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
-
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
1.1.1.169 2-dehydropantoate 2-reductaseAdvanced search results
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results (KM Value
KM Value on EC 1.1.1.169 - 2-dehydropantoate 2-reductase
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KM VALUE [mM] 
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
0.0096
(R)-4-dehydropantoate
wild type enzyme, at pH 7.5 and 25°C
8.1
(R)-4-dehydropantoate
mutant enzyme A181L, at pH 7.5 and 25°C
additional information
additional information
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steady-state kinetics, pH-dependence of kinetics with different substrates, overview
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additional information
additional information
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kinetics and thermodynamics, overview
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additional information
additional information
kinetics and thermodynamics, wild-type enzyme, overview
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additional information
additional information
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kinetics and thermodynamics, wild-type enzyme, overview
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additional information
additional information
kinetics of recombinant wild-type and mutant enzymes, overview
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additional information
additional information
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kinetics of recombinant wild-type and mutant enzymes, overview
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additional information
additional information
Michaelis-Menten kinetics in both reaction directions
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additional information
additional information
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Michaelis-Menten kinetics in both reaction directions
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additional information
additional information
the enzyme shows strong positive cooperativity in kinetics. The enzyme follows a random addition mechanism in which the initial binding of NADPH is the kinetically preferred path, with a small degree of cooperativity between subunits. The mechanism of Staphylococcus aureus KPR is distinct from those of previously described members of the family of 2-hydroxyacid dehydrogenases
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additional information
additional information
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the enzyme shows strong positive cooperativity in kinetics. The enzyme follows a random addition mechanism in which the initial binding of NADPH is the kinetically preferred path, with a small degree of cooperativity between subunits. The mechanism of Staphylococcus aureus KPR is distinct from those of previously described members of the family of 2-hydroxyacid dehydrogenases
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