EC Number   |
Title |
Organism |
|---|
  1.1.1.305 | A formyltransferase required for polymyxin resistance in Escherichia coli and the modification of lipid A with 4-Amino-4-deoxy-L-arabinose. Identification and function oF UDP-4-deoxy-4-formamido-L-arabinose |
Escherichia coli |
| 1.1.1.305 | Crystal structure of Escherichia coli ArnA (PmrI) decarboxylase domain. A key enzyme for lipid A modification with 4-amino-4-deoxy-L-arabinose and polymyxin resistance |
Escherichia coli |
| 1.1.1.305 | Human UDP-?-D-xylose synthase and Escherichia coli ArnA conserve a conformational shunt that controls whether xylose or 4-keto-xylose is produced |
Escherichia coli |
| 1.1.1.305 | Human UDP-?-D-xylose synthase and Escherichia coli ArnA conserve a conformational shunt that controls whether xylose or 4-keto-xylose is produced |
Homo sapiens |
| 1.1.1.305 | 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 |
Ralstonia solanacearum |
| 1.1.1.305 | Oxidative decarboxylation of UDP-glucuronic acid in extracts of polymyxin-resistant Escherichia coli. Origin of lipid a species modified with 4-amino-4-deoxy-L-arabinose |
Escherichia coli |
| 1.1.1.305 | Structure and function of both domains of ArnA, a dual function decarboxylase and a formyltransferase, involved in 4-amino-4-deoxy-L-arabinose biosynthesis |
Escherichia coli |
| 1.1.1.305 | Structure and mechanism of ArnA: conformational change implies ordered dehydrogenase mechanism in key enzyme for polymyxin resistance. |
Escherichia coli |
| 1.1.1.305 | Synthesis of flavonoid O-pentosides by Escherichia coli through engineering of nucleotide sugar pathways and glycosyltransferase |
Escherichia coli |
| 1.1.1.305 | The structure of apo ArnA features an unexpected central binding pocket and provides an explanation for enzymatic cooperativity |
Escherichia coli |
