TY - JOUR
T1 - Fungal laccases
AU - Rivera-Hoyos, Claudia M.
AU - Morales-Álvarez, Edwin David
AU - Poutou-Piñales, Raúl A.
AU - Pedroza-Rodríguez, Aura Marina
AU - RodrÍguez-Vázquez, Refugio
AU - Delgado-Boada, Julio M.
PY - 2013/12
Y1 - 2013/12
N2 - Laccases are enzymes widely distributed in plants, fungi, bacteria, and insects. They are multicopper oxidases that catalyze the transformation of aromatic and non-aromatic compounds with reduction of molecular oxygen to water. These enzymes participate in processes such as biosynthesis and lignin degradation, morphogenesis, and pigment biosynthesis, among others. In this review we discuss relevant aspects of fungal laccases regarding the existence of fungal laccases gene families, the growing interest in investigating mechanisms of their molecular regulation, and factors that influence the production of laccases, due to their potential biotechnological applications. In addition we comparatively analyzed some structural similarities and differences depicting general features of laccases' active site, demonstrating their frequency as monomeric proteins with highly conserved cupredoxine type domains. Although inter- and intra-specific differences have been determined, structural differences encountered between fungal laccases remain unclear based on Crystallography and X-ray diffraction.
AB - Laccases are enzymes widely distributed in plants, fungi, bacteria, and insects. They are multicopper oxidases that catalyze the transformation of aromatic and non-aromatic compounds with reduction of molecular oxygen to water. These enzymes participate in processes such as biosynthesis and lignin degradation, morphogenesis, and pigment biosynthesis, among others. In this review we discuss relevant aspects of fungal laccases regarding the existence of fungal laccases gene families, the growing interest in investigating mechanisms of their molecular regulation, and factors that influence the production of laccases, due to their potential biotechnological applications. In addition we comparatively analyzed some structural similarities and differences depicting general features of laccases' active site, demonstrating their frequency as monomeric proteins with highly conserved cupredoxine type domains. Although inter- and intra-specific differences have been determined, structural differences encountered between fungal laccases remain unclear based on Crystallography and X-ray diffraction.
KW - Biotechnological applications
KW - Cupredoxine type domains
KW - Laccases
KW - Lignin degradation
UR - http://www.scopus.com/inward/record.url?scp=84888297228&partnerID=8YFLogxK
U2 - 10.1016/j.fbr.2013.07.001
DO - 10.1016/j.fbr.2013.07.001
M3 - Review article
AN - SCOPUS:84888297228
SN - 1749-4613
VL - 27
SP - 67
EP - 82
JO - Fungal Biology Reviews
JF - Fungal Biology Reviews
IS - 3-4
ER -