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Literature summary for 2.5.1.15 extracted from
- Purification, properties, and crystallization of Saccharomyces cerevisiae dihydropterin pyrophosphokinase-dihydropteroate synthase (2005), Protein Expr. Purif., 41, 355-362.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| cDNA encoding dihydropterin pyrophosphokinase and dihyropteroate synthase domains of the trifunctional enzyme dihydroneopterin aldolase-dihydropterin pyrophosphokinase-dihydropteroate synthase is cloned. This bi-functional enzyme is expressed as a His6 fusion protein in Escherichia coli | Saccharomyces cerevisiae |
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| recombinant bifunctional fusion protein encoding dihydropterin pyrophosphokinase and dihyropteroate synthase domains of the trifunctional enzyme dihydroneopterin aldolase-dihydropterin pyrophosphokinase-dihydropteroate synthase | Saccharomyces cerevisiae |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.0004 | - |
2-Amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine | recombinant bifunctional fusion protein encoding dihydropterin pyrophosphokinase and dihyropteroate synthase domains of the trifunctional enzyme dihydroneopterin aldolase-dihydropterin pyrophosphokinase-dihydropteroate synthase | Saccharomyces cerevisiae |  |
| 0.0038 | - |
4-Aminobenzoate | recombinant bifunctional fusion protein encoding dihydropterin pyrophosphokinase and dihyropteroate synthase domains of the trifunctional enzyme dihydroneopterin aldolase-dihydropterin pyrophosphokinase-dihydropteroate synthase | Saccharomyces cerevisiae | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 110000 | - |
recombinant bifunctional fusion protein encoding dihydropterin pyrophosphokinase and dihyropteroate synthase domains of the trifunctional enzyme dihydroneopterin aldolase-dihydropterin pyrophosphokinase-dihydropteroate synthase, gel filtration | Saccharomyces cerevisiae |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Saccharomyces cerevisiae | P53848 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant bifunctional fusion protein encoding dihydropterin pyrophosphokinase and dihyropteroate synthase domains of the trifunctional enzyme dihydroneopterin aldolase-dihydropterin pyrophosphokinase-dihydropteroate synthase | Saccharomyces cerevisiae |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 1.25 | - |
recombinant bifunctional fusion protein encoding dihydropterin pyrophosphokinase and dihyropteroate synthase domains of the trifunctional enzyme dihydroneopterin aldolase-dihydropterin pyrophosphokinase-dihydropteroate synthase | Saccharomyces cerevisiae |
Storage Stability
| Storage Stability | Organism |
|---|---|
| -20°C, enzyme remains active in 50% glycerol, 1 mM MgCl2, 5 mM 2-mercaptoethanol, stable for long term-storage, dihydropteroate synthase activity of the recombinant bifunctional fusion protein encoding dihydropterin pyrophosphokinase and dihyropteroate synthase domains of the trifunctional enzyme dihydroneopterin aldolase-dihydropterin pyrophosphokinase-dihydropteroate synthase | Saccharomyces cerevisiae |
| 4°C, or -20°C, without glycerol, enzyme denaturates, dihydropteroate synthase activity of the recombinant bifunctional fusion protein encoding dihydropterin pyrophosphokinase and dihyropteroate synthase domains of the trifunctional enzyme dihydroneopterin aldolase-dihydropterin pyrophosphokinase-dihydropteroate synthase | Saccharomyces cerevisiae |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine + 4-aminobenzoate | - |
Saccharomyces cerevisiae | 7,8-dihydropteroate + diphosphate | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| dimer | recombinant bifunctional fusion protein encoding dihydropterin pyrophosphokinase and dihyropteroate synthase domains of the trifunctional enzyme dihydroneopterin aldolase-dihydropterin pyrophosphokinase-dihydropteroate synthase | Saccharomyces cerevisiae |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| DHPS | - |
Saccharomyces cerevisiae |
| dihydroneopterin aldolase-dihydropterin pyrophosphokinase-dihydropteroate synthase | trifunctional enzyme | Saccharomyces cerevisiae |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8.5 | - |
dihydropteroate synthase activity of the recombinant bifunctional fusion protein consisting of dihydropterin diphosphokinase and dihyropteroate synthase domains | Saccharomyces cerevisiae |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 7 | 9.3 | pH 7.0: about 50% of maximal activity, pH 9.3: about 60% of maximal activity, dihydropteroate synthase activity of the recombinant bifunctional fusion protein encoding dihydropterin pyrophosphokinase and dihyropteroate synthase domains of the trifunctional enzyme dihydroneopterin aldolase-dihydropterin pyrophosphokinase-dihydropteroate synthase | Saccharomyces cerevisiae |
pH Stability
| pH Stability | pH Stability Maximum | Comment | Organism |
|---|---|---|---|
| 6.5 | 10 | stable, dihydropteroate synthase activity of the recombinant bifunctional fusion protein encoding dihydropterin pyrophosphokinase and dihyropteroate synthase domains of the trifunctional enzyme dihydroneopterin aldolase-dihydropterin pyrophosphokinase-dihydropteroate synthase | Saccharomyces cerevisiae |
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