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Literature summary extracted from
- Potential anti-infective targets in pathogenic yeasts: structure and properties of 3,4-dihydroxy-2-butanone 4-phosphate synthase of Candida albicans (2004), J. Mol. Biol., 341, 1085-1096.
Application
| EC Number | Application | Comment | Organism |
|---|---|---|---|
| 4.1.99.12 | drug development | the enzyme is a potential anti-infective target in the pathogenic yeast | Candida albicans |
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 4.1.99.12 | functional expression of the synthetic gene in Escherichia coli strains XL1-Blue and M15 | Candida albicans |
Crystallization (Commentary)
| EC Number | Crystallization (Comment) | Organism |
|---|---|---|
| 4.1.99.12 | purified recombinant apoenzyme in complex with the substrate ribulose 5-phosphate, sitting drop vapour diffusion method, 0.003 ml of 17-34 mg/ml protein in 50 mM Tris-HCl, pH 7.5, is mixed with 0.001 ml of reservoir solution containing 85 mM sodium citrate, pH 5.0, and 17% PEG 8000, with or without 5 mM EDTA, equilibration against 0.3 ml reservoir solution, 0.003 ml of the complex solution is mixed with 0.001 ml of 90 mM Mes/NaOH, pH 6.0, containing 18% PEG 8000, addition of 2 mM D-ribulose 5-phosphate, 20°C, X-ray diffraction structure determination and analysis at 1.6-1.7 A resolution, molecular replacement, modelling | Candida albicans |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 4.1.99.12 | C59A | site-directed mutagenesis, the mutant shows 70% of wild-type enzyme activity | Candida albicans |
| 4.1.99.12 | D92A | site-directed mutagenesis, inactive mutant | Candida albicans |
| 4.1.99.12 | E166A | site-directed mutagenesis, inactive mutant | Candida albicans |
| 4.1.99.12 | Q181R/Q183R | site-directed mutagenesis, construction of a synthetic gene, derived from orf 6.2440, with nucleotide exchanges at positions 414, 426, 477, 480, and 581 | Candida albicans |
| 4.1.99.12 | Y87A | site-directed mutagenesis, the mutant shows 2% of wild-type enzyme activity | Candida albicans |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 4.1.99.12 | Ca2+ | not involved in catalysis, stabilize the enzyme | Candida albicans |  |
| 4.1.99.12 | Mg2+ | essential for activity | Candida albicans | |
| 4.1.99.12 | Zn2+ | not involved in catalysis, stabilize the enzyme | Candida albicans | |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 4.1.99.12 | 22530 | - |
2 * 22530, mass spectrometry, 2 * 22658, full-length enzyme, sequence calculation | Candida albicans |
| 4.1.99.12 | 22658 | - |
2 * 22530, mass spectrometry, 2 * 22658, full-length enzyme, sequence calculation | Candida albicans |
| 4.1.99.12 | 41000 | - |
recombinant enzyme, analytical ultracentrifugation, hydrodynamic studies | Candida albicans |
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 | Candida albicans | the enzyme is involved in riboflavin biosynthesis | formate + L-3,4-dihydroxy-2-butanone-4-phosphate | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 4.1.99.12 | Candida albicans | Q5A3V6 | wild-type enzyme; ATCC 10231D, orf 6.2440 | - |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 4.1.99.12 | recombinant enzyme, expressed from the synthetic gene in Escherichia coli, to homogeneity by hydrophobic interaction chromatography, ultrafiltration, and gel filtration | Candida albicans |
Reaction
| EC Number | Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|---|
| 4.1.99.12 | D-ribulose 5-phosphate = formate + L-3,4-dihydroxybutan-2-one 4-phosphate | reaction mechanism, the enzyme possesses an essential acidic active-site loop | Candida albicans |
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 | 0.332 | - |
purified recombinant enzyme | Candida albicans |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 4.1.99.12 | D-ribulose 5-phosphate | - |
Candida albicans | formate + L-3,4-dihydroxy-2-butanone-4-phosphate | - |
? | |
| 4.1.99.12 | D-ribulose 5-phosphate | the enzyme is involved in riboflavin biosynthesis | Candida albicans | formate + L-3,4-dihydroxy-2-butanone-4-phosphate | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 4.1.99.12 | dimer | 2 * 22530, mass spectrometry, 2 * 22658, full-length enzyme, sequence calculation | Candida albicans |
| 4.1.99.12 | More | the enzyme possesses an essential acidic active-site loop, active site structure, structure comparisons, overview | Candida albicans |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 4.1.99.12 | 3,4-dihydroxy-2-butanone 4-phosphate synthase | - |
Candida albicans |
| 4.1.99.12 | DHBPS | - |
Candida albicans |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 4.1.99.12 | 37 | - |
assay at | Candida albicans |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 4.1.99.12 | 7.5 | - |
assay at | Candida albicans |
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