EC Number | Cloned (Comment) | Organism |
---|---|---|
4.1.1.85 | expression of N-terminally His10-tagged wild-type and mutant enzymes in enzyme-deficient strain BLR(DE3) | Escherichia coli K-12 |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
4.1.1.85 | D67A | site-directed mutagenesis, reduced activity compared to the wild-type enzyme | Escherichia coli K-12 |
4.1.1.85 | D67A/H136A | site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme | Escherichia coli K-12 |
4.1.1.85 | D67N | site-directed mutagenesis, reduced activity compared to the wild-type enzyme | Escherichia coli K-12 |
4.1.1.85 | D67N/H136A | site-directed mutagenesis, reduced activity compared to the wild-type enzyme | Escherichia coli K-12 |
4.1.1.85 | E112A | site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme | Escherichia coli K-12 |
4.1.1.85 | E112A/H136A | site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme | Escherichia coli K-12 |
4.1.1.85 | E112A/H136A/R139V | site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme | Escherichia coli K-12 |
4.1.1.85 | E112Q | site-directed mutagenesis, reduced activity compared to the wild-type enzyme | Escherichia coli K-12 |
4.1.1.85 | E112Q/H136A | site-directed mutagenesis, reduced activity compared to the wild-type enzyme | Escherichia coli K-12 |
4.1.1.85 | E112Q/H136A/R139V | site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme | Escherichia coli K-12 |
4.1.1.85 | E33K | site-directed mutagenesis, inactive mutant | Escherichia coli K-12 |
4.1.1.85 | H136A | site-directed mutagenesis, reduced activity compared to the wild-type enzyme | Escherichia coli K-12 |
4.1.1.85 | H136A/R139V | site-directed mutagenesis, reduced activity compared to the wild-type enzyme | Escherichia coli K-12 |
4.1.1.85 | H136N | site-directed mutagenesis, reduced activity compared to the wild-type enzyme | Escherichia coli K-12 |
4.1.1.85 | H136Q | site-directed mutagenesis, reduced activity compared to the wild-type enzyme | Escherichia coli K-12 |
4.1.1.85 | K64A | site-directed mutagenesis, reduced activity compared to the wild-type enzyme | Escherichia coli K-12 |
4.1.1.85 | K64A/E112A/H136A/R139V | site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme | Escherichia coli K-12 |
4.1.1.85 | K64A/E112Q/H136A | site-directed mutagenesis, reduced activity compared to the wild-type enzyme | Escherichia coli K-12 |
4.1.1.85 | K64A/H136A | site-directed mutagenesis, reduced activity compared to the wild-type enzyme | Escherichia coli K-12 |
4.1.1.85 | K64A/R139V | site-directed mutagenesis, reduced activity compared to the wild-type enzyme | Escherichia coli K-12 |
4.1.1.85 | K64R | site-directed mutagenesis, slightly reduced activity compared to the wild-type enzyme | Escherichia coli K-12 |
4.1.1.85 | K64R/H136A | site-directed mutagenesis, reduced activity compared to the wild-type enzyme | Escherichia coli K-12 |
4.1.1.85 | R139V | site-directed mutagenesis, slightly reduced activity compared to the wild-type enzyme | Escherichia coli K-12 |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
4.1.1.85 | additional information | - |
additional information | analysis of kinetics and activity of the mutant enzymes, overview | Escherichia coli K-12 | |
4.1.1.85 | 0.15 | - |
3-dehydro-L-gulonate 6-phosphate | pH 7.5, 25°C, recombinant mutant E112Q/H136A | Escherichia coli K-12 | |
4.1.1.85 | 0.22 | - |
3-dehydro-L-gulonate 6-phosphate | pH 7.5, 25°C, recombinant mutant E112Q/H136A/R139V | Escherichia coli K-12 | |
4.1.1.85 | 0.27 | - |
3-dehydro-L-gulonate 6-phosphate | pH 7.5, 25°C, recombinant mutant D67A/H136A | Escherichia coli K-12 | |
4.1.1.85 | 0.3 | - |
3-dehydro-L-gulonate 6-phosphate | pH 7.5, 25°C, recombinant mutants K64R and D67N/H136A | Escherichia coli K-12 | |
4.1.1.85 | 0.31 | - |
3-dehydro-L-gulonate 6-phosphate | pH 7.5, 25°C, recombinant mutant E112Q | Escherichia coli K-12 | |
4.1.1.85 | 0.34 | - |
3-dehydro-L-gulonate 6-phosphate | pH 7.5, 25°C, recombinant mutant E112A | Escherichia coli K-12 | |
4.1.1.85 | 0.36 | - |
3-dehydro-L-gulonate 6-phosphate | pH 7.5, 25°C, recombinant mutant R139V | Escherichia coli K-12 | |
4.1.1.85 | 0.37 | - |
3-dehydro-L-gulonate 6-phosphate | pH 7.5, 25°C, recombinant mutant H136N | Escherichia coli K-12 | |
4.1.1.85 | 0.41 | - |
3-dehydro-L-gulonate 6-phosphate | pH 7.5, 25°C, recombinant mutant D67N | Escherichia coli K-12 | |
4.1.1.85 | 0.44 | - |
3-dehydro-L-gulonate 6-phosphate | pH 7.5, 25°C, recombinant mutant K64R/H136A | Escherichia coli K-12 | |
4.1.1.85 | 0.5 | - |
3-dehydro-L-gulonate 6-phosphate | pH 7.5, 25°C, recombinant mutant D67A | Escherichia coli K-12 | |
4.1.1.85 | 0.51 | - |
3-dehydro-L-gulonate 6-phosphate | pH 7.5, 25°C, recombinant mutant K64A | Escherichia coli K-12 | |
4.1.1.85 | 0.52 | - |
3-dehydro-L-gulonate 6-phosphate | pH 7.5, 25°C, recombinant mutant H136Q | Escherichia coli K-12 | |
4.1.1.85 | 0.55 | - |
3-dehydro-L-gulonate 6-phosphate | pH 7.5, 25°C, recombinant mutant K64A/E112Q/H136A | Escherichia coli K-12 | |
4.1.1.85 | 0.58 | - |
3-dehydro-L-gulonate 6-phosphate | pH 7.5, 25°C, recombinant mutant K64A/H136A | Escherichia coli K-12 | |
4.1.1.85 | 0.65 | - |
3-dehydro-L-gulonate 6-phosphate | pH 7.5, 25°C, recombinant mutant E112A/H136A | Escherichia coli K-12 | |
4.1.1.85 | 0.67 | - |
3-dehydro-L-gulonate 6-phosphate | pH 7.5, 25°C, recombinant wild-type enzyme | Escherichia coli K-12 | |
4.1.1.85 | 0.7 | - |
3-dehydro-L-gulonate 6-phosphate | pH 7.5, 25°C, recombinant mutant H136A | Escherichia coli K-12 | |
4.1.1.85 | 0.77 | - |
3-dehydro-L-gulonate 6-phosphate | pH 7.5, 25°C, recombinant mutant E112A/H136A/R139V | Escherichia coli K-12 | |
4.1.1.85 | 0.9 | - |
3-dehydro-L-gulonate 6-phosphate | pH 7.5, 25°C, recombinant mutant K64A/R139V | Escherichia coli K-12 | |
4.1.1.85 | 1.4 | - |
3-dehydro-L-gulonate 6-phosphate | pH 7.5, 25°C, recombinant mutants H136A/R139V and K64A/E112A/H136A/R139V | Escherichia coli K-12 |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
4.1.1.85 | Mg2+ | dependent on | Escherichia coli K-12 |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
4.1.1.85 | 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 | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
4.1.1.85 | Escherichia coli K-12 | - |
- |
- |
EC Number | Reaction | Comment | Organism | Reaction ID |
---|---|---|---|---|
4.1.1.85 | 3-dehydro-L-gulonate 6-phosphate + H+ = L-xylulose 5-phosphate + CO2 | catalytic mechanism, formation and Mg2+-stabilization of an cis-1,2-enediolate anion intermediate, important residues for the stereospecific exchange of the pro-1S hydrogen are Lys64, Asp67, Glu112, Arg139, and Lys64, the latter stabilizes the intermediate via hydrogen bonds to O1 and O2 of the intermediate involving conserved active site residue Asp67, His136 takes part in hydrogen exchange with solvent of the 1-hydroxymethylene group of the product, overview | Escherichia coli K-12 |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
4.1.1.85 | 3-dehydro-L-gulonate 6-phosphate + H+ | stereochemistry | Escherichia coli K-12 | L-xylulose 5-phosphate + CO2 | - |
? | |
4.1.1.85 | 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 | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
4.1.1.85 | dimer | (beta/alpha)8-barrel enzyme | Escherichia coli K-12 |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
4.1.1.85 | 3-keto-L-gulonate 6-phosphate decarboxylase | - |
Escherichia coli K-12 |
4.1.1.85 | KGPDC | - |
Escherichia coli K-12 |
4.1.1.85 | More | the enzyme belongs to the orotidine 5'-monophosphate decarboxylase OMPDC suprafamily | Escherichia coli K-12 |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
4.1.1.85 | 25 | - |
assay at | Escherichia coli K-12 |
EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
4.1.1.85 | 0.19 | - |
3-dehydro-L-gulonate 6-phosphate | pH 7.5, 25°C, recombinant mutant D67A/H136A | Escherichia coli K-12 | |
4.1.1.85 | 0.2 | - |
3-dehydro-L-gulonate 6-phosphate | pH 7.5, 25°C, recombinant mutant E112Q/H136A/R139V | Escherichia coli K-12 | |
4.1.1.85 | 0.21 | - |
3-dehydro-L-gulonate 6-phosphate | pH 7.5, 25°C, recombinant mutant E112A/H136A/R139V | Escherichia coli K-12 | |
4.1.1.85 | 0.23 | - |
3-dehydro-L-gulonate 6-phosphate | pH 7.5, 25°C, recombinant mutant E112Q/H136A | Escherichia coli K-12 | |
4.1.1.85 | 0.26 | - |
3-dehydro-L-gulonate 6-phosphate | pH 7.5, 25°C, recombinant mutant K64A/E112A/H136A/R139V | Escherichia coli K-12 | |
4.1.1.85 | 0.3 | - |
3-dehydro-L-gulonate 6-phosphate | pH 7.5, 25°C, recombinant mutant E112A | Escherichia coli K-12 | |
4.1.1.85 | 0.45 | - |
3-dehydro-L-gulonate 6-phosphate | pH 7.5, 25°C, recombinant mutant E112A/H136A | Escherichia coli K-12 | |
4.1.1.85 | 0.75 | - |
3-dehydro-L-gulonate 6-phosphate | pH 7.5, 25°C, recombinant mutant K64A/H136A | Escherichia coli K-12 | |
4.1.1.85 | 1.1 | - |
3-dehydro-L-gulonate 6-phosphate | pH 7.5, 25°C, recombinant mutant D67N | Escherichia coli K-12 | |
4.1.1.85 | 1.2 | - |
3-dehydro-L-gulonate 6-phosphate | pH 7.5, 25°C, recombinant mutant K64A/R139V | Escherichia coli K-12 | |
4.1.1.85 | 1.3 | - |
3-dehydro-L-gulonate 6-phosphate | pH 7.5, 25°C, recombinant mutant D67N/H136A | Escherichia coli K-12 | |
4.1.1.85 | 1.4 | - |
3-dehydro-L-gulonate 6-phosphate | pH 7.5, 25°C, recombinant mutant H136Q | Escherichia coli K-12 | |
4.1.1.85 | 2.4 | - |
3-dehydro-L-gulonate 6-phosphate | pH 7.5, 25°C, recombinant mutants D67A and H136A | Escherichia coli K-12 | |
4.1.1.85 | 2.9 | - |
3-dehydro-L-gulonate 6-phosphate | pH 7.5, 25°C, recombinant mutant K64A/E112Q/H136A | Escherichia coli K-12 | |
4.1.1.85 | 4 | - |
3-dehydro-L-gulonate 6-phosphate | pH 7.5, 25°C, recombinant mutant E112Q | Escherichia coli K-12 | |
4.1.1.85 | 4.2 | - |
3-dehydro-L-gulonate 6-phosphate | pH 7.5, 25°C, recombinant mutant K64R/H136A | Escherichia coli K-12 | |
4.1.1.85 | 4.3 | - |
3-dehydro-L-gulonate 6-phosphate | pH 7.5, 25°C, recombinant mutant H136N | Escherichia coli K-12 | |
4.1.1.85 | 8.3 | - |
3-dehydro-L-gulonate 6-phosphate | pH 7.5, 25°C, recombinant mutant K64A | Escherichia coli K-12 | |
4.1.1.85 | 8.9 | - |
3-dehydro-L-gulonate 6-phosphate | pH 7.5, 25°C, recombinant mutant R139V | Escherichia coli K-12 | |
4.1.1.85 | 9.2 | - |
3-dehydro-L-gulonate 6-phosphate | pH 7.5, 25°C, recombinant mutant H136A/R139V | Escherichia coli K-12 | |
4.1.1.85 | 17 | - |
3-dehydro-L-gulonate 6-phosphate | pH 7.5, 25°C, recombinant mutant K64R | Escherichia coli K-12 | |
4.1.1.85 | 51 | - |
3-dehydro-L-gulonate 6-phosphate | pH 7.5, 25°C, recombinant wild-type enzyme | Escherichia coli K-12 |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
4.1.1.85 | 7.5 | - |
assay at | Escherichia coli K-12 |