ArticleExtremophiles : life under extreme conditions2018
Biochemical and structural characterization of a novel cold-active esterase-like protein from the psychrophilic yeast Glaciozyma antarctica.
Article in Extremophiles : life under extreme conditions, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 28 citations in OpenAlex.
- Article
- Yeasts associated with microalgal cultures in marine environments: ecological roles and biotechnological potential.FEMS yeast research · 2026Review
- Structural and functional annotation of Glaciozyma antarctica hypothetical proteins using integrated modeling pipelines.Extremophiles : life under extreme conditions · 2025Article
- Expression and characterization of Est2: a novel cold-adapted esterase from Antarctic bacterium defining the new esterase family XXII.Frontiers in microbiology · 2025Article
- The Unusual Dominance of the Yeast GenusJournal of fungi (Basel, Switzerland) · 2023Article
- Cold-Active Lipases and Esterases: A Review on Recombinant Overexpression and Other Essential Issues.International journal of molecular sciences · 2022Review
- Yeasts Inhabiting Extreme Environments and Their Biotechnological Applications.Microorganisms · 2022Review
- Identification and Biochemical Characterization of a Novel Hormone-Sensitive Lipase Family Esterase Est19 from the Antarctic BacteriumBiomolecules · 2021Article
- Cold Adaptation Strategies and the Potential of Psychrophilic Enzymes from the Antarctic Yeast,Journal of fungi (Basel, Switzerland) · 2021Review
- Increased mRNA Stability and Expression Level ofJournal of microbiology and biotechnology · 2021Article
- Diversity, Ecological Role and Biotechnological Potential of Antarctic Marine Fungi.Journal of fungi (Basel, Switzerland) · 2021Review
- Article
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Authors and funding
6 authors at 4 institutions in 1 country.
Funding
Abstract
Dienelactone hydrolase, an α/β hydrolase enzyme, catalyzes the hydrolysis of dienelactone to maleylacetate, an intermediate for the Krebs cycle. Genome sequencing of the psychrophilic yeast, Glaciozyma antarctica predicted a putative open reading frame (ORF) for dienelactone hydrolase (GaDlh) with 52% sequence similarity to that from Coniophora puteana. Phylogenetic tree analysis showed that GaDlh is closely related to other reported dienelactone hydrolases, and distantly related to other α/β hydrolases. Structural prediction using MODELLER 9.14 showed that GaDlh has the same α/β hydrolase fold as other dienelactone hydrolases and esterase/lipase enzymes, with a catalytic triad consisting of Cys-His-Asp and a G-x-C-x-G-G motif. Based on the predicted structure, GaDlh exhibits several characteristics of cold-adapted proteins such as glycine clustering in the binding pocket, reduced protein core hydrophobicity, and the absence of proline residues in loops. The putative ORF was amplified, cloned, and overexpressed in an Escherichia coli expression system. The recombinant protein was overexpressed as soluble proteins and was purified via Ni-NTA affinity chromatography. Biochemical characterization of GaDlh revealed that it has an optimal temperature at 10 °C and that it retained almost 90% of its residual activity when incubated for 90 min at 10 °C. The optimal pH was at pH 8.0 and it was stable between pH 5-9 when incubated for 60 min (more than 50% residual activity). Its K
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