ArticleActa crystallographica. Section F, Structural biology communications2016
Crystal structure of fuculose aldolase from the Antarctic psychrophilic yeast Glaciozyma antarctica PI12.
Article in Acta crystallographica. Section F, Structural biology communications, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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7 citing papers in PubMed, 14 citations in OpenAlex.
- Crystal structure of a cold-active arginase from Glaciozyma antarctica.Acta crystallographica. Section F, Structural biology communications · 2026Article
- Mechanistic and Structural Analyses of Non-Heme Iron Enzyme TqaM for α-Tertiary Amino Acid Synthesis.Journal of the American Chemical Society · 2025Article
- Molecular and evolutionary determinants for protein interaction within a class II aldolase/Adducin domain.PloS one · 2025Article
- Synthesis of Chiral Acyclic Pyrimidine Nucleoside Analogues from DHAP-Dependent Aldolases.Biomolecules · 2024Article
- Cold-Active Enzymes and Their Potential Industrial Applications-A Review.Molecules (Basel, Switzerland) · 2022Review
- Cold Adaptation Strategies and the Potential of Psychrophilic Enzymes from the Antarctic Yeast,Journal of fungi (Basel, Switzerland) · 2021Review
- Salvage of the 5-deoxyribose byproduct of radical SAM enzymes.Nature communications · 2018Article
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9 authors at 4 institutions in 4 countries.
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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.
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