Cloned (Comment) | Organism |
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expression of N-terminally His10-tagged wild-type and mutant enzymes in enzyme-deficient strain BLR(DE3) | Escherichia coli K-12 |
Crystallization (Comment) | Organism |
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purified recombinant wild-type and mutant enzymes E112D/R139V, E112D/T169A, and E112D/R139V/T169A, 15 mg/ml protein in 50 mM HEPES, pH 7.5, 5 mM MgCl2, 100 mM NaCl, micro-batch method, 0.01 ml protein solution mixed with equal volume of crystallization solution containing 16% monomethyl PEG 5000, 100 mM Bis-Tris propane, pH 7.0, 5 mM MgCl2, and 25 mM L-xylulose 5-phosphate or D-ribulose 5-phosphate, cryoprotection of crystals in 15% monomethylPEG 5000, 100 mM PIPES, pH 7.0, 15% ethylene glycol, 200 mM NaCl, and 50 mM L-threonohydroxamate 4-phosphate or 50 mM D-ribulose 5-phosphate, X-ray diffraction structure determination and analysis at 1.6-1.8 A resolution, molecular replacement | Escherichia coli K-12 |
Protein Variants | Comment | Organism |
---|---|---|
E112D/R139V | site-directed mutagenesis, mutations alter the Escherichia coli residues to those of Methylomonas aminofaciens D-arabino-hex-3-ulose 6-phosphate synthase, a homologous enzyme, also altering the enzyme activity of the 3-keto-L-gulonate 6-phosphate decarboxylase performing th Mg2+-dependent aldol condensation between formaldehyde and D-ribulose 5-phosphate with highly increased activity compared to the wild-type enzyme | Escherichia coli K-12 |
E112D/R139V/T169A | site-directed mutagenesis, mutations alter the Escherichia coli residues to those of Methylomonas aminofaciens D-arabino-hex-3-ulose 6-phosphate synthase, a homologous enzyme, also altering the enzyme activity of the 3-keto-L-gulonate 6-phosphate decarboxylase performing th Mg2+-dependent aldol condensation between formaldehyde and D-ribulose 5-phosphate with highly increased activity compared to the wild-type enzyme | Escherichia coli K-12 |
E112D/T169A | site-directed mutagenesis, mutations alter the Escherichia coli residues to those of Methylomonas aminofaciens D-arabino-hex-3-ulose 6-phosphate synthase, a homologous enzyme, also altering the enzyme activity of the 3-keto-L-gulonate 6-phosphate decarboxylase performing th Mg2+-dependent aldol condensation between formaldehyde and D-ribulose 5-phosphate with highly increased activity compared to the wild-type enzyme | Escherichia coli K-12 |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
3-dehydro-L-gulonate 6-phosphate + H+ | Escherichia coli K-12 | - |
L-xylulose 5-phosphate + CO2 | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli K-12 | P39304 | - |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
3-dehydro-L-gulonate 6-phosphate + H+ = L-xylulose 5-phosphate + CO2 | active site structure, substrate binding structure, structure-function relationship, overview | Escherichia coli K-12 |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
3-dehydro-L-gulonate 6-phosphate + H+ | - |
Escherichia coli K-12 | L-xylulose 5-phosphate + CO2 | - |
? | |
additional information | the enzyme also performs the Methylomonas aminofaciens D-arabino-hex-3-ulose 6-phosphate synthase reaction with low activity catalyzing Mg2+-dependent aldol condensation between formaldehyde and D-ribulose 5-phosphate, while the Methylomonas aminofaciens enzyme also performs the 3-keto-L-gulonate 6-phosphate decarboxylase reaction, overview | Escherichia coli K-12 | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
3-keto-L-gulonate 6-phosphate decarboxylase | - |
Escherichia coli K-12 |
KGPDC | - |
Escherichia coli K-12 |
More | the enzyme belongs to the orotidine 5'-monophosphate decarboxylase OMPDC suprafamily | Escherichia coli K-12 |