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Literature summary extracted from

  • Yew, W.S.; Akana, J.; Wise, E.L.; Rayment, I.; Gerlt, J.A.
    Evolution of enzymatic activities in the orotidine 5'-monophosphate decarboxylase suprafamily: enhancing the promiscuous D-arabino-hex-3-ulose 6-phosphate synthase reaction catalyzed by 3-keto-L-gulonate 6-phosphate decarboxylase (2005), Biochemistry, 44, 1807-1815.
    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
4.1.1.85 expression of N-terminally His10-tagged wild-type and mutant enzymes in enzyme-deficient strain BLR(DE3) Methylomonas aminofaciens

Protein Variants

EC Number Protein Variants Comment Organism
4.1.1.85 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
4.1.1.85 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]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
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 0.91
-
 3-dehydro-L-gulonate 6-phosphate pH 7.5, 25°C, recombinant mutant E112D/R139V/T169A Escherichia coli K-12
4.1.1.85 5.4
-
 3-dehydro-L-gulonate 6-phosphate pH 7.5, 25°C, recombinant enzyme Methylomonas aminofaciens

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+ Methylomonas aminofaciens
-
 L-xylulose 5-phosphate + CO2
-
 ?
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
-
-
-
4.1.1.85 Methylomonas aminofaciens
-
-
-

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+
-
 Methylomonas aminofaciens L-xylulose 5-phosphate + CO2
-
 ?
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
-
 ?
4.1.1.85 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 ?
-
 ?
4.1.1.85 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

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

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 3-keto-L-gulonate 6-phosphate decarboxylase
-
 Methylomonas aminofaciens
4.1.1.85 KGPDC
-
 Escherichia coli K-12
4.1.1.85 KGPDC
-
 Methylomonas aminofaciens
4.1.1.85 More the enzyme belongs to the orotidine 5'-monophosphate decarboxylase OMPDC suprafamily Escherichia coli K-12
4.1.1.85 More the enzyme belongs to the orotidine 5'-monophosphate decarboxylase OMPDC suprafamily Methylomonas aminofaciens

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
4.1.1.85 25
-
 assay at Methylomonas aminofaciens

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
4.1.1.85 2.4
-
 3-dehydro-L-gulonate 6-phosphate pH 7.5, 25°C, recombinant mutant E112D/R139V/T169A Escherichia coli K-12
4.1.1.85 15
-
 3-dehydro-L-gulonate 6-phosphate pH 7.5, 25°C, recombinant enzyme Methylomonas aminofaciens
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
4.1.1.85 7.5
-
 assay at Methylomonas aminofaciens