Cloned (Comment) | Organism |
---|---|
expression as His-tagged protein in Escherichia coli | Staphylococcus aureus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Staphylococcus aureus | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
glycyl-tRNAGly + N-acetylmuramoyl-L-alanyl-D-isoglutaminyl-L-lysyl-D-alanyl-D-alanine-diphosphoundecaprenyl-N-acetylglucosamine | i.e. lipid II. Enzyme uses lipid II exclusively as acceptor | Staphylococcus aureus | tRNAGly + N-acetylmuramoyl-L-alanyl-D-isoglutaminyl-L-lysyl-(N6-glycyl)-D-alanyl-D-alanine-diphosphoundecaprenyl-N-acetylglucosamine | - |
? |
Synonyms | Comment | Organism |
---|---|---|
FemX | - |
Staphylococcus aureus |
General Information | Comment | Organism |
---|---|---|
physiological function | FemX catalyzes the first step in the synthesis of the pentaglycine interpeptide bridge crosslinking different glycan strands in Staphylococcus aureus. FemX uses MurNAc-L-Ala-D-Glu-L-Lys-D-Ala-D-Ala-diphosphoundecaprenyl-M-acetylglucosamine, i.e. lipid II, exclusively as acceptor for the first glycine residue. Addition of glycine residues 2, 3 and glycine residues 4, 5 is catalyzed by enzymes FemA and FemB, respectively. None of the FemABX enzymes requires the presence of one or two of the other Fem proteins for activity, rather, bridge formation is delayed in an in vitro system when all 3 enzymes are present | Staphylococcus aureus |