NDLI: Modeling the 3-D Structure of a Recombinant Laccase from Trametes trogii Active at a pH Close to Neutrality

Content Provider	Springer Nature Link
Author	Colao, Maria Chiara Caporale, Carlo Silvestri, Federica Ruzzi, Maurizio Buocore, Vincenzo
Copyright Year	2009
Abstract	A cDNA encoding a novel laccase from the white-rot fungus Trametes trogii was cloned and expressed in Pichia pastoris. The recombinant protein (Lcc2) exhibited kinetic parameters for both phenolic and non phenolic substrates that were different from the previously described Lcc1, the main laccase isoform expressed by T. trogii; in addition, the pH/activity profiles for phenolic substrates of Lcc2 were shifted upward by 1–1.5 pH units towards neutrality as compared to Lcc1. Comparative modeling of the two laccases (69.2% identity) showed that the overall fold of Lcc2 is very similar to Lcc1 and other laccases. The substrate cavity of Lcc2 contains the Asp residue which is thought to mediate the laccase activity at acidic pHs, whereas two hydrophobic residues (Phe, Ile) on the cavity orifice of Lcc2 replace the two polar residues (Thr, Ser) of Lcc1. These structural differences may be responsible for the unique kinetic performances of Lcc2.
Starting Page	375
Ending Page	383
Page Count	9
File Format	PDF
ISSN	15723887
Journal	The Protein Journal
Volume Number	28
Issue Number	9-10
e-ISSN	15734943
Language	English
Publisher	Springer US
Publisher Date	2009-10-06
Publisher Place	Boston
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Laccase Trametes trogii Heterologous expression Comparative modeling Pichia pastoris Animal Anatomy / Morphology / Histology Organic Chemistry Biochemistry Bioorganic Chemistry
Content Type	Text
Resource Type	Article
Subject	Organic Chemistry Analytical Chemistry Biochemistry Bioengineering

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