ArticleProtein science : a publication of the Protein Society2018
Fused dimerization increases expression, solubility, and activity of bacterial dehydratase enzymes.
Article in Protein science : a publication of the Protein Society, 2018. 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.
- Designed protein multimerization and polymerization for functionalization of proteins.Biotechnology letters · 2022Review
- Kinetically guided, ratiometric tuning of fatty acid biosynthesis.Metabolic engineering · 2022Review
- Engineering of a Peptide α-N-Methyltransferase to Methylate Non-Proteinogenic Amino Acids.Angewandte Chemie (International ed. in English) · 2021Article
- Engineering of a Peptide α-N-Methyltransferase to Methylate Non-Proteinogenic Amino Acids.Angewandte Chemie (Weinheim an der Bergstrasse, Germany) · 2021Article
- Strategies for Making Multimeric and Polymeric Bifunctional Protein Conjugates and Their Applications as Bioanalytical Tools.Analytical sciences : the international journal of the Japan Society for Analytical Chemistry · 2021Review
- A kinetic rationale for functional redundancy in fatty acid biosynthesis.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Recent Progress in the Understanding and Engineering of Coenzyme BFrontiers in bioengineering and biotechnology · 2020Review
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Authors and funding
4 authors at 3 institutions in 1 country.
Funding
Abstract
FabA and FabZ are the two dehydratase enzymes in Escherichia coli that catalyze the dehydration of acyl intermediates in the biosynthesis of fatty acids. Both enzymes form obligate dimers in which the active site contains key amino acids from both subunits. While FabA is a soluble protein that has been relatively straightforward to express and to purify from cultured E. coli, FabZ has shown to be mostly insoluble and only partially active. In an effort to increase the solubility and activity of both dehydratases, we made constructs consisting of two identical subunits of FabA or FabZ fused with a naturally occurring peptide linker, so as to force their dimerization. The fused dimer of FabZ (FabZ-FabZ) was expressed as a soluble enzyme with an ninefold higher activity in vitro than the unfused FabZ. This construct exemplifies a strategy for the improvement of enzymes from the fatty acid biosynthesis pathways, many of which function as dimers, catalyzing critical steps for the production of fatty acids.
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