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 (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 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 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 | UniProt | Comment | Textmining |
---|---|---|---|
Saccharomyces cerevisiae | P53848 | - |
- |
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 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 | 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 | 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 | 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 | Comment | Organism |
---|---|---|
DHPS | - |
Saccharomyces cerevisiae |
dihydroneopterin aldolase-dihydropterin pyrophosphokinase-dihydropteroate synthase | trifunctional enzyme | Saccharomyces cerevisiae |
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 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 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 |