Stereoselectivity and Conformational Stability of Haloalkane Dehalogenase DbjA from Bradyrhizobium japonicum USDA110: The Effect of pH and Temperature.
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14310%2F11%3A00049446" target="_blank" >RIV/00216224:14310/11:00049446 - isvavai.cz</a>
Alternative codes found
RIV/00159816:_____/11:#0000811
Result on the web
<a href="http://dx.doi.org/10.1111/j.1742-4658.2011.08203.x" target="_blank" >http://dx.doi.org/10.1111/j.1742-4658.2011.08203.x</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1111/j.1742-4658.2011.08203.x" target="_blank" >10.1111/j.1742-4658.2011.08203.x</a>
Alternative languages
Result language
angličtina
Original language name
Stereoselectivity and Conformational Stability of Haloalkane Dehalogenase DbjA from Bradyrhizobium japonicum USDA110: The Effect of pH and Temperature.
Original language description
The effect of pH and temperature on structure, stability, activity and enantioselectivity of haloalkane dehalogenase DbjA from Bradyrhizobium japonicum USDA110 was investigated in this study. Conformational changes have been assessed by circular dichroism spectroscopy, functional changes by kinetic analysis, while quaternary structure was studied by gel filtration chromatography. Our study shows that the DbjA enzyme is highly tolerant to pH changes. Its secondary and tertiary structure was not affectedby pH in the range of 5.3-10.3 and 6.2-10.1, respectively. Oligomerization of DbjA was strongly pH-dependent: monomer, dimer, tetramer and a high molecular weight cluster of the enzyme was distinguished in solution at different pH conditions. Moreover, different oligomeric states of DbjA possessed different thermal stability.
Czech name
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Czech description
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Classification
Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
CE - Biochemistry
OECD FORD branch
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Result continuities
Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>Z - Vyzkumny zamer (s odkazem do CEZ)
Others
Publication year
2011
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
FEBS Journal
ISSN
1742-464X
e-ISSN
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Volume of the periodical
278
Issue of the periodical within the volume
15
Country of publishing house
GB - UNITED KINGDOM
Number of pages
11
Pages from-to
2728-2738
UT code for WoS article
000292933300011
EID of the result in the Scopus database
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