EC Number | Application | Comment | Organism |
---|---|---|---|
2.1.2.11 | pharmacology | enzyme might be an attractive target for inhibitor design | Mycobacterium tuberculosis |
EC Number | Cloned (Comment) | Organism |
---|---|---|
2.1.2.11 | panB gene encoding enzyme is cloned and overexpressed in Escherichia coli BL21 (DE3) | Mycobacterium tuberculosis |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
2.1.2.11 | additional information | not inhibited by methylenetetrahydrofolate, i.e. equimolar formaldehyde and tetrahydrofolate, at concentrations up to 2 mM | Mycobacterium tuberculosis |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
2.1.2.11 | additional information | - |
additional information | - |
Mycobacterium tuberculosis | |
2.1.2.11 | 0.24 | - |
3-methyl-2-oxobutanoate | - |
Mycobacterium tuberculosis | |
2.1.2.11 | 0.82 | - |
5,10-methylenetetrahydrofolate | - |
Mycobacterium tuberculosis |
EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|---|
2.1.2.11 | soluble | - |
Mycobacterium tuberculosis | - |
- |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
2.1.2.11 | Ca2+ | substrate enolization is divalent metal-dependent with a preference for metal ions in decreasing order: Mg2+, Zn2+, Co2+, Ni2+, Ca2+ | Mycobacterium tuberculosis | |
2.1.2.11 | Ca2+ | Km: 0.27 mM, the reaction is divalent metal-dependent with descending order of preference: Mg2+, Zn2+, Co2+, Ni2+, Ca2+ | Mycobacterium tuberculosis | |
2.1.2.11 | Co2+ | substrate enolization is divalent metal-dependent with a preference for metal ions in decreasing order: Mg2+, Zn2+, Co2+, Ni2+, Ca2+ | Mycobacterium tuberculosis | |
2.1.2.11 | Co2+ | Km: 0.33 mM, the reaction is divalent metal-dependent with descending order of preference: Mg2+, Zn2+, Co2+, Ni2+, Ca2+ | Mycobacterium tuberculosis | |
2.1.2.11 | Mg2+ | substrate enolization is divalent metal-dependent with a preference for metal ions in decreasing order: Mg2+, Zn2+, Co2+, Ni2+, Ca2+ | Mycobacterium tuberculosis | |
2.1.2.11 | Mg2+ | Km: 0.61 mM, the reaction is divalent metal-dependent with descending order of preference: Mg2+, Zn2+, Co2+, Ni2+, Ca2+ | Mycobacterium tuberculosis | |
2.1.2.11 | additional information | metalloenzyme, inactive in absence of divalent metals, enzyme binds metal ions that assist in the polarization of the carbonyl group and stabilize the enolate anion | Mycobacterium tuberculosis | |
2.1.2.11 | Ni2+ | substrate enolization is divalent metal-dependent with a preference for metal ions in decreasing order: Mg2+, Zn2+, Co2+, Ni2+, Ca2+ | Mycobacterium tuberculosis | |
2.1.2.11 | Ni2+ | Km: 0.45 mM, the reaction is divalent metal-dependent with descending order of preference: Mg2+, Zn2+, Co2+, Ni2+, Ca2+ | Mycobacterium tuberculosis | |
2.1.2.11 | Zn2+ | substrate enolization is divalent metal-dependent with a preference for metal ions in decreasing order: Mg2+, Zn2+, Co2+, Ni2+, Ca2+ | Mycobacterium tuberculosis | |
2.1.2.11 | Zn2+ | Km: 0.08 mM, the reaction is divalent metal-dependent with descending order of preference: Mg2+, Zn2+, Co2+, Ni2+, Ca2+ | Mycobacterium tuberculosis |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
2.1.2.11 | 29000 | - |
recombinant enzyme expressed in Escherichia coli BL21 (DE3): 4 * 29000, SDS-PAGE, 4 * 29202, electrospray ionization/mass spectrometry, 4 * 29366, calculated from the amino acid sequence | Mycobacterium tuberculosis |
2.1.2.11 | 29202 | - |
recombinant enzyme expressed in Escherichia coli BL21 (DE3): 4 * 29000, SDS-PAGE, 4 * 29202, electrospray ionization/mass spectrometry, 4 * 29366, calculated from the amino acid sequence | Mycobacterium tuberculosis |
2.1.2.11 | 29366 | - |
recombinant enzyme expressed in Escherichia coli BL21 (DE3): 4 * 29000, SDS-PAGE, 4 * 29202, electrospray ionization/mass spectrometry, 4 * 29366, calculated from the amino acid sequence | Mycobacterium tuberculosis |
2.1.2.11 | 120000 | - |
gel filtration | Mycobacterium tuberculosis |
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 | Mycobacterium tuberculosis | first committed step in pantothenate biosynthesis | tetrahydrofolate + 2-dehydropantoate | - |
? | |
2.1.2.11 | 5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate | Mycobacterium tuberculosis | enzyme may be the rate-limiting reaction in pantothenate biosynthesis | tetrahydrofolate + 2-dehydropantoate | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.1.2.11 | Mycobacterium tuberculosis | - |
- |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
2.1.2.11 | purification of recombinant enzyme expressed in Escherichia coli BL21 (DE3) | Mycobacterium tuberculosis |
EC Number | Reaction | Comment | Organism | Reaction ID |
---|---|---|---|---|
2.1.2.11 | 5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate + H2O = tetrahydrofolate + 2-dehydropantoate | stereochemistry | Mycobacterium tuberculosis | |
2.1.2.11 | 5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate + H2O = tetrahydrofolate + 2-dehydropantoate | sequential kinetic mechanism, chemical mechanism | Mycobacterium tuberculosis |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.1.2.11 | 5,10-methylenetetrahydrofolate + 2-oxo-4-methylthiobutyrate | about 50% of the activity with 3-methyl-2-oxobutanoate | Mycobacterium tuberculosis | tetrahydrofolate + ? | - |
? | |
2.1.2.11 | 5,10-methylenetetrahydrofolate + 2-oxobutyrate | about 50% of the activity with 3-methyl-2-oxobutanoate | Mycobacterium tuberculosis | tetrahydrofolate + ? | - |
? | |
2.1.2.11 | 5,10-methylenetetrahydrofolate + 2-oxopentanoate | about 30% of the activity with 3-methyl-2-oxobutanoate | Mycobacterium tuberculosis | tetrahydrofolate + ? | - |
? | |
2.1.2.11 | 5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate | - |
Mycobacterium tuberculosis | tetrahydrofolate + 2-dehydropantoate | - |
? | |
2.1.2.11 | 5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate | first committed step in pantothenate biosynthesis | Mycobacterium tuberculosis | tetrahydrofolate + 2-dehydropantoate | - |
? | |
2.1.2.11 | 5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate | enzyme may be the rate-limiting reaction in pantothenate biosynthesis | Mycobacterium tuberculosis | tetrahydrofolate + 2-dehydropantoate | - |
? | |
2.1.2.11 | 5,10-methylenetetrahydrofolate + 3-methyl-2-oxopentanoate | about 65% of the activity with 3-methyl-2-oxobutanoate | Mycobacterium tuberculosis | tetrahydrofolate + ? | - |
? | |
2.1.2.11 | 5,10-methylenetetrahydrofolate + pyruvate | about 20% of the activity with 3-methyl-2-oxobutanoate | Mycobacterium tuberculosis | tetrahydrofolate + ? | - |
? | |
2.1.2.11 | formaldehyde + 3-methyl-2-oxobutanoate | enzyme catalyzes methylenetetrahydrofolate-independent hydroxymethyltransferase reaction between free formaldehyde and alpha-ketoisovalerate, formaldehyde is unlikely to be the natural substrate | Mycobacterium tuberculosis | 2-dehydropantoate | - |
? | |
2.1.2.11 | additional information | enzyme catalyzes deuterium exchange in the methylenetetrahydrofolate-independent enolization of alpha-ketoisovalerate or other alpha-keto acids with decreasing efficiency: alpha-ketoisovalerate, alpha-ketobutyrate, alpha-ketovalerate, pyruvate, alpha-ketomethylthiobutyrate, alpha-ketoisocaproate, stereochemistry, first step in the reaction leading to ketopantoate is the enolization of alpha-ketoisovalerate to form the stabilized carbanion | Mycobacterium tuberculosis | ? | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
2.1.2.11 | tetramer | recombinant enzyme expressed in Escherichia coli BL21 (DE3): 4 * 29000, SDS-PAGE, 4 * 29202, electrospray ionization/mass spectrometry, 4 * 29366, calculated from the amino acid sequence | Mycobacterium tuberculosis |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
2.1.2.11 | ketopantoate hydroxymethyltransferase | - |
Mycobacterium tuberculosis |
2.1.2.11 | PanB | - |
Mycobacterium tuberculosis |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
2.1.2.11 | 37 | - |
assay at | Mycobacterium tuberculosis |
EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
2.1.2.11 | 0.78 | - |
5,10-methylenetetrahydrofolate | - |
Mycobacterium tuberculosis | |
2.1.2.11 | 0.78 | - |
3-methyl-2-oxobutanoate | - |
Mycobacterium tuberculosis | |
2.1.2.11 | 0.783 | - |
3-methyl-2-oxobutanoate | - |
Mycobacterium tuberculosis |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
2.1.2.11 | 7 | 7.5 | - |
Mycobacterium tuberculosis |
2.1.2.11 | 7 | 7.5 | rate of substrate enolization is pH-dependent with optimal activity in the range of | Mycobacterium tuberculosis |
EC Number | pH Stability | pH Stability Maximum | Comment | Organism |
---|---|---|---|---|
2.1.2.11 | 5.5 | - |
loss of proper protein folding at pH values lower than 5.5 | Mycobacterium tuberculosis |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
2.1.2.11 | 5,10-methylenetetrahydrofolate | 5,10-methylenetetrahydrofolate as cofactor | Mycobacterium tuberculosis | |
2.1.2.11 | tetrahydrofolate | - |
Mycobacterium tuberculosis |