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Literature summary for 2.1.2.11 extracted from
- Steric course of ketopantoate hydroxymethyltransferase in E. coli (1984), J. Am. Chem. Soc., 106, 4902-4906.
No PubMed abstract available
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 | biosynthesis of coenzyme A | tetrahydrofolate + 2-dehydropantoate | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
strain ATCC 23783 | - |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| 5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate + H2O = tetrahydrofolate + 2-dehydropantoate | stereochemistry | Escherichia coli | |
| 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 + 3-methyl-2-oxobutanoate | condensation of alpha-ketoisovalerate with the C-1 donor takes place stereospecifically at C-3 and proceeds in a retention mode at C-3, 5,10-methylenetetrahydrofolate-dependent enzyme | Escherichia coli | tetrahydrofolate + 2-dehydropantoate | - |
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 | biosynthesis of coenzyme A | Escherichia coli | tetrahydrofolate + 2-dehydropantoate | - |
? | |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| 5,10-methylenetetrahydrofolate | 5,10-methylenetetrahydrofolate-dependent enzyme | Escherichia coli | |
| additional information | no requirement of pyridoxal 5-phosphate as cofactor | Escherichia coli | |
| tetrahydrofolate | - |
Escherichia coli | |
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