2.1.2.11: 3-methyl-2-oxobutanoate hydroxymethyltransferase
This is an abbreviated version!
For detailed information about 3-methyl-2-oxobutanoate hydroxymethyltransferase, go to the full flat file.
Word Map on EC 2.1.2.11
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2.1.2.11
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pantothen
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auxotrophs
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aldol
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l-valine
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beta-alanine
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pane
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betaalpha8
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2-oxoacids
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pharmacology
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alpha-ketobutyrate
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decameric
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4'-phosphopantetheine
- 2.1.2.11
-
pantothen
-
auxotrophs
-
aldol
- l-valine
- beta-alanine
-
pane
-
betaalpha8
- 2-oxoacids
- pharmacology
- alpha-ketobutyrate
-
decameric
- 4'-phosphopantetheine
Reaction
Synonyms
5,10-methylene tetrahydrofolate:alpha-ketoisovalerate hydroxymethyltransferase, alpha-ketoisovalerate hydroxymethyltransferase, dehydropantoate hydroxymethyltransferase, hydroxymethyltransferase, ketopantoate, ketopantoate hydroxymethyl transferase, ketopantoate hydroxymethyltransferase, KHMT, KPHMT, MOHMT, oxopantoate hydroxymethyltransferase, PanB
ECTree
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Metals Ions
Metals Ions on EC 2.1.2.11 - 3-methyl-2-oxobutanoate hydroxymethyltransferase
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Ca2+
Co2+
Mg2+
Mn2+
Ni2+
Zn2+
additional information
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substrate enolization is divalent metal-dependent with a preference for metal ions in decreasing order: Mg2+, Zn2+, Co2+, Ni2+, Ca2+
Ca2+
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Km: 0.27 mM, the reaction is divalent metal-dependent with descending order of preference: Mg2+, Zn2+, Co2+, Ni2+, Ca2+
Co2+
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substrate enolization is divalent metal-dependent with a preference for metal ions in decreasing order: Mg2+, Zn2+, Co2+, Ni2+, Ca2+
Co2+
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Km: 0.33 mM, the reaction is divalent metal-dependent with descending order of preference: Mg2+, Zn2+, Co2+, Ni2+, Ca2+
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activates and is required for activity, 0.1 mM Mg2+ is most active, Mn2+, Ni2+, Co2+ and Zn2+ are progressively less active, restores activity after dialysis
Mg2+
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substrate enolization is divalent metal-dependent with a preference for metal ions in decreasing order: Mg2+, Zn2+, Co2+, Ni2+, Ca2+
Mg2+
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Km: 0.61 mM, the reaction is divalent metal-dependent with descending order of preference: Mg2+, Zn2+, Co2+, Ni2+, Ca2+
Ni2+
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substrate enolization is divalent metal-dependent with a preference for metal ions in decreasing order: Mg2+, Zn2+, Co2+, Ni2+, Ca2+
Ni2+
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Km: 0.45 mM, the reaction is divalent metal-dependent with descending order of preference: Mg2+, Zn2+, Co2+, Ni2+, Ca2+
Zn2+
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substrate enolization is divalent metal-dependent with a preference for metal ions in decreasing order: Mg2+, Zn2+, Co2+, Ni2+, Ca2+
Zn2+
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Km: 0.08 mM, the reaction is divalent metal-dependent with descending order of preference: Mg2+, Zn2+, Co2+, Ni2+, Ca2+
additional information
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metalloenzyme, inactive in absence of divalent metals, enzyme binds metal ions that assist in the polarization of the carbonyl group and stabilize the enolate anion