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Literature summary extracted from

  • Meziane-Cherif, D.; Saul, F.A.; Moubareck, C.; Weber, P.; Haouz, A.; Courvalin, P.; Perichon, B.
    Molecular basis of vancomycin dependence in VanA-type Staphylococcus aureus VRSA-9 (2010), J. Bacteriol., 192, 5465-5471.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
6.1.2.1 expression of C-terminally His6-tagged VRSA-9 Ddl Staphylococcus aureus

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
6.1.2.1 VRSA-9 Ddl X-ray diffraction crystal structure determination and analysis Staphylococcus aureus

Protein Variants

EC Number Protein Variants Comment Organism
6.1.2.1 Q260K/A283E the two amino acid substitutions result from point mutations at nucleotide positions 778 and 848, respectively. The mutant enzyme VRSA-9 synthesizes precursors ending in D-Ala-D-Lac (72%) and D-Ala-D-Ala (21%) in the absence of vancomycin. VRSA-9 Ddl shows a 200fold loss of activity and the importance of conformational changes in the dimer interface which can indirectly affect the topology of the active site Staphylococcus aureus

Inhibitors

EC Number Inhibitors Comment Organism Structure
6.1.2.1 Oxacillin VRSA-9 Ddl is less sensitive than VRSA-6 Ddl Staphylococcus aureus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
6.1.2.1 Mg2+ required Staphylococcus aureus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
6.1.2.1 41000
-
 2 * 41000, recombinant C-terminally His6-tagged, SDS-PAGE Staphylococcus aureus
6.1.2.1 82000
-
 recombinant C-terminally His6-tagged, gel filtration Staphylococcus aureus

Organism

EC Number Organism UniProt Comment Textmining
6.1.2.1 Staphylococcus aureus
-
-
-
6.1.2.1 Staphylococcus aureus VRSA-9
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.1.2.1 additional information ligand binding sites of VRSA-9 Ddl, overview Staphylococcus aureus ?
-
 ?
6.1.2.1 additional information ligand binding sites of VRSA-9 Ddl, overview Staphylococcus aureus VRSA-9 ?
-
 ?

Subunits

EC Number Subunits Comment Organism
6.1.2.1 dimer 2 * 41000, recombinant C-terminally His6-tagged, SDS-PAGE Staphylococcus aureus

Synonyms

EC Number Synonyms Comment Organism
6.1.2.1 VRSA-9 Ddl
-
 Staphylococcus aureus

Cofactor

EC Number Cofactor Comment Organism Structure
6.1.2.1 ATP
-
 Staphylococcus aureus

General Information

EC Number General Information Comment Organism
6.1.2.1 evolution the two amino acid substitutions Q260K/A283E via exchange at nucleotide positions 778 and 848, respectively, in VRSA-9 Ddl lead to the ability to synthesize precursors ending in D-Ala-D-Lac (72%) and D-Ala-D-Ala (21%) in the absence of vancomycin. The VRSA-9 Ddl has an altered D-Ala:D-Ala ligase activity relative to that of VRSA-6 with a Km for D-Ala of 2 mM at subsite 1 and 240 mM at subsite 2. The binding affinity for D-Ala at subsite 2 is 14fold lower than that of VRSA-6. The residues at nucleotide positions 778 and 848 are not conserved among D-Ala:DAla ligases and do not interact directly with the substrates. VRSA-9 Ddl shows the importance of conformational changes in the dimer interface which can indirectly affect the topology of the active site Staphylococcus aureus