ArticleThe Journal of biological chemistry2011
Expanding the nucleotide and sugar 1-phosphate promiscuity of nucleotidyltransferase RmlA via directed evolution.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 42 citations in OpenAlex.
- Dysregulation of a nucleotidyltransferase induces division and surface glycan defects inProceedings of the National Academy of Sciences of the United States of America · 2026Article
- Biochemical Applications of Microbial Rare Glycan Biosynthesis, Recognition, and Sequencing.Biochemistry · 2025Review
- Defined Glycan Ligands for Detecting Rare l-Sugar-Binding Proteins.Journal of the American Chemical Society · 2025Article
- Glycosyltransferases: glycoengineers in human milk oligosaccharide synthesis and manufacturing.Frontiers in molecular biosciences · 2025Review
- Feedback Inhibition of Bacterial Nucleotidyltransferases by Rare Nucleotide l-Sugars Restricts Substrate Promiscuity.Journal of the American Chemical Society · 2023Article
- Biocatalytic Approaches to Building Blocks for Enzymatic and Chemical Glycan Synthesis.JACS Au · 2023Review
- Expanding the Substrate Scope of a Bacterial Nucleotidyltransferase via Allosteric Mutations.ACS infectious diseases · 2022Article
- Rhamnose-Containing Compounds: Biosynthesis and Applications.Molecules (Basel, Switzerland) · 2022Review
- Genome Characterization of Pseudomonas aeruginosa KT1115, a High Di-rhamnolipid-Producing Strain with Strong Oils Metabolizing Ability.Current microbiology · 2020Article
- Improvement of ST0452Applied and environmental microbiology · 2018Article
- Structure of the Bacillus anthracis dTDP-L-rhamnose-biosynthetic enzyme glucose-1-phosphate thymidylyltransferase (RfbA).Acta crystallographica. Section F, Structural biology communications · 2017Article
- Increasing the Thermostable Sugar-1-Phosphate Nucleotidylyltransferase Activities of the Archaeal ST0452 Protein through Site Saturation Mutagenesis of the 97th Amino Acid Position.Applied and environmental microbiology · 2017Article
- Distinct Substrate Specificity and Catalytic Activity of the Pseudoglycosyltransferase VldE.Chemistry & biology · 2015Article
- Crystal Structure of the N-Acetylmuramic Acid α-1-Phosphate (MurNAc-α1-P) Uridylyltransferase MurU, a Minimal Sugar Nucleotidyltransferase and Potential Drug Target Enzyme in Gram-negative Pathogens.The Journal of biological chemistry · 2015Article
- GlmU (N-acetylglucosamine-1-phosphate uridyltransferase) bound to three magnesium ions and ATP at the active site.Acta crystallographica. Section F, Structural biology communications · 2014Article
- Facile chemoenzymatic strategies for the synthesis and utilization of S-adenosyl-(L)-methionine analogues.Angewandte Chemie (International ed. in English) · 2014Article
- Redesign of substrate specificity and identification of the aminoglycoside binding residues of Eis from Mycobacterium tuberculosis.Biochemistry · 2013Article
- The structural biology of enzymes involved in natural product glycosylation.Natural product reports · 2012Review
- Biocatalyst development by directed evolution.Bioresource technology · 2012Review
- Studies on the substrate specificity of a GDP-mannose pyrophosphorylase from Salmonella enterica.Beilstein journal of organic chemistry · 2012Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Directed evolution is a valuable technique to improve enzyme activity in the absence of a priori structural knowledge, which can be typically enhanced via structure-guided strategies. In this study, a combination of both whole-gene error-prone polymerase chain reaction and site-saturation mutagenesis enabled the rapid identification of mutations that improved RmlA activity toward non-native substrates. These mutations have been shown to improve activities over 10-fold for several targeted substrates, including non-native pyrimidine- and purine-based NTPs as well as non-native D- and L-sugars (both α- and β-isomers). This study highlights the first broadly applicable high throughput sugar-1-phosphate nucleotidyltransferase screen and the first proof of concept for the directed evolution of this enzyme class toward the identification of uniquely permissive RmlA variants.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.