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5,10-methylenetetrahydrofolate + 2-oxobutyrate
?
5,10-methylenetetrahydrofolate + 2-oxopentanoate
?
-
-
-
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate + H2O
tetrahydrofolate + 2-dehydropantoate
-
-
-
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxopentanoate
?
-
-
-
-
?
formaldehyde + tetrahydrofolate
methylentetrahydrofolate
tetrahydropteroyldiglutamate + 2-dehydropantoate
5,10-methylenetetrahydropteroyldiglutamate + 3-methyl-2-oxobutanoate + H2O
-
-
-
-
r
tetrahydropteroylheptaglutamate + 2-dehydropantoate
5,10-methylenetetrahydropteroylheptaglutamate + 3-methyl-2-oxobutanoate + H2O
-
-
-
-
r
tetrahydropteroylhexaglutamate + 2-dehydropantoate
5,10-methylenetetrahydropteroylhexaglutamate + 3-methyl-2-oxobutanoate + H2O
-
-
-
-
r
tetrahydropteroylpentaglutamate + 2-dehydropantoate
5,10-methylenetetrahydropteroylpentaglutamate + 3-methyl-2-oxobutanoate + H2O
-
-
-
-
r
tetrahydropteroyltetraglutamate + 2-dehydropantoate
5,10-methylenetetrahydropteroyltetraglutamate + 3-methyl-2-oxobutanoate + H2O
-
-
-
-
r
tetrahydropteroyltriglutamate + 2-dehydropantoate
5,10-methylenetetrahydropteroyltriglutamate + 3-methyl-2-oxobutanoate + H2O
-
-
-
-
r
additional information
?
-
-
no substrates: pyruvate, isovalerate, D- and L-valine, 3-methyl-2-butanone
-
-
?
5,10-methylenetetrahydrofolate + 2-oxobutyrate
?
-
-
-
-
?
5,10-methylenetetrahydrofolate + 2-oxobutyrate
?
-
also a good substrate
-
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
-
-
-
r
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
-
-
formation of ketopantoate, syn. 2-keto-3,3-dimethyl-4-hydroxybutyrate, tetrahydrofolate-dependent enzyme
r
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
-
-
synthesis of ketopantoate, the following components can replace tetrahydrofolate: tetrahydropteroylmono-, di-, tri-, tetra-, penta-, hexa-, and heptaglutamate, absolute requirement for tetrahydrofolate, only the L-isomer is active
r
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
-
forms 2-oxopantoate, syn. 3-hydroxymethyl-3-methyl-2-oxobutanoic acid, from 2-oxoisovalerate with retention of configuration at C-3
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
-
condensation of alpha-ketoisovalerate with the C-1 donor takes place stereospecifically at C-3 and proceeds in a retention mode at C-3, 5,10-methylenetetrahydrofolate-dependent enzyme
-
r
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
-
specificity for alpha-ketoisovalerate is less rigid than for tetrahydrofolate
synthesis of ketopantoate, the following components can replace tetrahydrofolate: tetrahydropteroylmono-, di-, tri-, tetra-, penta-, hexa-, and heptaglutamate, absolute requirement for tetrahydrofolate, only the L-isomer is active
r
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
-
inversion of the configuration at C-3 of 2-ketoisovalerate
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
-
first committed step in pantothenate biosynthesis
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
-
first committed step in pantothenate biosynthesis
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
-
first committed step in pantothenate biosynthesis
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
-
first committed step in pantothenate biosynthesis
-
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
-
first committed step in pantothenate biosynthesis
enzyme is responsible for catalysis of ketopantoate formation in vivo
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
-
catalytic activity is regulated by the products of the reaction path of which it is one component
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
-
biosynthesis of coenzyme A
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
-
biosynthesis of coenzyme A
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
-
first step in pantoate biosynthesis
-
?
formaldehyde + tetrahydrofolate
methylentetrahydrofolate
-
-
-
?
formaldehyde + tetrahydrofolate
methylentetrahydrofolate
-
-
-
-
?
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5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate + H2O
tetrahydrofolate + 2-dehydropantoate
-
-
-
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
-
first committed step in pantothenate biosynthesis
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
-
first committed step in pantothenate biosynthesis
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
-
first committed step in pantothenate biosynthesis
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
-
first committed step in pantothenate biosynthesis
-
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
-
first committed step in pantothenate biosynthesis
enzyme is responsible for catalysis of ketopantoate formation in vivo
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
-
catalytic activity is regulated by the products of the reaction path of which it is one component
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
-
biosynthesis of coenzyme A
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
-
biosynthesis of coenzyme A
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
-
first step in pantoate biosynthesis
-
?
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Ni2+
-
activates, Mg2+ is most active followed by Mn2+, Ni2+, Co2+ and Zn2+
additional information
-
not activated by Cu2+ and Fe2+
Co2+
-
requires Mg2+, Mn2+, Co2+ and Zn2+ are progressively less active
Co2+
-
activates, Mg2+ is most active followed by Mn2+, Ni2+, Co2+ and Zn2+
Mg2+
-
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+
-
requires Mg2+, Mn2+, Co2+ and Zn2+ are progressively less active
Mn2+
-
requires Mg2+, Mn2+, Co2+ and Zn2+ are progressively less active
Mn2+
-
activates, Mg2+ is most active followed by Mn2+, Ni2+, Co2+ and Zn2+
Zn2+
-
requires Mg2+, Mn2+, Co2+ and Zn2+ are progressively less active
Zn2+
-
activates, Mg2+ is most active followed by Mn2+, Ni2+, Co2+ and Zn2+
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Teller, J.H.; Powers, S.G.; Snell, E.E.
Ketopantoate hydroxymethyltransferase. I. Purification and role in pantothenate biosynthesis
J. Biol. Chem.
251
3780-3785
1976
Escherichia coli, Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Powers, S.G.; Snell, E.E.
Ketopantoate hydroxymethyltransferase. II. Physical, catalytic, and regulatory properties
J. Biol. Chem.
251
3786-3793
1976
Escherichia coli
brenda
Powers, S.G.; Snell, E.E.
Purification and properties of ketopantoate hydroxymethyltransferase
Methods Enzymol.
62
204-209
1979
Escherichia coli
brenda
Wightman, R.H.
Stereochemistry of 2-oxopantoate formation by oxopantoate hydroxymethyltransferase
J. Chem. Soc. Chem. Commun.
1979
818-819
1979
Escherichia coli
-
brenda
Aberhart, D.J.
Stereochemistry of pantoate biosynthesis from 2-ketoisovalerate
J. Am. Chem. Soc.
101
1354-1355
1979
Escherichia coli
-
brenda
Aberhart, D.J.; Russell, D.J.
Steric course of ketopantoate hydroxymethyltransferase in E. coli
J. Am. Chem. Soc.
106
4902-4906
1984
Escherichia coli
-
brenda
Jones, C.E.; Brook, J.M.; Buck, D.; Abell, C.; Smith, A.G.
Cloning and sequencing of the Escherichia coli panB gene, which encodes ketopantoate hydroxymethyltransferase, and overexpression of the enzyme
J. Bacteriol.
175
2125-2130
1993
Escherichia coli
brenda
Schmitzberger, F.; Smith, A.G.; Abell, C.; Blundell, T.L.
Comparative analysis of the Escherichia coli ketopantoate hydroxymethyltransferase crystal structure confirms that it is a member of the (betaalpha)8 phosphoenolpyruvate/pyruvate superfamily
J. Bacteriol.
185
4163-4171
2003
Escherichia coli (P31057), Escherichia coli
brenda
von Delft, F.; Inoue, T.; Saldanha, S.A.; Ottenhof, H.H.; Schmitzberger, F.; Birch, L.M.; Dhanaraj, V.; Witty, M.; Smith, A.G.; Blundell, T.L.; Abell, C.
Structure of E. coli ketopantoate hydroxymethyl transferase complexed with ketopantoate and Mg2+, solved by locating 160 selenomethionine sites
Structure
11
985-996
2003
Escherichia coli
brenda
Thiaville, J.J.; Frelin, O.; Garcia-Salinas, C.; Harrison, K.; Hasnain, G.; Horenstein, N.A.; Diaz de la Garza, R.I.; Henry, C.S.; Hanson, A.D.; de Crecy-Lagard, V.
Experimental and metabolic modeling evidence for a folate-cleaving side-activity of ketopantoate hydroxymethyltransferase (PanB)
Front. Microbiol.
7
431
2016
Escherichia coli, Escherichia coli W3110
brenda