Crystallization behaviour of glyceraldehyde dehydrogenase from Thermoplasma acidophilum. Issue 12 (1st December 2015)

• Record Type: Journal Article
• Authors: Iermak, Iuliia; Degtjarik, Oksana; Steffler, Fabian; Sieber, Volker; Kuta Smatanova, Ivana
• Is Part Of: Acta crystallographica. Volume 71:Issue 12(2015:Dec.)
• Page Start: 1475
• Page End: 1480
• Publication Date: 2015-12-01
• Subjects: glyceraldehyde dehydrogenase -- cell‐free enzyme cascade -- bioproduction -- Thermoplasma acidophilum -- TaAlDH; Crystallography -- Periodicals; Crystals -- Periodicals; 548
• DOI: 10.1107/S2053230X15020270
• Languages: English
• ISSNs: 2053-230X

Abstract

Abstract : The glyceraldehyde dehydrogenase from Thermoplasma acidophilum ( Ta AlDH) 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 Ta AlDH 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 Ta AlDH ( Ta AlDHwt) and an F34M+S405N variant ( Ta AlDH F34M+S405N), were successfully crystallized. Crystals of Ta AlDHwt belonged to the monoclinic space group P 121 1 with eight molecules per asymmetric unit and diffracted to a resolution of 1.95 Å. Ta AlDH F34M+S405N crystallized in two different space groups: triclinic P 1 with 16 molecules per asymmetric unit and monoclinic C 121 with four molecules per asymmetric unit. These crystals diffracted to resolutions of 2.14 and 2.10 Å for the P 1 and C 121 crystals, respectively.