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

BRENDA support

Literature summary extracted from

  • Teller, J.H.; Powers, S.G.; Snell, E.E.
    Ketopantoate hydroxymethyltransferase. I. Purification and role in pantothenate biosynthesis (1976), J. Biol. Chem., 251, 3780-3785.
    View publication on PubMed

General Stability

EC Number General Stability Organism
2.1.2.11 ammonium sulfate fractionation inactivates, resistant to urea denaturation Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.1.2.11 additional information
-
additional information low Km-values for its substrates 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 Salmonella enterica subsp. enterica serovar Typhimurium first committed step in pantothenate biosynthesis tetrahydrofolate + 2-dehydropantoate
-
?
2.1.2.11 5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate Escherichia coli first committed step in pantothenate biosynthesis tetrahydrofolate + 2-dehydropantoate enzyme is responsible for catalysis of ketopantoate formation in vivo ?

Organism

EC Number Organism UniProt Comment Textmining
2.1.2.11 Escherichia coli
-
-
-
2.1.2.11 Escherichia coli
-
strains W and B
-
2.1.2.11 Salmonella enterica subsp. enterica serovar Typhimurium
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.1.2.11 strain K12, 2450fold purification Escherichia coli

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.1.2.11 7.3
-
-
Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.1.2.11 5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
-
Salmonella enterica subsp. enterica serovar Typhimurium tetrahydrofolate + 2-dehydropantoate
-
r
2.1.2.11 5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
-
Escherichia coli tetrahydrofolate + 2-dehydropantoate formation of ketopantoate, syn. 2-keto-3,3-dimethyl-4-hydroxybutyrate, tetrahydrofolate-dependent enzyme r
2.1.2.11 5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate first committed step in pantothenate biosynthesis Salmonella enterica subsp. enterica serovar Typhimurium tetrahydrofolate + 2-dehydropantoate
-
?
2.1.2.11 5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate first committed step in pantothenate biosynthesis Escherichia coli tetrahydrofolate + 2-dehydropantoate enzyme is responsible for catalysis of ketopantoate formation in vivo ?

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.1.2.11 37
-
assay at Salmonella enterica subsp. enterica serovar Typhimurium
2.1.2.11 37
-
assay at Escherichia coli

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
2.1.2.11 55
-
treatment at 55°C largely destroys enzyme in crude extract, partially purified enzyme is more heat-stabile Escherichia coli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.1.2.11 8
-
at or below Escherichia coli

pH Range

EC Number pH Minimum pH Maximum Comment Organism
2.1.2.11 10
-
no ketopantoate formation above pH 10 Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
2.1.2.11 5,10-methylenetetrahydrofolate
-
Salmonella enterica subsp. enterica serovar Typhimurium
2.1.2.11 5,10-methylenetetrahydrofolate
-
Escherichia coli
2.1.2.11 tetrahydrofolate
-
Salmonella enterica subsp. enterica serovar Typhimurium
2.1.2.11 tetrahydrofolate tetrahydrofolate-dependent reaction Escherichia coli