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Literature summary for 2.1.2.11 extracted from

  • Powers, S.G.; Snell, E.E.
    Ketopantoate hydroxymethyltransferase. II. Physical, catalytic, and regulatory properties (1976), J. Biol. Chem., 251, 3786-3793.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
3-Methyl-2-butanone 5 mM, 27% inhibition Escherichia coli
coenzyme A above 1 mM Escherichia coli
D-valine 5 mM, 16% inhibition Escherichia coli
formaldehyde 0.8 mM, partial inhibition Escherichia coli
Isovalerate 5 mM, 39% inhibition Escherichia coli
L-valine 5 mM, 23% inhibition Escherichia coli
additional information not inactivated by borohydride reduction in the presence of excess substrates Escherichia coli
Pantoate 0.05 mM or above Escherichia coli
pantothenate 0.5 mM or above Escherichia coli
pyruvate 5 mM, 38% inhibition Escherichia coli
tetrahydrofolate 0.38 mM, partial inhibition Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.1
-
Tetrahydropteroylpentaglutamate
-
Escherichia coli
0.1
-
tetrahydropteroyltetraglutamate
-
Escherichia coli
0.16
-
ketopantoate
-
Escherichia coli
0.17
-
tetrahydropteroylhexaglutamate
-
Escherichia coli
0.18
-
tetrahydropteroyltriglutamate
-
Escherichia coli
0.18
-
tetrahydrofolate forward and reverse reaction, methylenetetrahydrofolate: formaldehyde + tetrahydrofolate Escherichia coli
0.25
-
tetrahydropteroyldiglutamate
-
Escherichia coli
0.29
-
tetrahydropteroylheptaglutamate
-
Escherichia coli
0.33
-
tetrahydropteroylmonoglutamate
-
Escherichia coli
1.1
-
3-methyl-2-oxobutanoate
-
Escherichia coli
2.9
-
2-oxobutyrate
-
Escherichia coli
5.9
-
3-methyl-2-oxopentanoate
-
Escherichia coli
5.9
-
formaldehyde methylenetetrahydrofolate: formaldehyde + tetrahydrofolate Escherichia coli
25
-
2-oxopentanoate
-
Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Co2+ activates, Mg2+ is most active followed by Mn2+, Ni2+, Co2+ and Zn2+ Escherichia coli
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 Escherichia coli
Mn2+ activates, Mg2+ is most active followed by Mn2+, Ni2+, Co2+ and Zn2+ Escherichia coli
additional information not activated by Cu2+ and Fe2+ Escherichia coli
Ni2+ activates, Mg2+ is most active followed by Mn2+, Ni2+, Co2+ and Zn2+ Escherichia coli
Zn2+ activates, Mg2+ is most active followed by Mn2+, Ni2+, Co2+ and Zn2+ Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
25700
-
10 * 27000, SDS-PAGE, 10 * 25700, amino acid analysis Escherichia coli
27000
-
10 * 27000, SDS-PAGE, 10 * 25700, amino acid analysis Escherichia coli
255000
-
sedimentation equilibrium Escherichia coli
285000
-
gel filtration Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate Escherichia coli first committed step in pantothenate biosynthesis tetrahydrofolate + 2-dehydropantoate
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate Escherichia coli catalytic activity is regulated by the products of the reaction path of which it is one component tetrahydrofolate + 2-dehydropantoate
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Escherichia coli

Reaction

Reaction Comment Organism Reaction ID
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate + H2O = tetrahydrofolate + 2-dehydropantoate class II aldolase Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5,10-methylenetetrahydrofolate + 2-oxobutyrate also a good substrate Escherichia coli ?
-
?
5,10-methylenetetrahydrofolate + 2-oxopentanoate
-
Escherichia coli ?
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate specificity for alpha-ketoisovalerate is less rigid than for tetrahydrofolate Escherichia coli 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 first committed step in pantothenate biosynthesis Escherichia coli tetrahydrofolate + 2-dehydropantoate
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate catalytic activity is regulated by the products of the reaction path of which it is one component Escherichia coli tetrahydrofolate + 2-dehydropantoate
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxopentanoate
-
Escherichia coli ?
-
?
formaldehyde + tetrahydrofolate
-
Escherichia coli methylentetrahydrofolate
-
?
additional information no substrates: pyruvate, isovalerate, D- and L-valine, 3-methyl-2-butanone Escherichia coli ?
-
?
tetrahydropteroyldiglutamate + 2-dehydropantoate
-
Escherichia coli 5,10-methylenetetrahydropteroyldiglutamate + 3-methyl-2-oxobutanoate + H2O
-
r
tetrahydropteroylheptaglutamate + 2-dehydropantoate
-
Escherichia coli 5,10-methylenetetrahydropteroylheptaglutamate + 3-methyl-2-oxobutanoate + H2O
-
r
tetrahydropteroylhexaglutamate + 2-dehydropantoate
-
Escherichia coli 5,10-methylenetetrahydropteroylhexaglutamate + 3-methyl-2-oxobutanoate + H2O
-
r
tetrahydropteroylpentaglutamate + 2-dehydropantoate
-
Escherichia coli 5,10-methylenetetrahydropteroylpentaglutamate + 3-methyl-2-oxobutanoate + H2O
-
r
tetrahydropteroyltetraglutamate + 2-dehydropantoate
-
Escherichia coli 5,10-methylenetetrahydropteroyltetraglutamate + 3-methyl-2-oxobutanoate + H2O
-
r
tetrahydropteroyltriglutamate + 2-dehydropantoate
-
Escherichia coli 5,10-methylenetetrahydropteroyltriglutamate + 3-methyl-2-oxobutanoate + H2O
-
r

Subunits

Subunits Comment Organism
decamer 10 * 27000, SDS-PAGE, 10 * 25700, amino acid analysis Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
70 80 reverse reaction, activity decreases rapidly above 80°C Escherichia coli

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
80
-
rapid denaturation above Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
additional information
-
pI: 4.4 Escherichia coli
7 7.6
-
Escherichia coli

pH Range

pH Minimum pH Maximum Comment Organism
5 9 about 50% of activity maximum at pH 6 and 9, inactive below pH 5 Escherichia coli

pH Stability

pH Stability pH Stability Maximum Comment Organism
4.5
-
rapid inactivation below Escherichia coli
5 10 stable Escherichia coli

Cofactor

Cofactor Comment Organism Structure
5,10-methylenetetrahydrofolate
-
Escherichia coli
tetrahydrofolate absolute requirement for tetrahydrofolate Escherichia coli