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Crystallization behaviour of glyceraldehyde dehydrogenase from Thermoplasma acidophilum
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SYSNO ASEP 0452881 Druh ASEP J - Článek v odborném periodiku Zařazení RIV J - Článek v odborném periodiku Poddruh J Článek ve WOS Název Crystallization behaviour of glyceraldehyde dehydrogenase from Thermoplasma acidophilum Tvůrce(i) Lermark, L. (CZ)
Degtjarik, Oksana (UEK-B)
Steffler, F. (DE)
Sieber, V. (DE)
Kutá-Smatanová, Ivana (UEK-B) RIDZdroj.dok. Acta Crystallographica Section F-Structural Biology Communications
Roč. 71, č. 12 (2015), s. 1475-1480Poč.str. 6 s. Jazyk dok. eng - angličtina Země vyd. GB - Velká Británie Klíč. slova TaAlDH ; Thermoplasma acidophilum ; bioproduction ; cell-free enzyme cascade ; glyceraldehyde dehydrogenase Vědní obor RIV CE - Biochemie Institucionální podpora RVO:67179843 - RVO:67179843 UT WOS 000369376500006 DOI 10.1107/S2053230X15020270 Anotace The glyceraldehyde dehydrogenase from Thermoplasma acidophilum (TaAlDH) is a microbial enzyme that catalyzes the oxidation of D-glyceraldehyde to D-glycerate in the artificial enzyme cascade designed for the conversion of glucose to the organic solvents isobutanol and ethanol. Various mutants of TaAlDH were constructed by a random approach followed by site-directed and saturation mutagenesis in order to improve the properties of the enzyme that are essential for its functioning within the cascade. Two enzyme variants, wild-type TaAlDH (TaAlDHwt) and an F34M+S405N variant (TaAlDH F34M+S405N), were successfully crystallized. Crystals of TaAlDHwt belonged to the monoclinic space group P1211 with eight molecules per asymmetric unit and diffracted to a resolution of 1.95 A. TaAlDH F34M+S405N crystallized in two different space groups: triclinic P1 with 16 molecules per asymmetric unit and monoclinic C121 with four molecules per asymmetric unit. These crystals diffracted to resolutions of 2.14 and 2.10 A for the P1 and C121 crystals, respectively. Pracoviště Ústav výzkumu globální změny Kontakt Nikola Šviková, svikova.n@czechglobe.cz, Tel.: 511 192 268 Rok sběru 2016
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