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Literature summary for 3.5.2.6 extracted from

  • Risso, V.A.; Primo, M.E.; Ermacora, M.R.
    Re-engineering a beta-lactamase using prototype peptides from a library of local structural motifs (2009), Protein Sci., 18, 440-449.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.5.2.6

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Bacillus licheniformis

Protein Variants

Protein Variants Comment Organism
additional information replacement, separately or simultaneously, three of the ESBL alpha helices with prototype amphiphatic helices from a catalog of secondary structure elements. Although the substitutes bear no sequence similarity to the originals and pertain to unrelated protein families, all the engineered ESBL variants fold in native like structures with in vitro and in vivo enzymic activity. The triple substituted variant resembles a primitive protein, with folding defects such as a strong tendency to oligomerization and very low stability. It mimics a non homologous recombinant abandoning the family sequence space while preserving fold Bacillus licheniformis

Organism

Organism UniProt Comment Textmining
Bacillus licheniformis P00808
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-

Purification (Commentary)

Purification (Comment) Organism
-
 Bacillus licheniformis

Synonyms

Synonyms Comment Organism
ESBL
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 Bacillus licheniformis
exo-small beta-lactamase
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 Bacillus licheniformis