Jaafar, Nardiah Rizwana and Littler, Dene and Beddoe, Travis and Rossjohn, Jamie and Md. Illias, Rosli and Mahadi, Nor Muhammad and Mackeen, Mukram Mohamed and Abdul Murad, Abdul Munir and Abu Bakar, Farah Diba (2016) Crystal structure of fuculose aldolase from the Antarctic psychrophilic yeast Glaciozyma antarctica PI12. Acta Crystallographica Section:F Structural Biology Communications, 72 (11). pp. 831-839. ISSN 2053-230X
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Official URL: http://dx.doi.org/10.1107/S2053230X16015612
Abstract
Fuculose-1-phosphate aldolase (FucA) catalyses the reversible cleavage of l-fuculose 1-phosphate to dihydroxyacetone phosphate (DHAP) and l-lactaldehyde. This enzyme from mesophiles and thermophiles has been extensively studied; however, there is no report on this enzyme from a psychrophile. In this study, the gene encoding FucA from Glaciozyma antarctica PI12 (GaFucA) was cloned and the enzyme was overexpressed in Escherichia coli, purified and crystallized. The tetrameric structure of GaFucA was determined to 1.34 Å resolution. The overall architecture of GaFucA and its catalytically essential histidine triad are highly conserved among other fuculose aldolases. Comparisons of structural features between GaFucA and its mesophilic and thermophilic homologues revealed that the enzyme has typical psychrophilic attributes, indicated by the presence of a high number of nonpolar residues at the surface and a lower number of arginine residues.
| Item Type: | Article |
|---|---|
| Subjects: | T Technology > TP Chemical technology |
| Divisions: | Chemical Engineering |
| ID Code: | 69116 |
| Deposited By: | Siti Nor Hashidah Zakaria |
| Deposited On: | 01 Nov 2017 04:58 |
| Last Modified: | 20 Nov 2017 08:52 |
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