ArticleProtein science : a publication of the Protein Society2022
Double mutations far from the active site affect cold activity in an Antarctic halophilic β-galactosidase.
Article in Protein science : a publication of the Protein Society, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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2 citing papers in PubMed, 4 citations in OpenAlex.
- Effects of Salinity and Temperature on the Flexibility and Function of a Polyextremophilic Enzyme.International journal of molecular sciences · 2022Article
- Double mutations far from the active site affect cold activity in an Antarctic halophilic β-galactosidase.Protein science : a publication of the Protein Society · 2022Article
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Abstract
The Antarctic haloarchaeon, Halorubrum lacusprofundi, contains a polyextremophilic family 42 β-galactosidase, which we are using as a model for cold-active enzymes. Divergent amino acid residues in this 78 kDa protein were identified through comparative genomics and hypothesized to be important for cold activity. Six amino acid residues were previously mutated and five were shown by steady-state kinetic analysis to have altered temperature-dependent catalytic activity profiles via effects on K
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