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Literature summary extracted from
- The crystal structure and biochemical properties of DHBPS from Streptococcus pneumoniae, a potential anti-infective target for Gram-positive bacteria (2013), Protein Expr. Purif., 91, 161-168.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 4.1.99.12 | recombinant expression of wild-type andn mutant soluble His-tagged enzymes in Escherichia coli strain BL21(DE3) | Streptococcus pneumoniae |
Crystallization (Commentary)
| EC Number | Crystallization (Comment) | Organism |
|---|---|---|
| 4.1.99.12 | purified recombinant His-tagged enzyme, hanging-drop vapor diffusion method, mixing of 0.001 ml of 5 mg/ml protein in 5 mM Tris-HCl, pH 8.0, and 50 mM NaCl, with 0.001 ml of reservoir solution containing ammonium sulfate 2.0 M and 0.1 M BisTris pH7.02, X-ray diffraction structure determination and analysis at 2.0 A resolution | Streptococcus pneumoniae |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 4.1.99.12 | D32A | site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme | Streptococcus pneumoniae |
| 4.1.99.12 | E163A | site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme | Streptococcus pneumoniae |
| 4.1.99.12 | E30A | site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme | Streptococcus pneumoniae |
| 4.1.99.12 | H125A | site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme | Streptococcus pneumoniae |
| 4.1.99.12 | H142A | site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme | Streptococcus pneumoniae |
| 4.1.99.12 | T143A | site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme | Streptococcus pneumoniae |
| 4.1.99.12 | T96A | site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme | Streptococcus pneumoniae |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 4.1.99.12 | 0.181 | - |
D-ribulose 5-phosphate | pH 7.5, 37°C | Streptococcus pneumoniae |  |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 4.1.99.12 | Co2+ | activates | Streptococcus pneumoniae | |
| 4.1.99.12 | Fe3+ | the enzyme shows activity in the presence of the trivalent metal ion, Fe3+ | Streptococcus pneumoniae | |
| 4.1.99.12 | Mg2+ | required, best physiological metal activator, the divalent metal ion, Mg2+ plays a crucial role for acid/base catalysis | Streptococcus pneumoniae | |
| 4.1.99.12 | Mn2+ | activates | Streptococcus pneumoniae | |
| 4.1.99.12 | additional information | no activity with Cu2+ | Streptococcus pneumoniae | |
| 4.1.99.12 | Ni2+ | activates | Streptococcus pneumoniae | |
| 4.1.99.12 | Pb2+ | activates | Streptococcus pneumoniae | |
| 4.1.99.12 | Zn2+ | activates | Streptococcus pneumoniae | |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 4.1.99.12 | 35350 | - |
recombinant enzyme, gel filtration | Streptococcus pneumoniae |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 4.1.99.12 | D-ribulose 5-phosphate | Streptococcus pneumoniae | - |
formate + L-3,4-dihydroxybutan-2-one 4-phosphate | - |
? | |
| 4.1.99.12 | D-ribulose 5-phosphate | Streptococcus pneumoniae TIGR 4 | - |
formate + L-3,4-dihydroxybutan-2-one 4-phosphate | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 4.1.99.12 | Streptococcus pneumoniae | A0A0H2UN41 | gene Sp0176 | - |
| 4.1.99.12 | Streptococcus pneumoniae TIGR 4 | A0A0H2UN41 | gene Sp0176 | - |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 4.1.99.12 | recombinant wild-type and mutant soluble His-tagged enzymes from Escherichia coli strain BL21(DE3) by nickel affinity and anion exchange chromatography | Streptococcus pneumoniae |
Specific Activity [micromol/min/mg]
| EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|---|
| 4.1.99.12 | 0.109 | - |
substrate D-ribulose 5-phosphate, pH 7.5, 37°C | Streptococcus pneumoniae |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 4.1.99.12 | D-ribulose 5-phosphate | - |
Streptococcus pneumoniae | formate + L-3,4-dihydroxybutan-2-one 4-phosphate | - |
? | |
| 4.1.99.12 | D-ribulose 5-phosphate | - |
Streptococcus pneumoniae TIGR 4 | formate + L-3,4-dihydroxybutan-2-one 4-phosphate | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 4.1.99.12 | dimer | DHBPS exists as a homodimer in solution, and the active sites are located at the dimeric interface formed by charged residues from two monomers | Streptococcus pneumoniae |
| 4.1.99.12 | More | the enzyme comprises one beta-sheet (five-stranded) and eight alpha-helices, adopting a three-layered alpha-beta-alpha sandwich fold | Streptococcus pneumoniae |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 4.1.99.12 | DHBPS | - |
Streptococcus pneumoniae |
| 4.1.99.12 | Sp0176 | - |
Streptococcus pneumoniae |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 4.1.99.12 | 33 | - |
- |
Streptococcus pneumoniae |
Temperature Range [°C]
| EC Number | Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 4.1.99.12 | 5 | 55 | activity range, profile overview. Highest activity at 33°C, while at 30°C and 37°C, the activity decreases sharply to approximately 15-30% of the activity at 33°C | Streptococcus pneumoniae |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 4.1.99.12 | 7.5 | - |
assay at | Streptococcus pneumoniae |
pH Range
| EC Number | pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|---|
| 4.1.99.12 | 6 | 8 | narrow optimum, no activity below or above, profile overview | Streptococcus pneumoniae |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 4.1.99.12 | metabolism | 3,4-dihydroxy-2-butanone-4-phosphate synthase is one of the key enzymes in the biosynthesis of riboflavin | Streptococcus pneumoniae |
| 4.1.99.12 | additional information | the two key enzymes of the riboflavin biosynthetic pathway, DHBPS and GTP cyclohydrolaseII (GCHII), EC 3.5.4.25,are fused together into the bifunctional enzyme encoded by Sp0176 gene of Streptococcus pneumoniae strain TIGR 4, DHBPS active site architecture, overview | Streptococcus pneumoniae |
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