N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-(N6-triglycine)-D-alanyl-D-alanine-diphosphoundecaprenyl-N-acetylglucosamine:glycine glycyltransferase

N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-(N6-triglycine)-D-alanyl-D-alanine-diphosphoundecaprenyl-N-acetylglucosamine:glycine glycyltransferase
Identifiers
EC number 2.3.2.18
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum

N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-(N6-triglycine)-D-alanyl-D-alanine-diphosphoundecaprenyl-N-acetylglucosamine:glycine glycyltransferase (EC 2.3.2.18, femB (gene)) is an enzyme with systematic name N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-(N6-triglycine)-D-alanyl-D-alanine-ditrans,octacis-diphosphoundecaprenyl-N-acetylglucosamine:glycine glycyltransferase.[1][2][3] This enzyme catalyses the following chemical reaction

N-acetylmuramoyl-L-alanyl-D-isoglutaminyl-L-lysyl-(N6-triglycyl)-D-alanyl-D-alanine-diphospho-ditrans,octacis-undecaprenyl-N-acetylglucosamine + 2 glycyl-tRNA N-acetylmuramoyl-L-alanyl-D-isoglutaminyl-L-lysyl-(N6-pentaglycyl)-D-alanyl-D-alanine-diphospho-ditrans,octacis-undecaprenyl-N-acetylglucosamine + 2 tRNA

This Staphylococcus aureus enzyme catalyses the successive transfer of two glycine moieties from charged tRNAs to N-acetylmuramoyl-L-alanyl-D-isoglutaminyl-L-lysyl-(N6-triglycyl)-D-alanyl-D-alanine-diphosphoundecaprenyl-N-acetylglucosamine.

References

  1. Ehlert, K.; Schroder, W.; Labischinski, H. (1997). "Specificities of FemA and FemB for different glycine residues: FemB cannot substitute for FemA in staphylococcal peptidoglycan pentaglycine side chain formation". J. Bacteriol. 179: 7573–7576. PMID 9393725.
  2. Rohrer, S.; Berger-Bachi, B. (2003). "Application of a bacterial two-hybrid system for the analysis of protein-protein interactions between FemABX family proteins". Microbiology. 149: 2733–2738. doi:10.1099/mic.0.26315-0. PMID 14523106.
  3. Schneider, T.; Senn, M.M.; Berger-Bachi, B.; Tossi, A.; Sahl, H.G.; Wiedemann, I. (2004). "In vitro assembly of a complete, pentaglycine interpeptide bridge containing cell wall precursor (lipid II-Gly5) of Staphylococcus aureus". Mol. Microbiol. 53: 675–685. doi:10.1111/j.1365-2958.2004.04149.x. PMID 15228543.
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