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Literature summary for 2.4.2.53 extracted from
- 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 (2005), J. Biol. Chem., 280, 14154-14167.
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| UDP-4-deoxy-4-formamido-beta-L-arabinopyranose + ditrans,polycis-undecaprenyl phosphate | - |
Escherichia coli | UDP + 4-deoxy-4-formamido-alpha-L-arabinopyranosyl ditrans,polycis-undecaprenyl phosphate | - |
? |  |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| ArnC | - |
Escherichia coli |
General Information
| General Information | Comment | Organism |
|---|---|---|
| physiological function | enzyme takes part in the biosynthesis of UDP-4-amino-4-deoxy-L-arabinose in polymyxin-resistant Escherichia coli. The N-formylation of UDP-4-amino-4-deoxy-L-arabinose is an obligatory step in the biosynthesis of 4-amino-4-deoxy-L-arabinose-modified lipid A in polymyxin-resistant mutants. Only the formylated sugar nucleotide is converted in vitro to an undecaprenyl phosphate-linked form by the enzyme ArnC. Because the L-Ara4N unit attached to lipid A is not derivatized with a formyl group, a deformylase must be acting later in the pathway | Escherichia coli |
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