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Literature summary extracted from

  • Schneider, T.; Senn, M.M.; Berger-Bachi, B.; Tossi, A.; Sahl, H.G.; Wiedemann, I.
    In vitro assembly of a complete, pentaglycine interpeptide bridge containing cell wall precursor (lipid II-Gly5) of Staphylococcus aureus (2004), Mol. Microbiol., 53, 675-685.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.3.2.16 expression as His-tagged protein in Escherichia coli Staphylococcus aureus
2.3.2.17 expression as His-tagged protein in Escherichia coli Staphylococcus aureus
2.3.2.18 expression as His-tagged protein in Escherichia coli Staphylococcus aureus

Organism

EC Number Organism UniProt Comment Textmining
2.3.2.16 Staphylococcus aureus
-
-
-
2.3.2.17 Staphylococcus aureus
-
-
-
2.3.2.18 Staphylococcus aureus
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.2.16 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
-
 ?
2.3.2.17 N-acetylmuramoyl-L-alanyl-D-isoglutaminyl-L-lysyl-(N6-glycyl)-D-alanyl-D-alanine-diphosphoundecaprenyl-N-acetylglucosamine + 2 glycyl-tRNA i.e. lipid II-Gly. Enzyme is specific for lipid II-Gly as acceptor Staphylococcus aureus N-acetylmuramoyl-L-alanyl-D-isoglutaminyl-L-lysyl-(N6-triglycyl)-D-alanyl-D-alanine-diphosphoundecaprenyl-N-acetylglucosamine + 2 tRNA
-
 ?
2.3.2.18 N-acetylmuramoyl-L-alanyl-D-isoglutaminyl-L-lysyl-(N6-triglycyl)-D-alanyl-D-alanine-diphosphoundecaprenyl-N-acetylglucosamine + 2 glycyl-tRNA i.e. lipid II-Gly3. Enzyme is specific for lipid II-Gly3 as acceptor Staphylococcus aureus N-acetylmuramoyl-L-alanyl-D-isoglutaminyl-L-lysyl-(N6-pentaglycyl)-D-alanyl-D-alanine-diphosphoundecaprenyl-N-acetylglucosamine + 2 tRNA
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.3.2.16 FemX
-
 Staphylococcus aureus
2.3.2.17 FemA
-
 Staphylococcus aureus
2.3.2.18 FemB
-
 Staphylococcus aureus

General Information

EC Number General Information Comment Organism
2.3.2.16 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
2.3.2.17 physiological function FemA catalyzes the second step in the synthesis of the pentaglycine interpeptide bridge crosslinking different glycan strands in Staphylococcus aureus. FemX adds the first glycine residue to MurNAc-L-Ala-D-Glu-(N6-Gly)L-Lys-D-Ala-D-Ala-diphosphoundecaprenyl-M-acetylglucosamine, i.e. lipid II. 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
2.3.2.18 physiological function FemB catalyzes the third step in the synthesis of the pentaglycine interpeptide bridge crosslinking different glycan strands in Staphylococcus aureus. FemX adds the first glycine residue to MurNAc-L-Ala-D-Glu-(N6-Gly)L-Lys-D-Ala-D-Ala-diphosphoundecaprenyl-M-acetylglucosamine, i.e. lipid II. 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