ArticleScientific reports2018
Structure, computational and biochemical analysis of PcCel45A endoglucanase from Phanerochaete chrysosporium and catalytic mechanisms of GH45 subfamily C members.
Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 25 citations in OpenAlex.
- Cellulose nanocrystals formation leveraging synergy between lytic polysaccharide monooxygenase and endoglucanase.Bioprocess and biosystems engineering · 2026Article
- Uncovering Sequence and Structural Characteristics of Fungal Expansin-Related Proteins With Potential to Drive Substrate Targeting.Proteins · 2026Article
- A single-domain expansin-like protein fromProceedings of the National Academy of Sciences of the United States of America · 2026Article
- Structural and functional insights into extreme thermal stability and activity of two GH12 domains of a multidomain glycosidase from a hyperthermophilic euryarchaeon.The FEBS journal · 2025Article
- Expansins in Salt and Drought Stress Adaptation: From Genome-Wide Identification to Functional Characterisation in Crops.Plants (Basel, Switzerland) · 2025Review
- Article
- The first crystal structure of a family 45 glycoside hydrolase from a brown-rot fungus, Gloeophyllum trabeum GtCel45A.FEBS open bio · 2024Article
- Expression and characterization of a family 45 glycosyl hydrolase from Fomitopsis pinicola and comparison to Phanerochaete chrysosporium Cel45A.Enzyme and microbial technology · 2022Article
- QM/MM Simulations of Enzymatic Hydrolysis of Cellulose: Probing the Viability of an Endocyclic Mechanism for an Inverting Cellulase.Journal of chemical information and modeling · 2021Article
- A Swollenin FromFrontiers in microbiology · 2021Article
- The hydrolysis mechanism of a GH45 cellulase and its potential relation to lytic transglycosylase and expansin function.The Journal of biological chemistry · 2020Article
- Molecular simulation of PcCel45A protein expressed from Aspergillus nidulans to understand its structure, dynamics, and thermostability.Journal of molecular modeling · 2019Article
- Peptide-based functional annotation of carbohydrate-active enzymes by conserved unique peptide patterns (CUPP).Biotechnology for biofuels · 2019Article
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Authors and funding
11 authors at 4 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The glycoside hydrolase family 45 (GH45) of carbohydrate modifying enzymes is mostly comprised of β-1,4-endoglucanases. Significant diversity between the GH45 members has prompted the division of this family into three subfamilies: A, B and C, which may differ in terms of the mechanism, general architecture, substrate binding and cleavage. Here, we use a combination of X-ray crystallography, bioinformatics, enzymatic assays, molecular dynamics simulations and site-directed mutagenesis experiments to characterize the structure, substrate binding and enzymatic specificity of the GH45 subfamily C endoglucanase from Phanerochaete chrysosporium (PcCel45A). We investigated the role played by different residues in the binding of the enzyme to cellulose oligomers of different lengths and examined the structural characteristics and dynamics of PcCel45A that make subfamily C so dissimilar to other members of the GH45 family. Due to the structural similarity shared between PcCel45A and domain I of expansins, comparative analysis of their substrate binding was also carried out. Our bioinformatics sequence analyses revealed that the hydrolysis mechanisms in GH45 subfamily C is not restricted to use of the imidic asparagine as a general base in the "Newton's cradle" catalytic mechanism recently proposed for this subfamily.
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