J 2011

Stereoselectivity and Conformational Stability of Haloalkane Dehalogenase DbjA from Bradyrhizobium japonicum USDA110: The Effect of pH and Temperature.

CHALOUPKOVÁ, Radka, Zbyněk PROKOP, Yukari SATO, Yuji NAGATA, Jiří DAMBORSKÝ et. al.

Basic information

Original name

Stereoselectivity and Conformational Stability of Haloalkane Dehalogenase DbjA from Bradyrhizobium japonicum USDA110: The Effect of pH and Temperature.

Authors

CHALOUPKOVÁ, Radka (203 Czech Republic, belonging to the institution), Zbyněk PROKOP (203 Czech Republic, belonging to the institution), Yukari SATO (392 Japan, belonging to the institution), Yuji NAGATA (392 Japan, belonging to the institution) and Jiří DAMBORSKÝ (203 Czech Republic, guarantor, belonging to the institution)

Edition

FEBS Journal, 2011, 1742-464X

Other information

Language

English

Type of outcome

Článek v odborném periodiku

Field of Study

10600 1.6 Biological sciences

Country of publisher

United Kingdom of Great Britain and Northern Ireland

Confidentiality degree

není předmětem státního či obchodního tajemství

Impact factor

Impact factor: 3.790

RIV identification code

RIV/00216224:14310/11:00049446

Organization unit

Faculty of Science

DOI

UT WoS

000292933300011

Keywords in English

DbJA; Enantioselectivity;Haloalkane Dehalogenase

Tags

Změněno: 20/4/2012 10:36, Ing. Andrea Mikešková

Abstract

V originále

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 affected by 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.

Links

GA203/08/0114, research and development project
Name: Specifické iontové efekty pro proteiny v roztocích a podobné biologicky relevantní systémy.
Investor: Czech Science Foundation, Specific ion effects for proteins in solutions and related biologically relevant systems
IAA401630901, research and development project
Name: Evoluce substrátové specifity u enzymů aktivních s xenobiotickými látkami
Investor: Academy of Sciences of the Czech Republic, Evolution of substrate specificity in enzymes acting on xenobiotic compounds
LC06010, research and development project
Name: Centrum biokatalýzy a biotransformací
Investor: Ministry of Education, Youth and Sports of the CR, Center of Biocatalysis and Biotransformation
MSM0021622412, plan (intention)
Name: Interakce mezi chemickými látkami, prostředím a biologickými systémy a jejich důsledky na globální, regionální a lokální úrovni (INCHEMBIOL) (Acronym: INCHEMBIOL)
Investor: Ministry of Education, Youth and Sports of the CR, Interactions among the chemicals, environment and biological systems and their consequences on the global, regional and local scales (INCHEMBIOL)