Literature summary 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

Application

EC Number Application Comment Organism
1.1.1.305 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
2.1.2.13 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)

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

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.1.1.305 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
2.1.2.13 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

EC Number Protein Variants Comment Organism
1.1.1.305 E434Q mutant is inactive, suggesting that chemical rather than steric properties of this residue are crucial in the decarboxylation reaction Escherichia coli
2.1.2.13 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]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.305 1.3
-
NAD+ pH 7.5, 30°C, ArnA decarboxylase domain Escherichia coli
1.1.1.305 0.2
-
UDP-glucuronate pH 7.5, 30°C, S433A decarboxylase mutant Escherichia coli
1.1.1.305 0.4
-
UDP-glucuronate pH 7.5, 30°C, E434A decarboxylase mutant Escherichia coli
1.1.1.305 1.4
-
NAD+ pH 7.5, 30°C, S433A decarboxylase mutant Escherichia coli
1.1.1.305 0.7
-
UDP-glucuronate pH 7.5, 30°C, ArnA decarboxylase domain Escherichia coli
1.1.1.305 1.6
-
NAD+ pH 7.5, 30°C, E434A decarboxylase mutant, E434Q decarboxylase mutant Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.1.305 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+
-
?
2.1.2.13 10-formyltetrahydrofolate + UDP-4-amino-4-deoxy-beta-L-arabinopyranose 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 5,6,7,8-tetrahydrofolate + UDP-4-deoxy-4-formamido-beta-L-arabinopyranose
-
?

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.305 Escherichia coli P77398
-
-
2.1.2.13 Escherichia coli P77398
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.1.2.13 10-formyltetrahydrofolate + UDP-4-amino-4-deoxy-beta-L-arabinopyranose 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 5,6,7,8-tetrahydrofolate + UDP-4-deoxy-4-formamido-beta-L-arabinopyranose
-
?
2.1.2.13 10-formyltetrahydrofolate + UDP-4-amino-4-deoxy-beta-L-arabinopyranose 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. The active site of formyltransfer in ArnA includes the key catalytic residues Asn102, His104, and Asp140 Escherichia coli 5,6,7,8-tetrahydrofolate + UDP-4-deoxy-4-formamido-beta-L-arabinopyranose
-
?
1.1.1.305 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+
-
?
1.1.1.305 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]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.1.1.305 30
-
assay at Escherichia coli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.1.305 7.5
-
assay at Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.305 NAD+
-
Escherichia coli
2.1.2.13 NAD+
-
Escherichia coli