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 (Comment) | Organism |
---|---|
overexpression of native and selenomethionine decarboxylase and formyltransferase domains of ArnA | Escherichia coli |
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 | 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 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 | 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 | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | P77398 | - |
- |
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 Maximum [°C] | Comment | Organism |
---|---|---|---|
30 | - |
assay at | Escherichia coli |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.5 | - |
assay at | Escherichia coli |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NAD+ | - |
Escherichia coli |