Carbohydrate-Active Enzymes Structure, Activity and Reaction Products

• Muut tekijät: Benini, Stefano (Toimittaja)
• Aineistotyyppi: Elektroninen Kirjan osa
• Kieli: englanti
• Julkaistu: Basel, Switzerland MDPI - Multidisciplinary Digital Publishing Institute 2020
• Aiheet: Research & information: general; Biology, life sciences; glycoside hydrolase; xylanase; carbohydrate-binding module; CBM truncation; halo-tolerant; xylan hydrolysis; pectate lyase; Paenibacillus polymyxa; pectins; degradation; Lactobacillus; GH13_18; sucrose phosphorylase; glycoside phosphorylase; Ilumatobacter coccineus; Thermoanaerobacterium thermosaccharolyticum; crystallography; galactosidase; hydrolysis; reaction mechanism; complex structures; cold-adapted; GH2; Cellulase; random mutagenesis; cellulose degradation; structural analysis; α-amylase; starch degradation; biotechnology; structure; pyruvylation; pyruvyltransferase; exopolysaccharides; capsular polysaccharides; cell wall glycopolymers; N-glycans; lipopolysaccharides; biosynthesis; sequence space; pyruvate analytics; Nanopore sequencing; ganoderic acid; Bacillus thuringiensis; biotransformation; glycosyltransferase; whole genome sequencing; applied biocatalysis; enzyme cascades; chemoenzymatic synthesis; sugar chemistry; carbohydrate; Leloir; nucleotide; Enzymatic glycosylation; alkyl glycosides (AG)s; Deep eutectic solvents (DES); Amy A; alcoholysis; methanol; circular dichroism; protein stability; alpha-amylase; biomass; hemicellulose; bioethanol; xylanolytic enzyme; hemicellulase; lysozyme; peptidoglycan cleavage; avian gut GH22; crystal structure; glycosylation; UDP-glucose pyrophosphorylase; UDP-glucose; nucleotide donors; Rhodococcus, Actinobacteria, gene redundancy; Leloir glycosyltransferases; activated sugar; UTP; thermophilic fungus; β-glucosidases; Chaetomium thermophilum; protein structure; fungal enzymes; endo-α-(1→6)-d-mannase; mannoside; Mycobacterium; lipomannan; lipoarabinomannan; phosphatidylinositol mannosides; GH68; fructosyltransferase; fructooligosaccharides; FOS biosynthesis; prebiotic oligosaccharides; Arxula adeninivorans; α-glucosidase; maltose; panose; amylopectin; glycogen; inhibition by Tris; transglycosylation; glycoside hydrolyase; Trichoderma harzianum; complete saccharification; lignocellulose; N-acetylhexosamine specificity; GH20; phylogenetic analysis; NAG-oxazoline; acceptor diversity; lacto-N-triose II; human milk oligosaccharides; NMR; molecular phylogeny; α2,8-sialyltransferases; polySia motifs; evolution; ST8Sia; functional genomics; n/a
• Linkit: DOAB: download the publication; DOAB: description of the publication

Carbohydrate-active enzymes are responsible for both biosynthesis and the breakdown of carbohydrates and glycoconjugates. They are involved in many metabolic pathways; in the biosynthesis and degradation of various biomolecules, such as bacterial exopolysaccharides, starch, cellulose and lignin; and...