ArticleExtremophiles : life under extreme conditions2013
Prospects for robust biocatalysis: engineering of novel specificity in a halophilic amino acid dehydrogenase.
Article in Extremophiles : life under extreme conditions, 2013. 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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Who cites it
7 citing papers in PubMed, 9 citations in OpenAlex.
- Exploring Oxidoreductases from Extremophiles for Biosynthesis in a Non-Aqueous System.International journal of molecular sciences · 2023Review
- Directed evolution engineering to improve activity of glucose dehydrogenase by increasing pocket hydrophobicity.Frontiers in microbiology · 2022Article
- Extremophilic Oxidoreductases for the Industry: Five Successful Examples With Promising Projections.Frontiers in bioengineering and biotechnology · 2021Review
- Structural and functional analysis ofOpen biology · 2017Article
- Engineering substrate promiscuity in halophilic alcohol dehydrogenase (HvADH2) by in silico design.PloS one · 2017Article
- Archaeal Inorganic Pyrophosphatase Displays Robust Activity under High-Salt Conditions and in Organic Solvents.Applied and environmental microbiology · 2016Article
- Rational engineering of a mesohalophilic carbonic anhydrase to an extreme halotolerant biocatalyst.Nature communications · 2015Article
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Authors and funding
2 authors at 1 institution in 1 country.
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Abstract
Heat- and solvent-tolerant enzymes from halophiles, potentially important industrially, offer a robust framework for protein engineering, but few solved halophilic structures exist to guide this. Homology modelling has guided mutations in glutamate dehydrogenase (GDH) from Halobacterium salinarum to emulate conversion of a mesophilic GDH to a methionine dehydrogenase. Replacement of K89, A163 and S367 by leucine, glycine and alanine converted halophilic GDH into a dehydrogenase accepting L-methionine, L-norleucine and L-norvaline as substrates. Over-expression in the halophilic expression host Haloferax volcanii and three-step purification gave ~98 % pure protein exhibiting maximum activity at pH 10. This enzyme also showed enhanced thermostability and organic solvent tolerance even at 70 °C, offering a biocatalyst resistant to harsh industrial environments. To our knowledge, this is the first reported amino acid specificity change engineered in a halophilic enzyme, encouraging use of mesophilic models to guide engineering of novel halophilic biocatalysts for industrial application. Calibrated gel filtration experiments show that both the mutant and the wild-type enzyme are stable hexamers.
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