DOMAIN-STRUCTURE OF LACCASE-I FROM THE LIGNIN-DEGRADING BASIDIOMYCETEPM1 REVEALED BY DIFFERENTIAL SCANNING CALORIMETRY

Authors
COLL PM PEREZ P VILLAR E SHNYROV VL
Citation
Pm. Coll et al., DOMAIN-STRUCTURE OF LACCASE-I FROM THE LIGNIN-DEGRADING BASIDIOMYCETEPM1 REVEALED BY DIFFERENTIAL SCANNING CALORIMETRY, Biochemistry and molecular biology international, 34(6), 1994, pp. 1091-1098
Citations number
23
Categorie Soggetti
Biology
Journal title
Biochemistry and molecular biology international → ACNP
ISSN journal
10399712
Volume
34
Issue
6
Year of publication
1994
Pages
1091 - 1098
Database
ISI
SICI code
1039-9712(1994)34:6<1091:DOLFTL>2.0.ZU;2-P
Abstract
The application of scanning calorimetry to investigate laccase I from the lignin-degrading basidomycete PM1 (CECT 2971) showed three thermal transitions beneath the overall endotherm following the previous heat ing of the sample up to 60 degrees C. The thermodynamic parameters of these three transitions satisfy a model of two-state independent unfol ding, supporting a three-domain organization of the enzyme. It is show n that the catalytic site of laccase I is located in the domain with t he thermally-induced transition at 76 degrees C.