Structure and function of Aspergillus niger laccase McoG

Marta Ferraroni, Adrie H. Westphal, Marco Borsari, Juan Antonio Tamayo-Ramos, Fabrizio Briganti, Leo H. de Graaff, Willem J. H. van Berkel
  • Biocatalysis, January 2017, De Gruyter
  • DOI: 10.1515/boca-2017-0001

What is it about?

The ascomycete Aspergillus niger produces several multicopper oxidases, but their biocatalytic properties remain largely unknown. Elucidation of the crystal structure of A. niger laccase McoG at 1.7 Å resolution revealed that the enzyme contains a histidine (His253) instead of the common aspartate or glutamate expected to be involved in catalytic proton transfer with phenolic compounds. McoG and the H253D, H253A and H253N variants have similar activities with 2,2’-azino-bis(3- ethylbenzothiazoline-6-sulphonic acid or N,N-dimethyl-p-phenylenediamine sulphate. However, the activities of H253A and H253N with 2-amino-4-methylphenol and 2-amino-4-methoxyphenol are strongly reduced compared to that of wild type.

Why is it important?

Our results suggest that the His253 adaptation of McoG can be beneficial for the conversion of phenolic compounds.

Perspectives

Professor Willem J.H. van Berkel
Wageningen University

The work described here is a good basis for getting a better understanding of how laccases interact with phenolic substrates.

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http://dx.doi.org/10.1515/boca-2017-0001

The following have contributed to this page: Professor Willem J.H. van Berkel