1.1.1.169: 2-dehydropantoate 2-reductase
This is an abbreviated version!
For detailed information about 2-dehydropantoate 2-reductase, go to the full flat file.
Word Map on EC 1.1.1.169
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1.1.1.169
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pantothenate
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nadph-dependent
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pane
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hydroxymethyltransferase
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ketopantoyl
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2'-phosphate
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fragment-based
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d-2-hydroxyacid
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parapsilosis
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kodakarensis
- 1.1.1.169
- pantothenate
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nadph-dependent
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pane
- hydroxymethyltransferase
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ketopantoyl
- 2'-phosphate
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fragment-based
- d-2-hydroxyacid
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parapsilosis
- kodakarensis
Reaction
Synonyms
2-dehydropantoate 2-reductase, 2-ketopantoate reductase, 2-ketopantoic acid reductase, 2-oxopantoate reductase, conjugated polyketone reductase, CPR, ilvC, ketopantoate reductase, ketopantoic acid reductase, KPA reductase, KPR, More, PanE, panG, Tk-KPR, TK1968, TK1968 protein
ECTree
Advanced search results
Engineering
Engineering on EC 1.1.1.169 - 2-dehydropantoate 2-reductase
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D248A
E210A
E256A
K176A
K72A
N98A
R31A
site-directed mutagenesis, altered steady-state kinetics of the mutant compared to the wild-type enzyme, overview
S244A
A181L
C84A
C84A
additional information
D248A
site-directed mutagenesis, unaltered activity compared to the wild-type enzyme, functional complementation of a panE knockout mutant strain
E210A
site-directed mutagenesis, unaltered activity compared to the wild-type enzyme, functional complementation of a panE knockout mutant strain
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site-directed mutagenesis, significant reduction in catalytic efficiency of enzyme
E256A
site-directed mutagenesis, nearly inactive mutant, 2600fold decreased catalytic efficiency, no complementation of a panE knockout mutant strain
E256A
site-directed mutagenesis, altered steady-state kinetics of the mutant compared to the wild-type enzyme, overview
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site-directed mutagenesis, significant reduction in catalytic efficiency of enzyme
K176A
site-directed mutagenesis, nearly inactive mutant, 78000fold decreased catalytic efficiency, no complementation of a panE knockout mutant strain
K176A
site-directed mutagenesis, altered steady-state kinetics of the mutant compared to the wild-type enzyme, overview
K72A
site-directed mutagenesis, unaltered activity compared to the wild-type enzyme, functional complementation of a panE knockout mutant strain
K72A
site-directed mutagenesis, altered steady-state kinetics of the mutant compared to the wild-type enzyme, overview
site-directed mutagenesis, nearly inactive mutant, 4000fold reduced catalytic efficiency, no complementation of a panE knockout mutant strain
N98A
site-directed mutagenesis, altered steady-state kinetics of the mutant compared to the wild-type enzyme, overview
site-directed mutagenesis, unaltered activity compared to the wild-type enzyme, functional complementation of a panE knockout mutant strain
S244A
site-directed mutagenesis, altered steady-state kinetics of the mutant compared to the wild-type enzyme, overview
site-directed mutagenesis, the substitution displaces Ser239 and increases the Km for ketopantoate 844fold, without affecting kcat. The decrease in 2-dehydropantoate affinity enhances the already kinetically preferred NADPH binding path, making the random mechanism appear to be sequentially ordered and reducing the kinetic cooperativity
A181L
the substitution increases the Km of ketopantoate 844fold, without affecting the kcat value
C84A
site-directed mutagenesis, crystal structure analysis, overview
C84A
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site-directed mutagenesis, crystal structure analysis, overview
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Lys176 acts as general acid in ketopantoate reduction and is involved in catalysis and ketopantoate binding, E256A functions in D-pantoate and ketopantoate binding in ketopantoate reductase
additional information
Lys176 and Glu256 important for binding ketopantoate and the catalytic mechanism
additional information
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Lys176 and Glu256 important for binding ketopantoate and the catalytic mechanism
additional information
generation of a gene TK1968 disruption mutant
additional information
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generation of a gene TK1968 disruption mutant
additional information
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generation of a gene TK1968 disruption mutant
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