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Literature summary extracted from

  • Tremblay, L.W.; Fan, F.; Blanchard, J.S.
    Biochemical and structural characterization of Mycobacterium tuberculosis beta-lactamase with the carbapenems ertapenem and doripenem (2010), Biochemistry, 49, 3766-3773.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.5.2.6 BLaC is crystallized in the hanging drop vapor diffusion configuration over well conditions that include 0.1 M HEPES (pH 7.5) and 2 M NH4H2PO4. The final pH of the well solution is 4.1 Mycobacterium tuberculosis

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.5.2.6 doripenem the carbapenems doripenem and ertapenem are slow substrates that acylate the enzyme but are only slowly deacylated and can therefore act also as potent inhibitors of BlaC Mycobacterium tuberculosis
3.5.2.6 ertapenem the carbapenems doripenem and ertapenem are slow substrates that acylate the enzyme but are only slowly deacylated and can therefore act also as potent inhibitors of BlaC Mycobacterium tuberculosis

Organism

EC Number Organism UniProt Comment Textmining
3.5.2.6 Mycobacterium tuberculosis P9WKD3
-
-
3.5.2.6 Mycobacterium tuberculosis H37Rv P9WKD3
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.5.2.6 additional information the carbapenems doripenem and ertapenem are slow substrates that acylate the enzyme but are only slowly deacylated and can therefore act also as potent inhibitors of BlaC Mycobacterium tuberculosis ?
-
 ?
3.5.2.6 additional information the carbapenems doripenem and ertapenem are slow substrates that acylate the enzyme but are only slowly deacylated and can therefore act also as potent inhibitors of BlaC Mycobacterium tuberculosis H37Rv ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.5.2.6 BlaC
-
 Mycobacterium tuberculosis