Počet záznamů: 1
Deciphering the Structural Basis of High Thermostability of Dehalogenase from Psychrophilic Bacterium Marinobacter sp. ELB17
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SYSNO ASEP 0511267 Druh ASEP J - Článek v odborném periodiku Zařazení RIV J - Článek v odborném periodiku Poddruh J Článek ve WOS Název Deciphering the Structural Basis of High Thermostability of Dehalogenase from Psychrophilic Bacterium Marinobacter sp. ELB17 Tvůrce(i) Chrást, L. (CZ)
Tratsiak, Katsiaryna (UOCHB-X)
Planas-Iglesias, J. (CZ)
Daniel, L. (CZ)
Prudnikova, T. (CZ)
Brezovský, J. (CZ)
Bednář, D. (CZ)
Kutá Smatanová, I. (CZ)
Chaloupková, R. (CZ)
Damborský, J. (CZ)Číslo článku 498 Zdroj.dok. Microorganisms. - : MDPI
Roč. 7, č. 11 (2019)Poč.str. 20 s. Jazyk dok. eng - angličtina Země vyd. CH - Švýcarsko Klíč. slova haloalkane dehalogenase ; thermostability ; psychrophile ; access tunnel ; dimer ; catalytic pentad ; enantiselectivity Vědní obor RIV CE - Biochemie Obor OECD Biochemistry and molecular biology CEP LM2015047 GA MŠMT - Ministerstvo školství, mládeže a tělovýchovy Způsob publikování Open access Institucionální podpora UOCHB-X - RVO:61388963 UT WOS 000502273600021 EID SCOPUS 85074389188 DOI 10.3390/microorganisms7110498 Anotace 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 Tm,app = 65.9 °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 Å 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. Pracoviště Ústav organické chemie a biochemie Kontakt asep@uochb.cas.cz ; Kateřina Šperková, Tel.: 232 002 584 ; Jana Procházková, Tel.: 220 183 418 Rok sběru 2020 Elektronická adresa https://www.mdpi.com/2076-2607/7/11/498
Počet záznamů: 1