Cloned (Comment) | Organism |
---|---|
expression of N-terminally His10-tagged wild-type and mutant enzymes in enzyme-deficient strain BLR(DE3) | Escherichia coli K-12 |
expression of N-terminally His10-tagged wild-type and mutant enzymes in enzyme-deficient strain BLR(DE3) | Methylomonas aminofaciens |
Protein Variants | Comment | Organism |
---|---|---|
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/R139V/T169A/R192A | 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 |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.67 | - |
3-dehydro-L-gulonate 6-phosphate | pH 7.5, 25°C, recombinant wild-type enzyme | Escherichia coli K-12 | |
0.91 | - |
3-dehydro-L-gulonate 6-phosphate | pH 7.5, 25°C, recombinant mutant E112D/R139V/T169A | Escherichia coli K-12 | |
5.4 | - |
3-dehydro-L-gulonate 6-phosphate | pH 7.5, 25°C, recombinant enzyme | Methylomonas aminofaciens |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | dependent on | Escherichia coli K-12 |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
3-dehydro-L-gulonate 6-phosphate + H+ | Methylomonas aminofaciens | - |
L-xylulose 5-phosphate + CO2 | - |
? | |
3-dehydro-L-gulonate 6-phosphate + H+ | Escherichia coli K-12 | step in the catabolic pathway of L-ascorbate utilization | L-xylulose 5-phosphate + CO2 | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli K-12 | - |
- |
- |
Methylomonas aminofaciens | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
3-dehydro-L-gulonate 6-phosphate + H+ | - |
Methylomonas aminofaciens | L-xylulose 5-phosphate + CO2 | - |
? | |
3-dehydro-L-gulonate 6-phosphate + H+ | stereochemistry | Escherichia coli K-12 | L-xylulose 5-phosphate + CO2 | - |
? | |
3-dehydro-L-gulonate 6-phosphate + H+ | step in the catabolic pathway of L-ascorbate utilization | Escherichia coli K-12 | L-xylulose 5-phosphate + CO2 | - |
? | |
additional information | the D-arabino-hex-3-ulose 6-phosphate synthase of Methylomonas aminofaciens also performs the 3-keto-L-gulonate 6-phosphate decarboxylase reaction with lower activity than for the preferred reaction catalyzing Mg2+-dependent aldol condensation between formaldehyde and D-ribulose 5-phosphate, proton exchange reaction rates, overview | Methylomonas aminofaciens | ? | - |
? | |
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, proton exchange reaction rates, overview | Escherichia coli K-12 | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
dimer | (beta/alpha)8-barrel enzyme | Escherichia coli K-12 |
More | (beta/alpha)8-barrel enzyme | Methylomonas aminofaciens |
Synonyms | Comment | Organism |
---|---|---|
3-keto-L-gulonate 6-phosphate decarboxylase | - |
Escherichia coli K-12 |
3-keto-L-gulonate 6-phosphate decarboxylase | - |
Methylomonas aminofaciens |
KGPDC | - |
Escherichia coli K-12 |
KGPDC | - |
Methylomonas aminofaciens |
More | the enzyme belongs to the orotidine 5'-monophosphate decarboxylase OMPDC suprafamily | Escherichia coli K-12 |
More | the enzyme belongs to the orotidine 5'-monophosphate decarboxylase OMPDC suprafamily | Methylomonas aminofaciens |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | - |
assay at | Escherichia coli K-12 |
25 | - |
assay at | Methylomonas aminofaciens |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
2.4 | - |
3-dehydro-L-gulonate 6-phosphate | pH 7.5, 25°C, recombinant mutant E112D/R139V/T169A | Escherichia coli K-12 | |
15 | - |
3-dehydro-L-gulonate 6-phosphate | pH 7.5, 25°C, recombinant enzyme | Methylomonas aminofaciens | |
51 | - |
3-dehydro-L-gulonate 6-phosphate | pH 7.5, 25°C, recombinant wild-type enzyme | Escherichia coli K-12 |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.5 | - |
assay at | Escherichia coli K-12 |
7.5 | - |
assay at | Methylomonas aminofaciens |