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Literature summary for 1.1.1.305 extracted from

  • Williams, G.J.; Breazeale, S.D.; Raetz. C.R.; Naismith. J.H.
    Structure and function of both domains of ArnA, a dual function decarboxylase and a formyltransferase, involved in 4-amino-4-deoxy-L-arabinose biosynthesis (2005), J. Biol. Chem., 280, 23000-23008.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.1.1.305

Application

Application Comment Organism
medicine modification of the lipid A moiety of lipopolysaccharide by the addition of the sugar 4-amino-4-deoxy-L-arabinose is a strategy adopted by pathogenic Gram-negative bacteria to evade cationic antimicrobial peptides produced by the innate immune system. L-Ara4N biosynthesis is therefore a potential anti-infective target Escherichia coli

Cloned(Commentary)

Cloned (Comment) Organism
overexpression of native and selenomethionine decarboxylase and formyltransferase domains of ArnA Escherichia coli

Crystallization (Commentary)

Crystallization (Comment) Organism
crystallization of native and Se-Met decarboxylase protein. Good quality crystals are obtained with a precipitant solution of 3.2 M NaCl, 0.1 M Bistris, pH 5.2, using a drop containing 0.004 ml of protein and 0.004 ml of precipitant equilibrated against a reservoir of 0.1 ml of precipitant. Space group as P4(1)3(2), with cell dimensions a = b = c = 149.4 A, beta = gamma = 90° Escherichia coli

Protein Variants

Protein Variants Comment Organism
E434Q mutant is inactive, suggesting that chemical rather than steric properties of this residue are crucial in the decarboxylation reaction Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.2
-
 UDP-glucuronate pH 7.5, 30°C, S433A decarboxylase mutant Escherichia coli
0.4
-
 UDP-glucuronate pH 7.5, 30°C, E434A decarboxylase mutant Escherichia coli
0.7
-
 UDP-glucuronate pH 7.5, 30°C, ArnA decarboxylase domain Escherichia coli
1.3
-
 NAD+ pH 7.5, 30°C, ArnA decarboxylase domain Escherichia coli
1.4
-
 NAD+ pH 7.5, 30°C, S433A decarboxylase mutant Escherichia coli
1.6
-
 NAD+ pH 7.5, 30°C, E434A decarboxylase mutant, E434Q decarboxylase mutant Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
UDP-glucuronate + NAD+ Escherichia coli modification of the lipid A moiety of lipopolysaccharide by the addition of the sugar 4-amino-4-deoxy-L-arabinose is a strategy adopted by pathogenic Gram-negative bacteria to evade cationic antimicrobial peptides produced by the innate immune system. The bifunctional enzyme ArnA is required for 4-amino-4-deoxy-L-arabinose biosynthesis and catalyzes the NAD+-dependent oxidative decarboxylation of UDP-glucuronic acid to generate a UDP-4'-keto-pentose sugar and also catalyzes transfer of a formyl group from N-10-formyltetrahydrofolate to the 4'-amine of UDP-4-amino-4-deoxy-L-arabinose UDP-beta-L-threo-pentapyranos-4-ulose + CO2 + NADH + H+
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli P77398
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
UDP-glucuronate + NAD+ modification of the lipid A moiety of lipopolysaccharide by the addition of the sugar 4-amino-4-deoxy-L-arabinose is a strategy adopted by pathogenic Gram-negative bacteria to evade cationic antimicrobial peptides produced by the innate immune system. The bifunctional enzyme ArnA is required for 4-amino-4-deoxy-L-arabinose biosynthesis and catalyzes the NAD+-dependent oxidative decarboxylation of UDP-glucuronic acid to generate a UDP-4'-keto-pentose sugar and also catalyzes transfer of a formyl group from N-10-formyltetrahydrofolate to the 4'-amine of UDP-4-amino-4-deoxy-L-arabinose Escherichia coli UDP-beta-L-threo-pentapyranos-4-ulose + CO2 + NADH + H+
-
 ?
UDP-glucuronate + NAD+ modification of the lipid A moiety of lipopolysaccharide by the addition of the sugar 4-amino-4-deoxy-L-arabinose is a strategy adopted by pathogenic Gram-negative bacteria to evade cationic antimicrobial peptides produced by the innate immune system. The bifunctional enzyme ArnA is required for 4-amino-4-deoxy-L-arabinose biosynthesis and catalyzes the NAD+-dependent oxidative decarboxylation of UDP-glucuronic acid to generate a UDP-4'-keto-pentose sugar and also catalyzes transfer of a formyl group from N-10-formyltetrahydrofolate to the 4'-amine of UDP-4-amino-4-deoxy-L-arabinose. Residues Ser433 and Glu434 of the decarboxylase domain are required for the oxidative decarboxylation of UDP-glucuronate. Decarboxylase domain catalyzes both hydride abstraction (oxidation) from the C-4' position and the subsequent decarboxylation Escherichia coli UDP-beta-L-threo-pentapyranos-4-ulose + CO2 + NADH + H+
-
 ?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
 assay at Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
 assay at Escherichia coli

Cofactor

Cofactor Comment Organism Structure
NAD+
-
 Escherichia coli