Ligand 2-dehydro-4-hydroxyoctonate
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Basic Ligand Information
Molecular Structure
C8H14O4
2-dehydro-4-hydroxyoctonate
QDXJQNIRIVKJCB-UHFFFAOYSA-N
4-hydroxy-2-oxooctanoate, 4-hydroxy-2-oxooctonate
Roles as Enzyme Ligand
Substrate in Enzyme-catalyzed Reactions (2 results)
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2-dehydro-4-hydroxyoctonate = ?
-
4-hydroxy-2-oxooctonate = ?
-
Product in Enzyme-catalyzed Reactions (1 result)
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pentaldehyde + pyruvate = 4-hydroxy-2-oxooctanoate
-
Enzyme Kinetic Parameters
kcat Value (Turnover Number) (8 results)
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1.5
-
mutant S184F, pH 7.5, 25°C
1.7
-
mutant T161S, pH 7.5, 25°C
1.8
-
mutant enzyme S184D, in 100 mM HEPES, pH 7.5
2
-
wild type enzyme, in 100 mM HEPES, pH 7.5
2
-
wild-type, pH 7.5, 25°C
2.6
-
mutant enzyme S184A, in 100 mM HEPES, pH 7.5
2.9
-
mutant enzyme S184L, in 100 mM HEPES, pH 7.5
3.1
-
mutant T161S/S18L, pH 7.5, 25°C
KM Value (8 results)
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2
5
mutant S184F, pH 7.5, 25°C
4.3
-
mutant T161S/S18L, pH 7.5, 25°C
15
-
mutant T161S, pH 7.5, 25°C
26
-
mutant enzyme S184L, in 100 mM HEPES, pH 7.5
51
-
mutant enzyme S184D, in 100 mM HEPES, pH 7.5
56
-
mutant enzyme S184A, in 100 mM HEPES, pH 7.5
146
-
wild-type, pH 7.5, 25°C
150
-
wild type enzyme, in 100 mM HEPES, pH 7.5
References & Links
Literature References (2)
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Mutagenesis of the phosphate-binding pocket of KDPG aldolase enhances selectivity for hydrophobic substrates
2007
Cheriyan, M.; Toone, E.J.; Fierke, C.A.
Protein Sci.
16
2368-2377
Improving upon nature: active site remodeling produces highly efficient aldolase activity toward hydrophobic electrophilic substrates
2012
Cheriyan, M.; Toone, E.J.; Fierke, C.A.
Biochemistry
51
1658-1668
Links to other databases for 2-dehydro-4-hydroxyoctonate
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