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Literature summary for 1.1.1.305 extracted from

  • Gu, X.; Glushka, J.; Yin, Y.; Xu, Y.; Denny, T.; Smith, J.; Jiang, Y.; Bar-Peled, M.
    Identification of a bifunctional UDP-4-keto-pentose/UDP-xylose synthase in the plant pathogenic bacterium Ralstonia solanacearum strain GMI1000, a distinct member of the 4,6-dehydratase and decarboxylase family (2010), J. Biol. Chem., 285, 9030-9040.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.1.1.305

Cloned(Commentary)

Cloned (Comment) Organism
expression of His-tagged enzyme in Escherichia coli Ralstonia solanacearum

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0222
-
 UDP-glucuronic acid pH 7.6, 37°C, recombinant enzyme Ralstonia solanacearum
0.1132
-
 NAD+ pH 7.6, 37°C, recombinant enzyme Ralstonia solanacearum

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
80000 120000 gel filtration, recombinant enzyme Ralstonia solanacearum

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Ralstonia solanacearum one activity is to decarboxylate UDP-glucuronic acid to UDP-beta-L-threo-pentopyranosyl-4-ulose in the presence of NAD+. The second activity converts UDP-beta-L-threo-pentopyranosyl-4-ulose and NADH to UDP-xylose and NAD+, albeit at a lower rate. Following decarboxylation, there is stereospecific protonation at the C5pro-R position ?
-
 ?
UDP-alpha-D-glucuronate + NAD+ Ralstonia solanacearum
-
 UDP-beta-L-threo-pentapyranos-4-ulose + CO2 + NADH + H+
-
 ?

Organism

Organism UniProt Comment Textmining
Ralstonia solanacearum
-
 gene RsU4kpxs
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged enzyme from Escherichia coli by nicke affinity chromatography and gel filtration Ralstonia solanacearum

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information one activity is to decarboxylate UDP-glucuronic acid to UDP-beta-L-threo-pentopyranosyl-4-ulose in the presence of NAD+. The second activity converts UDP-beta-L-threo-pentopyranosyl-4-ulose and NADH to UDP-xylose and NAD+, albeit at a lower rate. Following decarboxylation, there is stereospecific protonation at the C5pro-R position Ralstonia solanacearum ?
-
 ?
UDP-alpha-D-glucuronate + NAD+
-
 Ralstonia solanacearum UDP-beta-L-threo-pentapyranos-4-ulose + CO2 + NADH + H+
-
 ?

Synonyms

Synonyms Comment Organism
RsU4kpxs
-
 Ralstonia solanacearum

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
-
 Ralstonia solanacearum

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
-
 60 activity range, profile overview Ralstonia solanacearum

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.285
-
 UDP-glucuronic acid pH 7.6, 37°C, recombinant enzyme Ralstonia solanacearum
0.32
-
 NAD+ pH 7.6, 37°C, recombinant enzyme Ralstonia solanacearum

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
9
-
-
 Ralstonia solanacearum

pH Range

pH Minimum pH Maximum Comment Organism
3.5 11 activity range, profile overview Ralstonia solanacearum

Cofactor

Cofactor Comment Organism Structure
NAD+
-
 Ralstonia solanacearum

General Information

General Information Comment Organism
evolution the ancestral enzyme of UDP-xylose synthase and UDP-apiose/UDP-xylose synthase is diverged to two distinct enzymatic activities in early bacteria. This separation gave rise to the current UDP-xylose synthase in animal, fungus, and plant as well as to the plant Uaxs and bacterial ArnA and U4kpxs homologues Ralstonia solanacearum

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
2.8
-
 NAD+ pH 7.6, 37°C, recombinant enzyme Ralstonia solanacearum
12.8
-
 UDP-glucuronic acid pH 7.6, 37°C, recombinant enzyme Ralstonia solanacearum