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Literature summary for 1.1.3.2 extracted from

  • Unterweger, B.; Stoisser, T.; Leitgeb, S.; Birner-Gruenberger, R.; Nidetzky, B.
    Engineering of Aerococcus viridans L-lactate oxidase for site-specific PEGylation characterization and selective bioorthogonal modification of a S218C mutant (2012), Bioconjug. Chem., 23, 1406-1414 .
    View publication on PubMed

Application

Application Comment Organism
biotechnology coupling of mutant S218C in 94% yield to maleimide-activated methoxypoly(ethylene glycol) 5000. PEGylation causes about 30% small decrease in the specific activity of the S218C mutant, and it does not change the protein stability Aerococcus viridans

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Aerococcus viridans

Protein Variants

Protein Variants Comment Organism
S218C introduction of a site for chemical modification, about 50% of wild-type activity Aerococcus viridans

Organism

Organism UniProt Comment Textmining
Aerococcus viridans Q44467
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