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Literature summary for 3.5.2.6 extracted from

  • Guntas, G.; Kanwar, M.; Ostermeier, M.
    Circular permutation in the omega-loop of TEM-1 beta-lactamase results in improved activity and altered substrate specificity (2012), PLoS ONE, 7, e35998.
    View publication on PubMedView publication on EuropePMC

Protein Variants

Protein Variants Comment Organism
additional information identification of two variants that confer elevated resistance to cefotaxime but decreased resistance to other antibiotics. These variants are circularly permuted in the omega-loop proximal to the active site. One variant is circularly permuted such that the key catalytic residue Glu166 is located at the N-terminus of the mature protein Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P62593
-
-

Synonyms

Synonyms Comment Organism
TEM-1
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Escherichia coli