ArticleApplied and environmental microbiology2014
Structure-based mutational studies of substrate inhibition of betaine aldehyde dehydrogenase BetB from Staphylococcus aureus.
Article in Applied and environmental microbiology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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21 citing papers in PubMed, 48 citations in OpenAlex.
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- Exploring the Potential of Phytocannabinoids Against Multidrug-Resistant Bacteria.Plants (Basel, Switzerland) · 2025Article
- Molecular insights into salt tolerance in Dunaliella tertiolecta involving two betaine aldehyde dehydrogenases.World journal of microbiology & biotechnology · 2024Article
- Acceptors and Effectors Alter Substrate Inhibition Kinetics of a Plant Glucosyltransferase NbUGT72AY1 and Its Mutants.International journal of molecular sciences · 2023Article
- Subfunctionalization of a monolignol to a phytoalexin glucosyltransferase is accompanied by substrate inhibition.Plant communications · 2023Article
- Molecular Mechanism of Chloramphenicol and Thiamphenicol Resistance Mediated by a Novel Oxidase, CmO, inApplied and environmental microbiology · 2023Article
- Antarctic aldehyde dehydrogenase from Flavobacterium PL002 as a potent catalyst for acetaldehyde determination in wine.Scientific reports · 2022Article
- Removal of lycopene substrate inhibition enables high carotenoid productivity in Yarrowia lipolytica.Nature communications · 2022Article
- An NAD-Specific 6-Hydroxy-3-Succinoyl-Semialdehyde-Pyridine Dehydrogenase from Nicotine-Degrading Agrobacterium tumefaciens Strain S33.Microbiology spectrum · 2021Article
- Substrate inhibition by the blockage of product release and its control by tunnel engineering.RSC chemical biology · 2021Article
- Insights into Aldehyde Dehydrogenase Enzymes: A Structural Perspective.Frontiers in molecular biosciences · 2021Review
- Crystal Structure of Inorganic Pyrophosphatase FromFrontiers in cell and developmental biology · 2021Article
- Enhanced succinic acid production by Mannheimia employing optimal malate dehydrogenase.Nature communications · 2020Article
- Structural and Biochemical Characterization of Aldehyde Dehydrogenase 12, the Last Enzyme of Proline Catabolism in Plants.Journal of molecular biology · 2019Article
- iTRAQ-Based Quantitative Proteomic Profiling ofFrontiers in microbiology · 2019Article
- Indole-3-acetaldehyde dehydrogenase-dependent auxin synthesis contributes to virulence of Pseudomonas syringae strain DC3000.PLoS pathogens · 2018Article
- The ClpXP protease is dispensable for degradation of unfolded proteins in Staphylococcus aureus.Scientific reports · 2017Article
- Exploring the transcriptome of Staphylococcus aureus in its natural niche.Scientific reports · 2016Article
- Article
- Structural and functional analysis of betaine aldehyde dehydrogenase from Staphylococcus aureus.Acta crystallographica. Section D, Biological crystallography · 2015Article
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Authors and funding
8 authors at 2 institutions in 3 countries.
Funding
Abstract
Inhibition of enzyme activity by high concentrations of substrate and/or cofactor is a general phenomenon demonstrated in many enzymes, including aldehyde dehydrogenases. Here we show that the uncharacterized protein BetB (SA2613) from Staphylococcus aureus is a highly specific betaine aldehyde dehydrogenase, which exhibits substrate inhibition at concentrations of betaine aldehyde as low as 0.15 mM. In contrast, the aldehyde dehydrogenase YdcW from Escherichia coli, which is also active against betaine aldehyde, shows no inhibition by this substrate. Using the crystal structures of BetB and YdcW, we performed a structure-based mutational analysis of BetB and introduced the YdcW residues into the BetB active site. From a total of 32 mutations, those in five residues located in the substrate binding pocket (Val288, Ser290, His448, Tyr450, and Trp456) greatly reduced the substrate inhibition of BetB, whereas the double mutant protein H448F/Y450L demonstrated a complete loss of substrate inhibition. Substrate inhibition was also reduced by mutations of the semiconserved Gly234 (to Ser, Thr, or Ala) located in the BetB NAD(+) binding site, suggesting some cooperativity between the cofactor and substrate binding sites. Substrate docking analysis of the BetB and YdcW active sites revealed that the wild-type BetB can bind betaine aldehyde in both productive and nonproductive conformations, whereas only the productive binding mode can be modeled in the active sites of YdcW and the BetB mutant proteins with reduced substrate inhibition. Thus, our results suggest that the molecular mechanism of substrate inhibition of BetB is associated with the nonproductive binding of betaine aldehyde.
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