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Literature summary for 2.1.2.11 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

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

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information low Km-values for its substrates 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 Salmonella enterica subsp. enterica serovar Typhimurium first committed step in pantothenate biosynthesis tetrahydrofolate + 2-dehydropantoate
-
?
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

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

Purification (Commentary)

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

Specific Activity [micromol/min/mg]

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
-
Salmonella enterica subsp. enterica serovar Typhimurium tetrahydrofolate + 2-dehydropantoate
-
r
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
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate first committed step in pantothenate biosynthesis Salmonella enterica subsp. enterica serovar Typhimurium tetrahydrofolate + 2-dehydropantoate
-
?
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]

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

Temperature Stability [°C]

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

pH Optimum

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

pH Range

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

Cofactor

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