Literature DB >> 7696981

Domain structure of laccase I from the lignin-degrading basidiomycete PM1 revealed by differential scanning calorimetry.

P M Coll1, P Pérez, E Villar, V L Shnyrov.   

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 heating of the sample up to 60 degrees C. The thermodynamic parameters of these three transitions satisfy a model of two-state independent unfolding, supporting a three-domain organization of the enzyme. It is shown that the catalytic site of laccase I is located in the domain with the thermally-induced transition at 76 degrees C.

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Year:  1994        PMID: 7696981

Source DB:  PubMed          Journal:  Biochem Mol Biol Int        ISSN: 1039-9712


  2 in total

1.  Isolation, Purification and Characterization of Two Laccases from Carrot (Daucus carota L.) and Their Response to Abiotic and Metal Ions Stresses.

Authors:  Jing Ma; Zhi-Sheng Xu; Feng Wang; Ai-Sheng Xiong
Journal:  Protein J       Date:  2015-12       Impact factor: 2.371

2.  Kinetic analysis and structural studies of a high-efficiency laccase from Cerrena sp. RSD1.

Authors:  Meng-Hsuan Wu; Cheng-Chung Lee; An-Shan Hsiao; Su-May Yu; Andrew H-J Wang; Tuan-Hua David Ho
Journal:  FEBS Open Bio       Date:  2018-07-03       Impact factor: 2.693

  2 in total

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