A Haloalkane Dehalogenase From a Marine Microbial Consortium
Possessing Exceptionally Broad Substrate Specificity

J 2018

A Haloalkane Dehalogenase From a Marine Microbial Consortium Possessing Exceptionally Broad Substrate Specificity

BURYŠKA, Tomáš, Petra BABKOVÁ, Ondřej VÁVRA, Jiří DAMBORSKÝ, Zbyněk PROKOP et. al.

Basic information

Original name

A Haloalkane Dehalogenase From a Marine Microbial Consortium Possessing Exceptionally Broad Substrate Specificity

Authors

BURYŠKA, Tomáš (203 Czech Republic, belonging to the institution), Petra BABKOVÁ (203 Czech Republic, belonging to the institution), Ondřej VÁVRA (203 Czech Republic, belonging to the institution), Jiří DAMBORSKÝ (203 Czech Republic, guarantor, belonging to the institution) and Zbyněk PROKOP (203 Czech Republic, belonging to the institution)

Edition

APPLIED AND ENVIRONMENTAL MICROBIOLOGY, American Society for Microbiology, 2018, 0099-2240

Other information

Language

English

Type of outcome

Článek v odborném periodiku

Field of Study

20801 Environmental biotechnology

Country of publisher

United States of America

Confidentiality degree

není předmětem státního či obchodního tajemství

Impact factor

Impact factor: 4.077

RIV identification code

RIV/00216224:14310/18:00100776

Organization unit

Faculty of Science

UT WoS

000419048900005

Keywords in English

biotechnology; cosolvents; enzyme; haloalkane dehalogenase; marine; microbial; stability; substrate specificity

Abstract

V originále

The haloalkane dehalogenase enzyme DmmA was identified by marine metagenomic screening. Determination of its crystal structure revealed an unusually large active site compared to those of previously characterized haloalkane dehalogenases. Here we present a biochemical characterization of this interesting enzyme with emphasis on its structure-function relationships. DmmA exhibited an exceptionally broad substrate specificity and degraded several halogenated environmental pollutants that are resistant to other members of this enzyme family. In addition to having this unique substrate specificity, the enzyme was highly tolerant to organic cosolvents such as dimethyl sulfoxide, methanol, and acetone. Its broad substrate specificity, high overexpression yield (200 mg of protein per liter of cultivation medium; 50% of total protein), good tolerance to organic cosolvents, and a broad pH range make DmmA an attractive biocatalyst for various biotechnological applications.

Links

GA16-07965S, research and development project

Name: Řízená evoluce dynamických elementů v enzymech s využitím mikrofluidních čipů

Investor: Czech Science Foundation

LM2011028, research and development project

Name: RECETOX ? Národní infrastruktura pro výzkum toxických látek v prostředí

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

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

BURYŠKA, Tomáš, Petra BABKOVÁ, Ondřej VÁVRA, Jiří DAMBORSKÝ and Zbyněk PROKOP. A Haloalkane Dehalogenase From a Marine Microbial Consortium Possessing Exceptionally Broad Substrate Specificity. APPLIED AND ENVIRONMENTAL MICROBIOLOGY. American Society for Microbiology, 2018, vol. 84, No 2, p. 1-13. ISSN 0099-2240.

@article{1402018,
   author = {Buryška, Tomáš and Babková, Petra and Vávra, Ondřej and Damborský, Jiří and Prokop, Zbyněk},
   article_number = {2},
   keywords = {biotechnology; cosolvents; enzyme; haloalkane dehalogenase; marine; microbial; stability; substrate specificity},
   language = {eng},
   issn = {0099-2240},
   journal = {APPLIED AND ENVIRONMENTAL MICROBIOLOGY},
   title = {A Haloalkane Dehalogenase From a Marine Microbial Consortium Possessing Exceptionally Broad Substrate Specificity},
   volume = {84},
   year = {2018}
}

TY  - JOUR
ID  - 1402018
AU  - Buryška, Tomáš - Babková, Petra - Vávra, Ondřej - Damborský, Jiří - Prokop, Zbyněk
PY  - 2018
TI  - A Haloalkane Dehalogenase From a Marine Microbial Consortium Possessing Exceptionally Broad Substrate Specificity
JF  - APPLIED AND ENVIRONMENTAL MICROBIOLOGY
VL  - 84
IS  - 2
SP  - 1-13
EP  - 1-13
PB  - American Society for Microbiology
SN  - 00992240
KW  - biotechnology
KW  - cosolvents
KW  - enzyme
KW  - haloalkane dehalogenase
KW  - marine
KW  - microbial
KW  - stability
KW  - substrate specificity
N2  - The haloalkane dehalogenase enzyme DmmA was identified by marine metagenomic screening. Determination of its crystal structure revealed an unusually large active site compared to those of previously characterized haloalkane dehalogenases. Here we present a biochemical characterization of this interesting enzyme with emphasis on its structure-function relationships. DmmA exhibited an exceptionally broad substrate specificity and degraded several halogenated environmental pollutants that are resistant to other members of this enzyme family. In addition to having this unique substrate specificity, the enzyme was highly tolerant to organic cosolvents such as dimethyl sulfoxide, methanol, and acetone. Its broad substrate specificity, high overexpression yield (200 mg of protein per liter of cultivation medium; 50% of total protein), good tolerance to organic cosolvents, and a broad pH range make DmmA an attractive biocatalyst for various biotechnological applications.
ER  -

BURYŠKA, Tomáš, Petra BABKOVÁ, Ondřej VÁVRA, Jiří DAMBORSKÝ and Zbyněk PROKOP. A Haloalkane Dehalogenase From a Marine Microbial Consortium Possessing Exceptionally Broad Substrate Specificity. \textit{APPLIED AND ENVIRONMENTAL MICROBIOLOGY}. American Society for Microbiology, 2018, vol.~84, No~2, p.~1-13. ISSN~0099-2240.

Detailed Information on Publication Record