
H153Q
increase of Km
H209Q
increase of Km
H257Q
increase of Km
S177D
-
inactive
S177E
-
inactive
D151N/E222Q
loss of catalytic ability, loss of binding of Mn2+. Crystallization data
W203A
complete loss of activity
W203F
turnover is largely limited by product release for the wild-type enzyme, chemistry is significantly more rate-limiting for mutants W203F and W203Y. Mutant is more sensitive to fosmidomycin than wild-type. Mutation strongly tips the entropy-enthalpy balance of total binding energy
W203G
complete loss of activity
W203Y
turnover is largely limited by product release for the wild-type enzyme, chemistry is significantly more rate-limiting for mutants W203F and W203Y. Mutant is more sensitive to fosmidomycin than wild-type. Mutation strongly tips the entropy-enthalpy balance of total binding energy
D151N/E222Q
-
loss of catalytic ability, loss of binding of Mn2+. Crystallization data
-
W203A
-
complete loss of activity
-
W203F
-
turnover is largely limited by product release for the wild-type enzyme, chemistry is significantly more rate-limiting for mutants W203F and W203Y. Mutant is more sensitive to fosmidomycin than wild-type. Mutation strongly tips the entropy-enthalpy balance of total binding energy
-
W203G
-
complete loss of activity
-
W203Y
-
turnover is largely limited by product release for the wild-type enzyme, chemistry is significantly more rate-limiting for mutants W203F and W203Y. Mutant is more sensitive to fosmidomycin than wild-type. Mutation strongly tips the entropy-enthalpy balance of total binding energy
-
H219Q
site-directed mutagenesis, the mutation decreased the affinity toward the substrate 1-deoxy-D-xylulose 5-phosphate with an 8-fold increase in the Km compared to the wild-type enzyme
D152A
-
site-directed mutagenesis, active site mutant, in sense and antisense orientation, 4.1% activity compared to the wild-type enzyme
D152N
-
site-directed mutagenesis, active site mutant, in sense and antisense orientation, inactive mutant
E154D
-
site-directed mutagenesis, active site mutant, in sense and antisense orientation, 0.28% activity compared to the wild-type enzyme
E154Q
-
site-directed mutagenesis, active site mutant, in sense and antisense orientation, 0.008% activity compared to the wild-type enzyme
E223H
-
site-directed mutagenesis, active site mutant, in sense and antisense orientation, 0.007% activity compared to the wild-type enzyme
E223Q
-
site-directed mutagenesis, active site mutant, in sense and antisense orientation, inactive mutant
H155A
-
site-directed mutagenesis, active site mutant, in sense and antisense orientation, 32% activity compared to the wild-type enzyme
M206A
-
site-directed mutagenesis, active site mutant, in sense and antisense orientation, 9% activity compared to the wild-type enzyme
M206V
-
site-directed mutagenesis, active site mutant, in sense and antisense orientation, inactive mutant
S153A
-
site-directed mutagenesis, active site mutant, in sense and antisense orientation, 0.11% activity compared to the wild-type enzyme
S153N
-
site-directed mutagenesis, active site mutant, in sense and antisense orientation, 0.76% activity compared to the wild-type enzyme
S153T
-
site-directed mutagenesis, active site mutant, in sense and antisense orientation, 4.8% activity compared to the wild-type enzyme
W204A
-
site-directed mutagenesis, the mutant shows reduced activity and altered kinetics compared to the wild-type enzyme
W204F
-
site-directed mutagenesis, the mutant shows reduced activity and altered kinetics compared to the wild-type enzyme, the mutant is active with the substrate analogue 1,2-dideoxy-D-threo-3-hexulose 6-phosphate in contrast to the wild-type enzyme
W204L
-
site-directed mutagenesis, the mutant shows reduced activity and altered kinetics compared to the wild-type enzyme
W204V
-
site-directed mutagenesis, the mutant shows reduced activity and altered kinetics compared to the wild-type enzyme
additional information