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.

Základní údaje

Originální název

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

Název česky

Re-konstrukce mycobakteriální dehalogenázy Rv2579 kumulativní mutagenezí haloalkán dehalogenázy LinB

Autoři

NAGATA, Yuji; Zbyněk PROKOP; Soňa MARVANOVÁ; Jana SÝKOROVÁ; Marta MONINCOVÁ; Masataka TSUDA a Jiří DAMBORSKÝ

Vydání

Applied and Environmental Microbiology, 2003, 1098-5336

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10600 1.6 Biological sciences

Stát vydavatele

Spojené státy

Utajení

není předmětem státního či obchodního tajemství

Odkazy

URL

Kód RIV

RIV/00216224:14310/03:00009851

Organizační jednotka

Přírodovědecká fakulta

UT WoS

000182151800061

Klíčová slova anglicky

MUTANT; EVOLUTION; MYCOBACTERIUM; DEHALOGENATION; BIODEGRADATION

Štítky

biodegradation, dehalogenation, Evolution, MUTANT, MYCOBACTERIUM

Změněno: 19. 3. 2010 11:05, prof. Mgr. Jiří Damborský, Dr.

Anotace

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.

Česky

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

Návaznosti

LN00A016, projekt VaV

Název: BIOMOLEKULÁRNÍ CENTRUM

Investor: Ministerstvo školství, mládeže a tělovýchovy ČR, Biomolekulární centrum

Citovat

NAGATA, Yuji; Zbyněk PROKOP; Soňa MARVANOVÁ; Jana SÝKOROVÁ; Marta MONINCOVÁ; Masataka TSUDA a Jiří DAMBORSKÝ. Re-construction of mycobacterial dehalogenase Rv2579 by cumulative mutagenesis of haloalkane dehalogenase LinB. Applied and Environmental Microbiology. 2003, roč. 69, č. 4, s. 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 a Jiří DAMBORSKÝ. Re-construction of mycobacterial dehalogenase Rv2579 by cumulative mutagenesis of haloalkane dehalogenase LinB. \textit{Applied and Environmental Microbiology}. 2003, roč.~69, č.~4, s.~2349-2355. ISSN~1098-5336.

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