Literature summary extracted from
Berglez, J.; Pilling, P.; Macreadie, I.; Fernley, R.T.
Purification, properties, and crystallization of Saccharomyces cerevisiae dihydropterin pyrophosphokinase-dihydropteroate synthase (2005), Protein Expr. Purif., 41, 355-362.
Cloned(Commentary)
EC Number |
Cloned (Comment) |
Organism |
---|
2.5.1.15 |
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)
EC Number |
Crystallization (Comment) |
Organism |
---|
2.5.1.15 |
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]
EC Number |
KM Value [mM] |
KM Value Maximum [mM] |
Substrate |
Comment |
Organism |
Structure |
---|
2.5.1.15 |
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 |
|
2.5.1.15 |
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]
EC Number |
Molecular Weight [Da] |
Molecular Weight Maximum [Da] |
Comment |
Organism |
---|
2.5.1.15 |
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
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
2.5.1.15 |
Saccharomyces cerevisiae |
P53848 |
- |
- |
Purification (Commentary)
EC Number |
Purification (Comment) |
Organism |
---|
2.5.1.15 |
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]
EC Number |
Specific Activity Minimum [µmol/min/mg] |
Specific Activity Maximum [µmol/min/mg] |
Comment |
Organism |
---|
2.5.1.15 |
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
EC Number |
Storage Stability |
Organism |
---|
2.5.1.15 |
-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 |
2.5.1.15 |
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)
EC Number |
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
---|
2.5.1.15 |
2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine + 4-aminobenzoate |
- |
Saccharomyces cerevisiae |
7,8-dihydropteroate + diphosphate |
- |
? |
|
Subunits
EC Number |
Subunits |
Comment |
Organism |
---|
2.5.1.15 |
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
EC Number |
Synonyms |
Comment |
Organism |
---|
2.5.1.15 |
DHPS |
- |
Saccharomyces cerevisiae |
2.5.1.15 |
dihydroneopterin aldolase-dihydropterin pyrophosphokinase-dihydropteroate synthase |
trifunctional enzyme |
Saccharomyces cerevisiae |
pH Optimum
EC Number |
pH Optimum Minimum |
pH Optimum Maximum |
Comment |
Organism |
---|
2.5.1.15 |
8.5 |
- |
dihydropteroate synthase activity of the recombinant bifunctional fusion protein consisting of dihydropterin diphosphokinase and dihyropteroate synthase domains |
Saccharomyces cerevisiae |
pH Range
EC Number |
pH Minimum |
pH Maximum |
Comment |
Organism |
---|
2.5.1.15 |
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
EC Number |
pH Stability |
pH Stability Maximum |
Comment |
Organism |
---|
2.5.1.15 |
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 |