دورية أكاديمية
Amphipatic molecules affect the kinetic profile of Pseudomonas putida chlorocatechol 1,2-dioxygenase.
العنوان: | Amphipatic molecules affect the kinetic profile of Pseudomonas putida chlorocatechol 1,2-dioxygenase. |
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المؤلفون: | Mesquita NC; Grupo de Biofísica Molecular Sérgio Mascarenhas, Instituto de Física de São Carlos, Universidade de São Paulo, Av. Trabalhador São-carlense 400, C.P. 369 São Carlos, SP 13560-970, Brazil., Dyszy FH, Kumagai PS, Araújo AP, Costa-Filho AJ |
المصدر: | European biophysics journal : EBJ [Eur Biophys J] 2013 Aug; Vol. 42 (8), pp. 655-60. Date of Electronic Publication: 2013 Jun 11. |
نوع المنشور: | Journal Article; Research Support, Non-U.S. Gov't |
اللغة: | English |
بيانات الدورية: | Publisher: Springer Verlag and the European Biophysical Societies Association Country of Publication: Germany NLM ID: 8409413 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1432-1017 (Electronic) Linking ISSN: 01757571 NLM ISO Abbreviation: Eur Biophys J Subsets: MEDLINE |
أسماء مطبوعة: | Publication: 1996- : Berlin : Springer Verlag and the European Biophysical Societies Association Original Publication: Berlin ; New York : Springer International, c1984- |
مواضيع طبية MeSH: | Hydrophobic and Hydrophilic Interactions*, Dioxygenases/*metabolism , Pseudomonas putida/*enzymology, Catechols/metabolism ; Dioxygenases/chemistry ; Kinetics ; Lipid Metabolism |
مستخلص: | Dioxygenases are nonheme iron enzymes that biodegrade recalcitrant compounds, such as catechol and derivatives, released into the environment by modern industry. Intradiol dioxygenases have attracted much attention due to the interest in their use for bioremediation, which has demanded efforts towards understanding their action mechanism and also how to control it. The role of unexpected amphipatic molecules, observed in crystal structures of intradiol dioxygenases, during catalysis has been poorly explored. We report results obtained with the intradiol enzyme chlorocatechol 1,2-dioxygenase (1,2-CCD) from Pseudomonas putida subjected to delipidation. The delipidated enzyme is more stable and shows more cooperative thermal denaturation. The kinetics changes from Michaelis-Menten to a cooperative scheme, indicating that conformational changes propagate between monomers in the absence of amphipatic molecules. Furthermore, these molecules inhibit catalysis, yielding lower v(max) values. To the best of our knowledge, this is the first report concerning the effects of amphipatic molecules on 1,2-CCD function. |
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المشرفين على المادة: | 0 (Catechols) EC 1.13.11.- (Dioxygenases) EC 1.13.11.- (chlorocatechol 1,2-dioxygenase) LF3AJ089DQ (catechol) |
تواريخ الأحداث: | Date Created: 20130612 Date Completed: 20140710 Latest Revision: 20211021 |
رمز التحديث: | 20231215 |
DOI: | 10.1007/s00249-013-0914-0 |
PMID: | 23754625 |
قاعدة البيانات: | MEDLINE |
تدمد: | 1432-1017 |
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DOI: | 10.1007/s00249-013-0914-0 |