Stepwise Enhancement of Catalytic Performance of Haloalkane
Dehalogenase LinB towards Beta-Hexachlorocyclohexane.

J 2014

Stepwise Enhancement of Catalytic Performance of Haloalkane Dehalogenase LinB towards Beta-Hexachlorocyclohexane.

MORIUCHI, Ryota, Hiroki TANAKA, Yuki NIKAWADORI, Mayuko ISHITSUKA, Michihiro ITO et. al.

Basic information

Original name

Stepwise Enhancement of Catalytic Performance of Haloalkane Dehalogenase LinB towards Beta-Hexachlorocyclohexane.

Authors

MORIUCHI, Ryota (392 Japan), Hiroki TANAKA (392 Japan), Yuki NIKAWADORI (392 Japan), Mayuko ISHITSUKA (392 Japan), Michihiro ITO (392 Japan), Yoshiyuki OHTSUBO (392 Japan), Masataka TSUDA (392 Japan), Jiří DAMBORSKÝ (203 Czech Republic, guarantor, belonging to the institution), Zbyněk PROKOP (203 Czech Republic, belonging to the institution) and Yuji NAGATA (392 Japan)

Edition

Applied Microbiology and Biotechnology Express, London, Springer, 2014, 2191-0855

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

References:

Full Text

RIV identification code

RIV/00216224:14310/14:00074201

Organization unit

Faculty of Science

DOI

http://dx.doi.org/10.1186/s13568-014-0072-5

UT WoS

000358066200001

Keywords in English

beta -Hexachlorocyclohexane; Xenobiotics; Biodegradation; Haloalkane dehalogenase; Protein evolution

Abstract

V originále

Two haloalkane dehalogenases, LinBUT and LinBMI, each with 296 amino acid (aa) residues, exhibit only seven amino acid residue differences between them, but LinBMI‘s catalytic performance towards beta-hexachlorocyclohexane (beta-HCH) is considerably higher than LinBUT‘s. To elucidate the molecular basis governing this difference, intermediate mutants between LinBUT and LinBMI were constructed and kinetically characterized. The activities of LinBUT-based mutants gradually increased by cumulative mutations into LinBUT, and the effects of the individual amino acid substitutions depended on combination with other mutations. These results indicated that LinBUT‘s b-HCH degradation activity can be enhanced in a stepwise manner by the accumulation of point mutations.

Links

GAP503/12/0572, research and development project

Name: Konstrukce syntetické metabolické dráhy pro degradaci důležitého environmentálního polutantu proteinovým a metabolickým inženýrstvím

Investor: Czech Science Foundation

LO1214, research and development project

Name: Centrum pro výzkum toxických látek v prostředí (Acronym: RECETOX)

Investor: Ministry of Education, Youth and Sports of the CR

Citovat

MORIUCHI, Ryota, Hiroki TANAKA, Yuki NIKAWADORI, Mayuko ISHITSUKA, Michihiro ITO, Yoshiyuki OHTSUBO, Masataka TSUDA, Jiří DAMBORSKÝ, Zbyněk PROKOP and Yuji NAGATA. Stepwise Enhancement of Catalytic Performance of Haloalkane Dehalogenase LinB towards Beta-Hexachlorocyclohexane. Applied Microbiology and Biotechnology Express. London: Springer, 2014, vol. 4, No 72, p. 1-10. ISSN 2191-0855. Available from: https://dx.doi.org/10.1186/s13568-014-0072-5.

@article{1213423,
   author = {Moriuchi, Ryota and Tanaka, Hiroki and Nikawadori, Yuki and Ishitsuka, Mayuko and Ito, Michihiro and Ohtsubo, Yoshiyuki and Tsuda, Masataka and Damborský, Jiří and Prokop, Zbyněk and Nagata, Yuji},
   article_location = {London},
   article_number = {72},
   doi = {http://dx.doi.org/10.1186/s13568-014-0072-5},
   keywords = {beta -Hexachlorocyclohexane; Xenobiotics; Biodegradation; Haloalkane dehalogenase; Protein evolution},
   language = {eng},
   issn = {2191-0855},
   journal = {Applied Microbiology and Biotechnology Express},
   title = {Stepwise Enhancement of Catalytic Performance of Haloalkane Dehalogenase LinB towards Beta-Hexachlorocyclohexane.},
   url = {https://amb-express.springeropen.com/track/pdf/10.1186/s13568-014-0072-5},
   volume = {4},
   year = {2014}
}

TY  - JOUR
ID  - 1213423
AU  - Moriuchi, Ryota - Tanaka, Hiroki - Nikawadori, Yuki - Ishitsuka, Mayuko - Ito, Michihiro - Ohtsubo, Yoshiyuki - Tsuda, Masataka - Damborský, Jiří - Prokop, Zbyněk - Nagata, Yuji
PY  - 2014
TI  - Stepwise Enhancement of Catalytic Performance of Haloalkane Dehalogenase LinB towards Beta-Hexachlorocyclohexane.
JF  - Applied Microbiology and Biotechnology Express
VL  - 4
IS  - 72
SP  - 1-10
EP  - 1-10
PB  - Springer
SN  - 21910855
KW  - beta -Hexachlorocyclohexane
KW  - Xenobiotics
KW  - Biodegradation
KW  - Haloalkane dehalogenase
KW  - Protein evolution
UR  - https://amb-express.springeropen.com/track/pdf/10.1186/s13568-014-0072-5
L2  - https://amb-express.springeropen.com/track/pdf/10.1186/s13568-014-0072-5
N2  - Two haloalkane dehalogenases, LinBUT and LinBMI, each with 296 amino acid (aa) residues, exhibit only seven amino acid residue differences between them, but LinBMI‘s catalytic performance towards beta-hexachlorocyclohexane (beta-HCH) is considerably higher than LinBUT‘s. To elucidate the molecular basis governing this difference, intermediate mutants between LinBUT and LinBMI were constructed and kinetically characterized. The activities of LinBUT-based mutants gradually increased by cumulative mutations into LinBUT, and the effects of the individual amino acid substitutions depended on combination with other mutations. These results indicated that LinBUT‘s b-HCH degradation activity can be enhanced in a stepwise manner by the accumulation of point mutations.
ER  -

MORIUCHI, Ryota, Hiroki TANAKA, Yuki NIKAWADORI, Mayuko ISHITSUKA, Michihiro ITO, Yoshiyuki OHTSUBO, Masataka TSUDA, Jiří DAMBORSKÝ, Zbyněk PROKOP and Yuji NAGATA. Stepwise Enhancement of Catalytic Performance of Haloalkane Dehalogenase LinB towards Beta-Hexachlorocyclohexane. \textit{Applied Microbiology and Biotechnology Express}. London: Springer, 2014, vol.~4, No~72, p.~1-10. ISSN~2191-0855. Available from: https://dx.doi.org/10.1186/s13568-014-0072-5.

Detailed Information on Publication Record