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Literature summary for 2.3.2.16 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)

Cloned (Comment) Organism
expression as His-tagged protein in Escherichia coli Staphylococcus aureus

Organism

Organism UniProt Comment Textmining
Staphylococcus aureus
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-
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Substrates and Products (Substrate)

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
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Synonyms

Synonyms Comment Organism
FemX
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Staphylococcus aureus

General Information

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