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Literature summary for 3.5.2.6 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 PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
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

Inhibitors Comment Organism Structure
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
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

Organism UniProt Comment Textmining
Mycobacterium tuberculosis P9WKD3
-
-
Mycobacterium tuberculosis H37Rv P9WKD3
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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 ?
-
?
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

Synonyms Comment Organism
BlaC
-
Mycobacterium tuberculosis