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Literature summary extracted from

  • Yew, W.S.; Wise, E.L.; Rayment, I.; Gerlt, J.A.
    Evolution of enzymatic activities in the orotidine 5'-monophosphate decarboxylase suprafamily: mechanistic evidence for a proton relay system in the active site of 3-keto-L-gulonate 6-phosphate decarboxylase (2004), Biochemistry, 43, 6427-6437.
    View publication on PubMed

Cloned(Commentary)

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

Protein Variants

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

KM Value [mM]

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

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
4.1.1.85 Mg2+ dependent on Escherichia coli K-12

Natural Substrates/ Products (Substrates)

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
-
?

Organism

EC Number Organism UniProt Comment Textmining
4.1.1.85 Escherichia coli K-12
-
-
-

Reaction

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

Substrates and Products (Substrate)

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
-
?

Subunits

EC Number Subunits Comment Organism
4.1.1.85 dimer (beta/alpha)8-barrel enzyme Escherichia coli K-12

Synonyms

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

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
4.1.1.85 25
-
assay at Escherichia coli K-12

Turnover Number [1/s]

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

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
4.1.1.85 7.5
-
assay at Escherichia coli K-12