title: Optimization of a small laccase by active-site redesign.
abstract: Small but faster: A small laccase from Streptomyces coelicolor (SLAC) has been engineered by structure-based design and site-directed mutagenesis to improve the activity on commercially relevant substrates. The variants generated showed up to 40-fold increased efficiency on 2,6-dimethoxyphenol and the ability to use mediators with considerably higher redox potentials (methylsyringate and TEMPO).
authors.affiliation: Department of Protein Diversity, Novozymes A/S, Krogshoejvej 36, 2880 Bagsvaerd, Denmark. mdto@novozymes.com
authors.forename: Miguel D
authors.initials: MD
authors.lastname: Toscano
authors.forename: Leonardo
authors.initials: L
authors.lastname: De Maria
authors.forename: Sune
authors.initials: S
authors.lastname: Lobedanz
authors.forename: Lars H
authors.initials: LH
authors.lastname: Ostergaard
mesh_terms: D001711:Biotransformation; D020134:Catalytic Domain; D042845:Laccase / Q000737:chemistry* / Q000378:metabolism*; D008958:Models, Molecular; D015202:Protein Engineering; D013379:Substrate Specificity
chemical_list: D042845:Laccase
keywords: biotransformations; enzymes; laccase; mutagenesis; protein engineering