ArticleThe Journal of biological chemistry2014
Structural insights into the low pH adaptation of a unique carboxylesterase from Ferroplasma: altering the pH optima of two carboxylesterases.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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16 citing papers in PubMed, 36 citations in OpenAlex.
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- N-terminal lid swapping contributes to the substrate specificity and activity of thermophilic lipase TrLipE.Frontiers in microbiology · 2023Article
- Metagenomic Mining for Esterases in the Microbial Community of Los Rueldos Acid Mine Drainage Formation.Frontiers in microbiology · 2022Article
- Mechanism and Structural Insights Into a Novel Esterase, E53, Isolated FromFrontiers in microbiology · 2021Article
- The acid-base-nucleophile catalytic triad in ABH-fold enzymes is coordinated by a set of structural elements.PloS one · 2020Article
- First Evidence of Acyl-Hydrolase/Lipase Activity From Human Probiotic Bacteria:Frontiers in microbiology · 2020Article
- Structural characterization of a prolyl aminodipeptidase (PepX) from Lactobacillus helveticus.Acta crystallographica. Section F, Structural biology communications · 2019Article
- Distinctive structural motifs co-ordinate the catalytic nucleophile and the residues of the oxyanion hole in the alpha/beta-hydrolase fold enzymes.Protein science : a publication of the Protein Society · 2019Article
- Article
- Two novel deep-sea sediment metagenome-derived esterases: residue 199 is the determinant of substrate specificity and preference.Microbial cell factories · 2018Article
- A family of archaea-like carboxylesterases preferentially expressed in the symbiotic phase of the mychorrizal fungus Tuber melanosporum.Scientific reports · 2017Article
- A Novel Subfamily Esterase with a Homoserine Transacetylase-like Fold but No Transferase Activity.Applied and environmental microbiology · 2017Article
- Sequence homolog-based molecular engineering for shifting the enzymatic pH optimum.Synthetic and systems biotechnology · 2016Article
- Conserved tyrosine 182 residue in hyperthermophilic esterase EstE1 plays a critical role in stabilizing the active site.Extremophiles : life under extreme conditions · 2016Article
- Interdomain hydrophobic interactions modulate the thermostability of microbial esterases from the hormone-sensitive lipase family.The Journal of biological chemistry · 2015Article
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10 authors at 3 institutions in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
To investigate the mechanism for low pH adaptation by a carboxylesterase, structural and biochemical analyses of EstFa_R (a recombinant, slightly acidophilic carboxylesterase from Ferroplasma acidiphilum) and SshEstI (an alkaliphilic carboxylesterase from Sulfolobus shibatae DSM5389) were performed. Although a previous proteomics study by another group showed that the enzyme purified from F. acidiphilum contained an iron atom, EstFa_R did not bind to iron as analyzed by inductively coupled plasma MS and isothermal titration calorimetry. The crystal structures of EstFa_R and SshEstI were determined at 1.6- and 1.5-Å resolutions, respectively. EstFa_R had a catalytic triad with an extended hydrogen bond network that was not observed in SshEstI. Quadruple mutants of both proteins were created to remove or introduce the extended hydrogen bond network. The mutation on EstFa_R enhanced its catalytic efficiency and gave it an alkaline pH optimum, whereas the mutation on SshEstI resulted in opposite effects (i.e. a decrease in the catalytic efficiency and a downward shift in the optimum pH). Our experimental results suggest that the low pH optimum of EstFa_R activity was a result of the unique extended hydrogen bond network in the catalytic triad and the highly negatively charged surface around the active site. The change in the pH optimum of EstFa_R happened simultaneously with a change in the catalytic efficiency, suggesting that the local flexibility of the active site in EstFa_R could be modified by quadruple mutation. These observations may provide a novel strategy to elucidate the low pH adaptation of serine hydrolases.
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