| CHRÁST, Lukáš, K. TRATSIAK, Joan PLANAS IGLESIAS, Lukáš DANIEL, T. PRUDNIKOVA, Jan BREZOVSKÝ, David BEDNÁŘ, I.K. SMATANOVA, Radka CHALOUPKOVÁ a Jiří DAMBORSKÝ. Deciphering the Structural Basis of High Thermostability of Dehalogenase from Psychrophilic Bacterium Marinobacter sp. ELB17. Microorganisms. Basel: MDPI, 2019, roč. 7, č. 11, s. 1-20. ISSN 2076-2607. Dostupné z: https://dx.doi.org/10.3390/microorganisms7110498. |
Další formáty:
BibTeX
LaTeX
RIS
@article{1640679,
author = {Chrást, Lukáš and Tratsiak, K. and Planas Iglesias, Joan and Daniel, Lukáš and Prudnikova, T. and Brezovský, Jan and Bednář, David and Smatanova, I.K. and Chaloupková, Radka and Damborský, Jiří},
article_location = {Basel},
article_number = {11},
doi = {http://dx.doi.org/10.3390/microorganisms7110498},
keywords = {haloalkane dehalogenase; thermostability; psychrophile; access tunnel; dimer; catalytic pentad; enantiselectivity},
language = {eng},
issn = {2076-2607},
journal = {Microorganisms},
title = {Deciphering the Structural Basis of High Thermostability of Dehalogenase from Psychrophilic Bacterium Marinobacter sp. ELB17},
url = {https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6920932/},
volume = {7},
year = {2019}
}
TY - JOUR
ID - 1640679
AU - Chrást, Lukáš - Tratsiak, K. - Planas Iglesias, Joan - Daniel, Lukáš - Prudnikova, T. - Brezovský, Jan - Bednář, David - Smatanova, I.K. - Chaloupková, Radka - Damborský, Jiří
PY - 2019
TI - Deciphering the Structural Basis of High Thermostability of Dehalogenase from Psychrophilic Bacterium Marinobacter sp. ELB17
JF - Microorganisms
VL - 7
IS - 11
SP - 1-20
EP - 1-20
PB - MDPI
SN - 20762607
KW - haloalkane dehalogenase
KW - thermostability
KW - psychrophile
KW - access tunnel
KW - dimer
KW - catalytic pentad
KW - enantiselectivity
UR - https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6920932/
L2 - https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6920932/
N2 - Haloalkane dehalogenases are enzymes with a broad application potential in biocatalysis, bioremediation, biosensing and cell imaging. The new haloalkane dehalogenase DmxA originating from the psychrophilic bacterium Marinobacter sp. ELB17 surprisingly possesses the highest thermal stability (apparent melting temperature T-m,T-app = 65.9 degrees C) of all biochemically characterized wild type haloalkane dehalogenases belonging to subfamily II. The enzyme was successfully expressed and its crystal structure was solved at 1.45 angstrom resolution. DmxA structure contains several features distinct from known members of haloalkane dehalogenase family: (i) a unique composition of catalytic residues; (ii) a dimeric state mediated by a disulfide bridge; and (iii) narrow tunnels connecting the enzyme active site with the surrounding solvent. The importance of narrow tunnels in such paradoxically high stability of DmxA enzyme was confirmed by computational protein design and mutagenesis experiments.
ER -
CHRÁST, Lukáš, K. TRATSIAK, Joan PLANAS IGLESIAS, Lukáš DANIEL, T. PRUDNIKOVA, Jan BREZOVSKÝ, David BEDNÁŘ, I.K. SMATANOVA, Radka CHALOUPKOVÁ a Jiří DAMBORSKÝ. Deciphering the Structural Basis of High Thermostability of Dehalogenase from Psychrophilic Bacterium Marinobacter sp. ELB17. \textit{Microorganisms}. Basel: MDPI, 2019, roč.~7, č.~11, s.~1-20. ISSN~2076-2607. Dostupné z: https://dx.doi.org/10.3390/microorganisms7110498.
|
