Directed evolution of CotA laccase for increased substrate specificity using Bacillus subtilis spores
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چکیده
منابع مشابه
Directed evolution of CotA laccase for increased substrate specificity using Bacillus subtilis spores.
Directed evolution is an effective strategy to engineer and optimize protein properties, and microbial cell-surface display is a successful method to screen protein libraries. Protein surface display on Bacillus subtilis spores is demonstrated as a tool for screening protein libraries for the first time. Spore display offers advantages over more commonly utilized microbe cell-surface display sy...
متن کاملCotA of Bacillus subtilis is a copper-dependent laccase.
The spore coat protein CotA of Bacillus subtilis displays similarities with multicopper oxidases, including manganese oxidases and laccases. B. subtilis is able to oxidize manganese, but neither CotA nor other sporulation proteins are involved. We demonstrate that CotA is a laccase. Syringaldazine, a specific substrate of laccases, reacted with wild-type spores but not with DeltacotA spores. Co...
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Bacterial dd-peptidases are the targets of the β-lactam antibiotics. The sharp increase in bacterial resistance toward these antibiotics in recent years has stimulated the search for non-β-lactam alternatives. The substrates of dd-peptidases are elements of peptidoglycan from bacterial cell walls. Attempts to base dd-peptidase inhibitor design on peptidoglycan structure, however, have not been ...
متن کاملInsight into stability of CotA laccase from the spore coat of Bacillus subtilis.
The axial ligand of the catalytic mononuclear T1 copper site (Met(502)) of the CotA laccase was replaced by a leucine or phenylalanine residue to increase the redox potential of the enzyme. These mutations led to an increase in the redox potential by approx. 100 mV relative to the wild-type enzyme but the catalytic constant k(cat) in the mutant enzymes was severely compromised. This decrease in...
متن کاملBilirubin oxidase activity of Bacillus subtilis CotA.
The spore coat protein CotA from Bacillus subtilis was previously identified as a laccase. We have now found that CotA also shows strong bilirubin oxidase activity and markedly higher affinity for bilirubin than conventional bilirubin oxidase. This is the first characterization of bilirubin oxidase activity in a bacterial protein.
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ژورنال
عنوان ژورنال: Protein Engineering, Design and Selection
سال: 2010
ISSN: 1741-0134,1741-0126
DOI: 10.1093/protein/gzq036