ArticleScientific reports2018
Strategic single point mutation yields a solvent- and salt-stable transaminase from Virgibacillus sp. in soluble form.
Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers, 1 of them a synthesis that pooled it.
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Who cites it
5 citing papers in PubMed, 1 synthesis or guideline pooled it, 15 citations in OpenAlex.
- Recombinant expression of insoluble enzymes in Escherichia coli: a systematic review of experimental design and its manufacturing implications.Microbial cell factories · 2021Pooled it
- Inhibition of Pancreatic α-amylase by Resveratrol Derivatives: Biological Activity and Molecular Modelling Evidence for Cooperativity between Viniferin Enantiomers.Molecules (Basel, Switzerland) · 2019Article
- Phenomics and Genomics Reveal Adaptation ofFrontiers in microbiology · 2019Article
- Enhancing PLP-Binding Capacity of Class-III ω-Transaminase by Single Residue Substitution.Frontiers in bioengineering and biotechnology · 2019Article
- Characterization of a Putrescine Transaminase FromFrontiers in bioengineering and biotechnology · 2018Article
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Authors and funding
9 authors at 2 institutions in 2 countries.
Funding
Abstract
A new transaminase (VbTA) was identified from the genome of the halotolerant marine bacterium Virgibacillus 21D. Following heterologous expression in Escherichia coli, it was located entirely in the insoluble fraction. After a single mutation, identified via sequence homology analyses, the VbTA T16F mutant was successfully expressed in soluble form and characterised. VbTA T16F showed high stability towards polar organic solvents and salt exposure, accepting mainly hydrophobic aromatic amine and carbonyl substrates. The 2.0 Å resolution crystal structure of VbTA T16F is here reported, and together with computational calculations, revealed that this mutation is crucial for correct dimerisation and thus correct folding, leading to soluble protein expression.
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