ArticleThe Journal of biological chemistry2012
Hallmarks of processivity in glycoside hydrolases from crystallographic and computational studies of the Serratia marcescens chitinases.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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37 citing papers in PubMed, 100 citations in OpenAlex.
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- Chitinous material bioconversion by three new chitinases from the yeast Mestchnikowia pulcherrima.Microbial cell factories · 2024Review
- Molecular mechanisms of processive glycoside hydrolases underline catalytic pragmatism.Biochemical Society transactions · 2023Article
- Genomic analysis and chitinase characterization ofFrontiers in microbiology · 2023Article
- Machine learning reveals sequence-function relationships in family 7 glycoside hydrolases.The Journal of biological chemistry · 2021Article
- Plasmodium chitinases: revisiting a target of transmission-blockade against malaria.Protein science : a publication of the Protein Society · 2021Review
- Strategic aromatic residues in the catalytic cleft of the xyloglucanase MtXgh74 modifying thermostability, mode of enzyme action, and viscosity reduction ability.Applied microbiology and biotechnology · 2021Article
- Computational Analysis of Thermal Adaptation in Extremophilic Chitinases: The Achilles' Heel in Protein Structure and Industrial Utilization.Molecules (Basel, Switzerland) · 2021Article
- Structural inspection and protein motions modelling of a fungal glycoside hydrolase family 18 chitinase by crystallography depicts a dynamic enzymatic mechanism.Computational and structural biotechnology journal · 2021Article
- A trimodular bacterial enzyme combining hydrolytic activity with oxidative glycosidic bond cleavage efficiently degrades chitin.The Journal of biological chemistry · 2020Article
- Enzymatic characterization and structure-function relationship of two chitinases, LmChiA and LmChiB, fromHeliyon · 2020Article
- Structural and biochemical characterization of the exopolysaccharide deacetylase Agd3 required for Aspergillus fumigatus biofilm formation.Nature communications · 2020Article
- Ega3 from the fungal pathogenThe Journal of biological chemistry · 2019Article
- Insights into the mechanism(s) of digestion of crystalline cellulose by plant class C GH9 endoglucanases.Journal of molecular modeling · 2019Article
- Molecular mechanism ofThe Journal of biological chemistry · 2019Article
- The crystal structure of the chitinase ChiA74 of Bacillus thuringiensis has a multidomain assembly.Scientific reports · 2019Article
- Structural Insight Into Chitin Degradation and Thermostability of a Novel Endochitinase From the Glycoside Hydrolase Family 18.Frontiers in microbiology · 2019Article
- Bioinformatic Exploration of Metal-Binding Proteome of Zoonotic PathogenFrontiers in genetics · 2019Article
- A novel thermostable chitinolytic machinery ofBiotechnology for biofuels · 2019Article
- Chitinase: diversity, limitations, and trends in engineering for suitable applications.Bioscience reports · 2018Review
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Authors and funding
11 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Degradation of recalcitrant polysaccharides in nature is typically accomplished by mixtures of processive and nonprocessive glycoside hydrolases (GHs), which exhibit synergistic activity wherein nonprocessive enzymes provide new sites for productive attachment of processive enzymes. GH processivity is typically attributed to active site geometry, but previous work has demonstrated that processivity can be tuned by point mutations or removal of single loops. To gain additional insights into the differences between processive and nonprocessive enzymes that give rise to their synergistic activities, this study reports the crystal structure of the catalytic domain of the GH family 18 nonprocessive endochitinase, ChiC, from Serratia marcescens. This completes the structural characterization of the co-evolved chitinolytic enzymes from this bacterium and enables structural analysis of their complementary functions. The ChiC catalytic module reveals a shallow substrate-binding cleft that lacks aromatic residues vital for processivity, a calcium-binding site not previously seen in GH18 chitinases, and, importantly, a displaced catalytic acid (Glu-141), suggesting flexibility in the catalytic center. Molecular dynamics simulations of two processive chitinases (ChiA and ChiB), the ChiC catalytic module, and an endochitinase from Lactococcus lactis show that the nonprocessive enzymes have more flexible catalytic machineries and that their bound ligands are more solvated and flexible. These three features, which relate to the more dynamic on-off ligand binding processes associated with nonprocessive action, correlate to experimentally measured differences in processivity of the S. marcescens chitinases. These newly defined hallmarks thus appear to be key dynamic metrics in determining processivity in GH enzymes complementing structural insights.
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