Structure–function relationship among bacterial, fungal and plant laccases

By U. Dwivedi, Priyanka Singh, V. P. Pandey, Anoop Kumar. 2011

444 citations recorded by the source corpus.

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

The cell biology of lignification in higher plants. (2015, background): “structural conservation between bacteria, fungi and plants (Dwivedi et al., 2011).”
Lignin Biodegradation with Laccase-Mediator Systems (2014, background): “It has been shown that small halide anions can inhibit the activity of laccase due to disturbance of the internal electron transfer of the type 2 and 3 copper atoms that coordinate these anions (Dwivedi et al., 2011).”
Fungal laccases as green catalysts for dye synthesis (2012, background): “Most of the bacterial laccases occur intracellularly and do not contain a carbohydrate moiety in the enzyme molecule [35].”
Lignocellulases: a review of emerging and developing enzymes, systems, and practices (2017, background): “Laccases have four copper atoms present in their active sites which are distributed at three different copper centers, namely: Type-1 (blue copper center), Type-2 (normal copper), and Type-3 (coupled binuclear copper centers) (Dwivedi et al. 2011).”