ArticleThe Journal of biological chemistry2015
Active site and laminarin binding in glycoside hydrolase family 55.
Article in The Journal of biological chemistry, 2015. 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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Who cites it
21 citing papers in PubMed.
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- Secretome Analysis ofJournal of fungi (Basel, Switzerland) · 2024Article
- An objective criterion to evaluate sequence-similarity networks helps in dividing the protein family sequence space.PLoS computational biology · 2023Article
- Engineering Caldicellulosiruptor bescii with Surface Layer Homology Domain-Linked Glycoside Hydrolases Improves Plant Biomass Solubilization.Applied and environmental microbiology · 2022Article
- Marine microbial enzymes for the production of algal oligosaccharides and its bioactive potential for application as nutritional supplements.Folia microbiologica · 2022Review
- Heterologous expression and characterization of a novel glycoside hydrolase family 55 β-1,3-glucanase, AcGluA, from Archangium sp. strain AC19.Applied microbiology and biotechnology · 2021Article
- Mannose- and Mannobiose-Specific Responses of the Insect-Associated Cellulolytic BacteriumApplied and environmental microbiology · 2021Article
- Unique active-site and subsite features in the arabinogalactan-degrading GH43 exo-β-1,3-galactanase fromThe Journal of biological chemistry · 2020Article
- Reconstitution of Drosophila and human chromatins by wheat germ cell-free co-expression system.BMC biotechnology · 2020Article
- Substrate-recognition mechanism of tomato β-galactosidase 4 using X-ray crystallography and docking simulation.Planta · 2020Article
- Structural insights into β-1,3-glucan cleavage by a glycoside hydrolase family.Nature chemical biology · 2020Article
- Function-driven single-cell genomics uncovers cellulose-degrading bacteria from the rare biosphere.The ISME journal · 2020Article
- Identification, characterization, and structural analyses of a fungal endo-β-1,2-glucanase reveal a new glycoside hydrolase family.The Journal of biological chemistry · 2019Article
- Properties of a family 56 carbohydrate-binding module and its role in the recognition and hydrolysis of β-1,3-glucan.The Journal of biological chemistry · 2017Article
- Lentinula edodes Genome Survey and Postharvest Transcriptome Analysis.Applied and environmental microbiology · 2017Article
- Biochemical and structural analyses of a bacterialThe Journal of biological chemistry · 2017Article
- Eng1 and Exg8 Are the Major β-Glucanases Secreted by the Fungal PathogenThe Journal of biological chemistry · 2017Article
- GO annotation in InterPro: why stability does not indicate accuracy in a sea of changing annotations.Database : the journal of biological databases and curation · 2016Article
- Identifying and Visualizing Macromolecular Flexibility in Structural Biology.Frontiers in molecular biosciences · 2016Review
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7 authors.
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No grant is acknowledged in the PubMed record.
Abstract
The Carbohydrate Active Enzyme (CAZy) database indicates that glycoside hydrolase family 55 (GH55) contains both endo- and exo-β-1,3-glucanases. The founding structure in the GH55 is PcLam55A from the white rot fungus Phanerochaete chrysosporium (Ishida, T., Fushinobu, S., Kawai, R., Kitaoka, M., Igarashi, K., and Samejima, M. (2009) Crystal structure of glycoside hydrolase family 55 β-1,3-glucanase from the basidiomycete Phanerochaete chrysosporium. J. Biol. Chem. 284, 10100-10109). Here, we present high resolution crystal structures of bacterial SacteLam55A from the highly cellulolytic Streptomyces sp. SirexAA-E with bound substrates and product. These structures, along with mutagenesis and kinetic studies, implicate Glu-502 as the catalytic acid (as proposed earlier for Glu-663 in PcLam55A) and a proton relay network of four residues in activating water as the nucleophile. Further, a set of conserved aromatic residues that define the active site apparently enforce an exo-glucanase reactivity as demonstrated by exhaustive hydrolysis reactions with purified laminarioligosaccharides. Two additional aromatic residues that line the substrate-binding channel show substrate-dependent conformational flexibility that may promote processive reactivity of the bound oligosaccharide in the bacterial enzymes. Gene synthesis carried out on ∼30% of the GH55 family gave 34 active enzymes (19% functional coverage of the nonredundant members of GH55). These active enzymes reacted with only laminarin from a panel of 10 different soluble and insoluble polysaccharides and displayed a broad range of specific activities and optima for pH and temperature. Application of this experimental method provides a new, systematic way to annotate glycoside hydrolase phylogenetic space for functional properties.
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