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Literature summary extracted from

  • Bianchet, M.A.; Pan, Y.H.; Basta, L.A.B.; Saavedra, H.; Lloyd, E.P.; Kumar, P.; Mattoo, R.; Townsend, C.A.; Lamichhane, G.
    Structural insight into the inactivation of Mycobacterium tuberculosis non-classical transpeptidase LdtMt2 by biapenem and tebipenem (2017), BMC Biochem., 18, 008 .
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.3.2.B14 crystal structures of L,D-transpeptidase 2 complexed with biapenem or tebipenem. Biapenem and tebipenem bind to the outer cavity, covalently inactivate the enzyme, and subsequently degrade via an S-conjugate elimination mechanism Mycobacterium tuberculosis

Organism

EC Number Organism UniProt Comment Textmining
2.3.2.B14 Mycobacterium tuberculosis I6Y9J2
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2.3.2.B14 Mycobacterium tuberculosis H37Rv I6Y9J2
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