Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | required | Escherichia coli |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine | Escherichia coli | - |
AMP + (2-amino-4-hydroxy-7,8-dihydropteridin-6-yl)methyl diphosphate | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | P26281 | - |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
ATP + 6-hydroxymethyl-7,8-dihydropterin = AMP + 6-hydroxymethyl-7,8-dihydropterin diphosphate | during its catalytic cycle, the enzyme must assume at least five liganded forms: the apoenzyme form (without either of the substrates), the binary substrate complex with MgATP, the ternary substrate complex (Michaelis complex) with MgATP and 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine, the ternary product complex with AMP and 6-hydroxymethyl-7,8-dihydropterin diphosphate (HPPP), and the binary product complex with HPPP | Escherichia coli |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine | - |
Escherichia coli | AMP + (2-amino-4-hydroxy-7,8-dihydropteridin-6-yl)methyl diphosphate | - |
? |
Subunits | Comment | Organism |
---|---|---|
More | the enzyme has an alphabetaalpha fold with a central six-stranded beta-sheet sandwiched by two alpha-helices on either side | Escherichia coli |
Synonyms | Comment | Organism |
---|---|---|
6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase | - |
Escherichia coli |
HPPK | - |
Escherichia coli |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
ATP | - |
Escherichia coli |
General Information | Comment | Organism |
---|---|---|
metabolism | 6-hydroxymethyl-7,8-dihydropterin diphosphokinase catalyzes the first reaction in the folate biosynthetic pathway | Escherichia coli |
additional information | putative large-scale induced-fit conformational change of enzyme HPPK. The loops 2 and 3 remain rather flexible when the enzyme is in its apoform, but loops 2 and 3 adopt the open, semi-open, and closed conformations throughout its catalytic cycle, flexibility of the three catalytic loops in the apoform of the enzyme. Molecular dynamics simulations of the apoenzyme at two different temperatures, overview | Escherichia coli |
physiological function | the enzyme is essential for microbial growth | Escherichia coli |