Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary 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

EC Number Inhibitors Comment Organism Structure
2.1.2.11 3-Methyl-2-butanone 5 mM, 27% inhibition Escherichia coli
2.1.2.11 coenzyme A above 1 mM Escherichia coli
2.1.2.11 D-valine 5 mM, 16% inhibition Escherichia coli
2.1.2.11 formaldehyde 0.8 mM, partial inhibition Escherichia coli
2.1.2.11 Isovalerate 5 mM, 39% inhibition Escherichia coli
2.1.2.11 L-valine 5 mM, 23% inhibition Escherichia coli
2.1.2.11 additional information not inactivated by borohydride reduction in the presence of excess substrates Escherichia coli
2.1.2.11 Pantoate 0.05 mM or above Escherichia coli
2.1.2.11 pantothenate 0.5 mM or above Escherichia coli
2.1.2.11 pyruvate 5 mM, 38% inhibition Escherichia coli
2.1.2.11 tetrahydrofolate 0.38 mM, partial inhibition Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.1.2.11 0.1
-
Tetrahydropteroylpentaglutamate
-
Escherichia coli
2.1.2.11 0.1
-
tetrahydropteroyltetraglutamate
-
Escherichia coli
2.1.2.11 0.16
-
ketopantoate
-
Escherichia coli
2.1.2.11 0.17
-
tetrahydropteroylhexaglutamate
-
Escherichia coli
2.1.2.11 0.18
-
tetrahydropteroyltriglutamate
-
Escherichia coli
2.1.2.11 0.18
-
tetrahydrofolate forward and reverse reaction, methylenetetrahydrofolate: formaldehyde + tetrahydrofolate Escherichia coli
2.1.2.11 0.25
-
tetrahydropteroyldiglutamate
-
Escherichia coli
2.1.2.11 0.29
-
tetrahydropteroylheptaglutamate
-
Escherichia coli
2.1.2.11 0.33
-
tetrahydropteroylmonoglutamate
-
Escherichia coli
2.1.2.11 1.1
-
3-methyl-2-oxobutanoate
-
Escherichia coli
2.1.2.11 2.9
-
2-oxobutyrate
-
Escherichia coli
2.1.2.11 5.9
-
3-methyl-2-oxopentanoate
-
Escherichia coli
2.1.2.11 5.9
-
formaldehyde methylenetetrahydrofolate: formaldehyde + tetrahydrofolate Escherichia coli
2.1.2.11 25
-
2-oxopentanoate
-
Escherichia coli

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.1.2.11 Co2+ activates, Mg2+ is most active followed by Mn2+, Ni2+, Co2+ and Zn2+ Escherichia coli
2.1.2.11 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
2.1.2.11 Mn2+ activates, Mg2+ is most active followed by Mn2+, Ni2+, Co2+ and Zn2+ Escherichia coli
2.1.2.11 additional information not activated by Cu2+ and Fe2+ Escherichia coli
2.1.2.11 Ni2+ activates, Mg2+ is most active followed by Mn2+, Ni2+, Co2+ and Zn2+ Escherichia coli
2.1.2.11 Zn2+ activates, Mg2+ is most active followed by Mn2+, Ni2+, Co2+ and Zn2+ Escherichia coli

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.1.2.11 25700
-
10 * 27000, SDS-PAGE, 10 * 25700, amino acid analysis Escherichia coli
2.1.2.11 27000
-
10 * 27000, SDS-PAGE, 10 * 25700, amino acid analysis Escherichia coli
2.1.2.11 255000
-
sedimentation equilibrium Escherichia coli
2.1.2.11 285000
-
gel filtration Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.1.2.11 5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate Escherichia coli first committed step in pantothenate biosynthesis tetrahydrofolate + 2-dehydropantoate
-
?
2.1.2.11 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

EC Number Organism UniProt Comment Textmining
2.1.2.11 Escherichia coli
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.1.2.11
-
Escherichia coli

Reaction

EC Number Reaction Comment Organism Reaction ID
2.1.2.11 5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate + H2O = tetrahydrofolate + 2-dehydropantoate class II aldolase Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.1.2.11 5,10-methylenetetrahydrofolate + 2-oxobutyrate also a good substrate Escherichia coli ?
-
?
2.1.2.11 5,10-methylenetetrahydrofolate + 2-oxopentanoate
-
Escherichia coli ?
-
?
2.1.2.11 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
2.1.2.11 5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate first committed step in pantothenate biosynthesis Escherichia coli tetrahydrofolate + 2-dehydropantoate
-
?
2.1.2.11 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
-
?
2.1.2.11 5,10-methylenetetrahydrofolate + 3-methyl-2-oxopentanoate
-
Escherichia coli ?
-
?
2.1.2.11 formaldehyde + tetrahydrofolate
-
Escherichia coli methylentetrahydrofolate
-
?
2.1.2.11 additional information no substrates: pyruvate, isovalerate, D- and L-valine, 3-methyl-2-butanone Escherichia coli ?
-
?
2.1.2.11 tetrahydropteroyldiglutamate + 2-dehydropantoate
-
Escherichia coli 5,10-methylenetetrahydropteroyldiglutamate + 3-methyl-2-oxobutanoate + H2O
-
r
2.1.2.11 tetrahydropteroylheptaglutamate + 2-dehydropantoate
-
Escherichia coli 5,10-methylenetetrahydropteroylheptaglutamate + 3-methyl-2-oxobutanoate + H2O
-
r
2.1.2.11 tetrahydropteroylhexaglutamate + 2-dehydropantoate
-
Escherichia coli 5,10-methylenetetrahydropteroylhexaglutamate + 3-methyl-2-oxobutanoate + H2O
-
r
2.1.2.11 tetrahydropteroylpentaglutamate + 2-dehydropantoate
-
Escherichia coli 5,10-methylenetetrahydropteroylpentaglutamate + 3-methyl-2-oxobutanoate + H2O
-
r
2.1.2.11 tetrahydropteroyltetraglutamate + 2-dehydropantoate
-
Escherichia coli 5,10-methylenetetrahydropteroyltetraglutamate + 3-methyl-2-oxobutanoate + H2O
-
r
2.1.2.11 tetrahydropteroyltriglutamate + 2-dehydropantoate
-
Escherichia coli 5,10-methylenetetrahydropteroyltriglutamate + 3-methyl-2-oxobutanoate + H2O
-
r

Subunits

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

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.1.2.11 70 80 reverse reaction, activity decreases rapidly above 80°C Escherichia coli

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
2.1.2.11 80
-
rapid denaturation above Escherichia coli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.1.2.11 additional information
-
pI: 4.4 Escherichia coli
2.1.2.11 7 7.6
-
Escherichia coli

pH Range

EC Number pH Minimum pH Maximum Comment Organism
2.1.2.11 5 9 about 50% of activity maximum at pH 6 and 9, inactive below pH 5 Escherichia coli

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
2.1.2.11 4.5
-
rapid inactivation below Escherichia coli
2.1.2.11 5 10 stable Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
2.1.2.11 5,10-methylenetetrahydrofolate
-
Escherichia coli
2.1.2.11 tetrahydrofolate absolute requirement for tetrahydrofolate Escherichia coli