EC 6.3.5.13 - Lipid II isoglutaminyl synthase (glutamine-hydrolysing)

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IntEnz Enzyme Nomenclature
EC 6.3.5.13

Names

Accepted name:
lipid II isoglutaminyl synthase (glutamine-hydrolysing)
Systematic name:
β-D-GlcNAc-(1→4)-Mur2Ac(oyl-L-Ala-γ-D-Glu-L-Lys-D-Ala-D-Ala)-diphospho-ditrans,octacis-undecaprenol:L-glutamine amidoligase (ADP-forming)

Reaction

Comments:

The enzyme complex, found in Gram-positive bacteria, consists of two subunits. A glutaminase subunit (cf. EC 3.5.1.2, glutaminase) produces an ammonia molecule that is channeled to a ligase subunit, which adds it to the activated D-glutamate residue of lipid II, converting it to an isoglutamine residue.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
UniProtKB/Swiss-Prot:

References

  1. Munch, D., Roemer, T., Lee, S. H., Engeser, M., Sahl, H. G., Schneider, T.
    Identification and in vitro analysis of the GatD/MurT enzyme-complex catalyzing lipid II amidation in Staphylococcus aureus.
    PLoS Pathog. 8: e1002509 (2012). [PMID: 22291598]
  2. Noldeke, E. R., Muckenfuss, L. M., Niemann, V., Muller, A., Stork, E., Zocher, G., Schneider, T., Stehle, T.
    Structural basis of cell wall peptidoglycan amidation by the GatD/MurT complex of Staphylococcus aureus.
    Sci Rep 8: 12953 (2018). [PMID: 30154570]
  3. Morlot, C., Straume, D., Peters, K., Hegnar, O. A., Simon, N., Villard, A. M., Contreras-Martel, C., Leisico, F., Breukink, E., Gravier-Pelletier, C., Le Corre, L., Vollmer, W., Pietrancosta, N., Håvarstein, L. S., Zapun, A.
    Structure of the essential peptidoglycan amidotransferase MurT/GatD complex from Streptococcus pneumoniae.
    Nat Commun 9: 3180 (2018). [PMID: 30093673]

[EC 6.3.5.13 created 2019]