Crystallization (Comment) | Organism |
---|---|
crystal structure of the ArnA decarboxylase domain | Escherichia coli |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.054 | - |
UDP-glucuronate | pH 8.0, 37°C, C-terminal domain of ArnA | Escherichia coli | |
0.086 | - |
UDP-glucuronate | pH 8.0, 37°C, full-length enzyme | Escherichia coli | |
0.57 | - |
NAD+ | pH 8.0, 37°C, C-terminal domain of ArnA | Escherichia coli | |
0.76 | - |
NAD+ | pH 8.0, 37°C, full-length enzyme | Escherichia coli |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
UDP-glucuronate + NAD+ | Escherichia coli | ArnA is a key enzyme in the lipid A modification pathway, and its deletion abolishes both the Ara4N-lipid A modification and polymyxin resistance. ArnA is a bifunctional enzyme. It can catalyze the NAD+-dependent decarboxylation of UDP-glucuronic acid to UDP-4-keto-arabinose and the N-10-formyltetrahydrofolate dependent formylation 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+ | ArnA is a key enzyme in the lipid A modification pathway, and its deletion abolishes both the Ara4N-lipid A modification and polymyxin resistance. ArnA is a bifunctional enzyme. It can catalyze the NAD+-dependent decarboxylation of UDP-glucuronic acid to UDP-4-keto-arabinose and the N-10-formyltetrahydrofolate dependent formylation of UDP-4-amino-4-deoxy-L-arabinose | Escherichia coli | UDP-beta-L-threo-pentapyranos-4-ulose + CO2 + NADH + H+ | - |
? | |
UDP-glucuronate + NAD+ | ArnA is a bifunctional enzyme. It can catalyze the NAD+-dependent decarboxylation of UDP-glucuronic acid to UDP-4-keto-arabinose and the N-10-formyltetrahydrofolate dependent formylation of UDP-4-amino-4-deoxy-L-arabinose. The NAD+-dependent decarboxylating activity is contained in the 360 amino acid C-terminal domain of ArnA. This domain is separable from the N-terminal fragment, and its activity is identical to that of the full-length enzyme. T432, Y463, K467, R619, and S433 are involved in the mechanism of NAD+-dependent oxidation of the 4''-OH of the UDP-glucuronic acid and decarboxylation of the UDP-4-keto-glucuronic acid intermediate | Escherichia coli | UDP-beta-L-threo-pentapyranos-4-ulose + CO2 + NADH + H+ | - |
? |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Escherichia coli |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8 | - |
assay at | Escherichia coli |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NAD+ | - |
Escherichia coli |