ArticleJournal of bacteriology2012
Synthesis of long-chain chitooligosaccharides by a hypertransglycosylating processive endochitinase of Serratia proteamaculans 568.
Article in Journal of bacteriology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 69 citations in OpenAlex.
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- Chitinous material bioconversion by three new chitinases from the yeast Mestchnikowia pulcherrima.Microbial cell factories · 2024Review
- Crude Enzyme Concentrate of Filamentous Fungus Hydrolyzed Chitosan to Obtain Oligomers of Different Sizes.Polymers · 2023Article
- Property and Function of a Novel Chitinase Containing Dual Catalytic Domains Capable of Converting Chitin IntoFrontiers in microbiology · 2022Article
- Computational Analysis of Thermal Adaptation in Extremophilic Chitinases: The Achilles' Heel in Protein Structure and Industrial Utilization.Molecules (Basel, Switzerland) · 2021Article
- Progress and challenges in the synthesis of sequence controlled polysaccharides.Beilstein journal of organic chemistry · 2021Review
- Enzymatic Modification of Native Chitin and Conversion to Specialty Chemical Products.Marine drugs · 2020Review
- Chemoenzymatic Production and Engineering of Chitooligosaccharides andFrontiers in chemistry · 2020Review
- Chitinase: diversity, limitations, and trends in engineering for suitable applications.Bioscience reports · 2018Review
- Cloning, purification, and characterization of an organic solvent-tolerant chitinase, MtCh509, fromBiotechnology for biofuels · 2018Article
- Molecular characterization of a novel chitinaseBiotechnology for biofuels · 2018Article
- Transglycosylation by a chitinase from Enterobacter cloacae subsp. cloacae generates longer chitin oligosaccharides.Scientific reports · 2017Article
- Amino Groups of Chitosan Are Crucial for Binding to a Family 32 Carbohydrate Binding Module of a Chitosanase from Paenibacillus elgii.The Journal of biological chemistry · 2016Article
- Antifungal performance of extracellular chitinases and culture supernatants of Streptomyces galilaeus CFFSUR-B12 against Mycosphaerella fijiensis Morelet.World journal of microbiology & biotechnology · 2016Article
- Endoglycosidases for the Synthesis of Polysaccharides and Glycoconjugates.Advances in carbohydrate chemistry and biochemistry · 2016Review
- Characterization of the Pseudomonas aeruginosa Glycoside Hydrolase PslG Reveals That Its Levels Are Critical for Psl Polysaccharide Biosynthesis and Biofilm Formation.The Journal of biological chemistry · 2015Article
- Inverse relationship between chitobiase and transglycosylation activities of chitinase-D from Serratia proteamaculans revealed by mutational and biophysical analyses.Scientific reports · 2015Article
- Catalytic efficiency of chitinase-D on insoluble chitinous substrates was improved by fusing auxiliary domains.PloS one · 2015Article
- Structure of chitinase D from Serratia proteamaculans reveals the structural basis of its dual action of hydrolysis and transglycosylation.International journal of biochemistry and molecular biology · 2013Article
- Transglycosylation by chitinase D from Serratia proteamaculans improved through altered substrate interactions.The Journal of biological chemistry · 2012Article
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2 authors at 1 institution in 1 country.
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Abstract
We describe the heterologous expression and characterization of a 407-residue single-domain glycosyl hydrolase family 18 chitinase (SpChiD) from Gram-negative Serratia proteamaculans 568 that has unprecedented catalytic properties. SpChiD was optimally active at pH 6.0 and 40 °C, where it showed a K(m) of 83 mg ml(-1), a k(cat) of 3.9 × 10(2) h(-1), and a k(cat)/K(m) of 4.7 h mg(-1) ml(-1) on colloidal chitin. On chitobiose, the K(m), k(cat), and k(cat)/K(m) were 203 μM, 1.3 × 10(2) h(-1), and 0.62 h(-1) μM(-1), respectively. Hydrolytic activity on chitooligosaccharides (CHOS) and colloidal chitin indicated that SpChiD was an endo-acting processive enzyme, with the unique ability to convert released chitobiose to N-acetylglucosamine, the major end product. SpChiD showed hyper transglycosylation (TG) with trimer-hexamer CHOS substrates, generating considerable amounts of long-chain CHOS. The TG activity of SpChiD was dependent on both the length and concentration of the oligomeric substrate and also on the enzyme concentration. The length and amount of accumulated TG products increased with increases in the length of the substrate and its concentration and decreased with increases in the enzyme concentration. The SpChiD bound to insoluble and soluble chitin substrates despite the absence of accessory domains. Sequence alignments and structural modeling indicated that SpChiD would have a deep substrate-binding groove lined with aromatic residues, which is characteristic of processive enzymes. SpChiD shows a combination of properties that seems rare among family 18 chitinases and that may resemble the properties of human chitotriosidase.
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