Re-construction of mycobacterial dehalogenase Rv2579 by
cumulative mutagenesis of haloalkane dehalogenase LinB

J 2003

Re-construction of mycobacterial dehalogenase Rv2579 by cumulative mutagenesis of haloalkane dehalogenase LinB

NAGATA, Yuji, Zbyněk PROKOP, Soňa MARVANOVÁ, Jana SÝKOROVÁ, Marta MONINCOVÁ et. al.

Basic information

Original name

Re-construction of mycobacterial dehalogenase Rv2579 by cumulative mutagenesis of haloalkane dehalogenase LinB

Name in Czech

Re-konstrukce mycobakteriální dehalogenázy Rv2579 kumulativní mutagenezí haloalkán dehalogenázy LinB

Authors

NAGATA, Yuji (392 Japan), Zbyněk PROKOP (203 Czech Republic), Soňa MARVANOVÁ (203 Czech Republic), Jana SÝKOROVÁ (203 Czech Republic), Marta MONINCOVÁ (203 Czech Republic), Masataka TSUDA (392 Japan) and Jiří DAMBORSKÝ (203 Czech Republic, guarantor)

Edition

Applied and Environmental Microbiology, 2003, 1098-5336

Other information

Language

English

Type of outcome

Článek v odborném periodiku

Field of Study

10600 1.6 Biological sciences

Country of publisher

United States of America

Confidentiality degree

není předmětem státního či obchodního tajemství

References:

URL

Impact factor

Impact factor: 3.820

RIV identification code

RIV/00216224:14310/03:00009851

Organization unit

Faculty of Science

UT WoS

000182151800061

Keywords in English

MUTANT; EVOLUTION; MYCOBACTERIUM; DEHALOGENATION; BIODEGRADATION

Abstract

ORIG CZ

V originále

The homology model of protein Rv2579 from Mycobacterium tuberculosis H37Rv was compared with the crystal structure of haloalkane dehalogenase LinB from Sphingomonas paucimobilis UT26 and uncovered that six out of nineteen amino acid residues which form an active site and entrance tunnel are different between LinB and Rv2579. To characterize an effect of replacements of these six amino acid residues, mutations were introduced cumulatively into the six amino acid residues of LinB. The six-fold mutant which is supposed to have an active site of Rv2579 showed haloalkane dehalogenase activity with tested haloalkanes, confirming that Rv2579 is a member of haloalkane dehalogenase protein family.

In Czech

Model proteinu Rv2579 z bakterie Mycobacretium tuberculosis byl srovnán s krystalovou strukturou haloalkán dehalogenázy LinB z bakterie Sphingomonas paucimobilis.

Links

LN00A016, research and development project

Name: BIOMOLEKULÁRNÍ CENTRUM

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

Citovat

NAGATA, Yuji, Zbyněk PROKOP, Soňa MARVANOVÁ, Jana SÝKOROVÁ, Marta MONINCOVÁ, Masataka TSUDA and Jiří DAMBORSKÝ. Re-construction of mycobacterial dehalogenase Rv2579 by cumulative mutagenesis of haloalkane dehalogenase LinB. Applied and Environmental Microbiology. 2003, vol. 69, No 4, p. 2349-2355. ISSN 1098-5336.

@article{485836,
   author = {Nagata, Yuji and Prokop, Zbyněk and Marvanová, Soňa and Sýkorová, Jana and Monincová, Marta and Tsuda, Masataka and Damborský, Jiří},
   article_number = {4},
   keywords = {MUTANT; EVOLUTION; MYCOBACTERIUM; DEHALOGENATION; BIODEGRADATION},
   language = {eng},
   issn = {1098-5336},
   journal = {Applied and Environmental Microbiology},
   title = {Re-construction of mycobacterial dehalogenase Rv2579 by cumulative mutagenesis of haloalkane dehalogenase LinB},
   url = {http://ncbr.chemi.muni.cz/~jiri/ABSTRACTS/aem03a.html},
   volume = {69},
   year = {2003}
}

TY  - JOUR
ID  - 485836
AU  - Nagata, Yuji - Prokop, Zbyněk - Marvanová, Soňa - Sýkorová, Jana - Monincová, Marta - Tsuda, Masataka - Damborský, Jiří
PY  - 2003
TI  - Re-construction of mycobacterial dehalogenase Rv2579 by cumulative mutagenesis of haloalkane dehalogenase LinB
JF  - Applied and Environmental Microbiology
VL  - 69
IS  - 4
SP  - 2349-2355
EP  - 2349-2355
SN  - 10985336
KW  - MUTANT
KW  - EVOLUTION
KW  - MYCOBACTERIUM
KW  - DEHALOGENATION
KW  - BIODEGRADATION
UR  - http://ncbr.chemi.muni.cz/~jiri/ABSTRACTS/aem03a.html
N2  - The homology model of protein Rv2579 from Mycobacterium tuberculosis H37Rv was compared with the crystal structure of haloalkane dehalogenase LinB from Sphingomonas paucimobilis UT26 and uncovered that six out of nineteen amino acid residues which form an active site and entrance tunnel are different between LinB and Rv2579. To characterize an effect of replacements of these six amino acid residues, mutations were introduced cumulatively into the six amino acid residues of LinB. The six-fold mutant which is supposed to have an active site of Rv2579 showed haloalkane dehalogenase activity with tested haloalkanes, confirming that Rv2579 is a member of haloalkane dehalogenase protein family.
ER  -

NAGATA, Yuji, Zbyněk PROKOP, Soňa MARVANOVÁ, Jana SÝKOROVÁ, Marta MONINCOVÁ, Masataka TSUDA and Jiří DAMBORSKÝ. Re-construction of mycobacterial dehalogenase Rv2579 by cumulative mutagenesis of haloalkane dehalogenase LinB. \textit{Applied and Environmental Microbiology}. 2003, vol.~69, No~4, p.~2349-2355. ISSN~1098-5336.

Detailed Information on Publication Record