Costs and benefits of processivity in enzymatic degradation of recalcitrant polysaccharides. - Wikidata - wikimedia - TriplyDB

Costs and benefits of processivity in enzymatic degradation of recalcitrant polysaccharides.

Costs and benefits of processivity in enzymatic degradation of recalcitrant polysaccharides.

http://www.wikidata.org/entity/Q35722100

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Bioproduction of chitooligosaccharides: present and perspectives Crystal Structures of Bacillus cereus NCTU2 Chitinase Complexes with Chitooligomers Reveal Novel Substrate Binding for Catalysis: A CHITINASE WITHOUT CHITIN BINDING AND INSERTION DOMAINS Crystal structure and mode of action of a class V chitinase from Nicotiana tabacum Hallmarks of Processivity in Glycoside Hydrolases from Crystallographic and Computational Studies of the Serratia marcescens Chitinases Crystal Structures of the Laminarinase Catalytic Domain from Thermotoga maritima MSB8 in Complex with Inhibitors: ESSENTIAL RESIDUES FOR -1,3- and -1,4-GLUCAN SELECTION Structural, Biochemical, and Computational Characterization of the Glycoside Hydrolase Family 7 Cellobiohydrolase of the Tree-killing Fungus Heterobasidion irregulare Structural characterization of a unique marine animal family 7 cellobiohydrolase suggests a mechanism of cellulase salt tolerance.Crystal structure and chitin oligosaccharide-binding mode of a 'loopful' family GH19 chitinase from rye, Secale cereale, seeds Cel48A from Thermobifida fusca: structure and site directed mutagenesis of key residues Crystal structures of substrate-bound chitinase from the psychrophilic bacterium Moritella marina and its structure in solution Structural insights into the substrate-binding mechanism for a novel chitosanase Soil bacterial community shifts after chitin enrichment: an integrative metagenomic approach Dual substrate specificity of an N-acetylglucosamine phosphotransferase system in Clostridium beijerinckii Multiple functions of aromatic-carbohydrate interactions in a processive cellulase examined with molecular simulation Structure, dynamics, and specificity of endoglucanase D from Clostridium cellulovorans Chitinase from Autographa californica multiple nucleopolyhedrovirus: rapid purification from Sf-9 medium and mode of action.Introduction of a tryptophan side chain into subsite +1 enhances transglycosylation activity of a GH-18 chitinase from Arabidopsis thaliana, AtChiC.Cellobiohydrolase and endoglucanase respond differently to surfactants during the hydrolysis of cellulose.Computational investigation of glycosylation effects on a family 1 carbohydrate-binding module.X-Ray Crystal Structure of the Full Length Human Chitotriosidase (CHIT1) Reveals Features of Its Chitin Binding Domain.Corynebacterium glutamicum possesses β-N-acetylglucosaminidase Novel enzymes for the degradation of cellulose Increased enzyme binding to substrate is not necessary for more efficient cellulose hydrolysis.Processive endoglucanases mediate degradation of cellulose by Saccharophagus degradans A Lytic Polysaccharide Monooxygenase with Broad Xyloglucan Specificity from the Brown-Rot Fungus Gloeophyllum trabeum and Its Action on Cellulose-Xyloglucan Complexes.Production of chitooligosaccharides and their potential applications in medicine Biocatalytic conversion of lignocellulose to platform chemicals.Chitinolytic enzymes: an appraisal as a product of commercial potential.Transglycosylation by a chitinase from Enterobacter cloacae subsp. cloacae generates longer chitin oligosaccharides Modulation of the transglycosylation activity of plant family GH18 chitinase by removing or introducing a tryptophan side chain.Temperature Effects on Kinetic Parameters and Substrate Affinity of Cel7A Cellobiohydrolases.Kinetics of cellobiohydrolase (Cel7A) variants with lowered substrate affinity.Molecular dynamics simulation of the processive endocellulase Cel48F from Clostridium cellulolyticum: a novel "water-control mechanism" in enzymatic hydrolysis of cellulose.Structure-guided analysis of catalytic specificity of the abundantly secreted chitosanase SACTE_5457 from Streptomyces sp. SirexAA-E.Analysis of productive binding modes in the human chitotriosidase.The first identification of carbohydrate binding modules specific to chitosan.Characterization of two Listeria innocua chitinases of different sizes that were expressed in Escherichia coli.Substrate dynamics in enzyme action: rotations of monosaccharide subunits in the binding groove are essential for pectin methylesterase processivity.Processivity of cellobiohydrolases is limited by the substrate.Listeria monocytogenes has a functional chitinolytic system and an active lytic polysaccharide monooxygenase.

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P2860

Costs and benefits of processivity in enzymatic degradation of recalcitrant polysaccharides.

http://www.wikidata.org/entity/Q35722100

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2006 nî lūn-bûn

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2006年の論文

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Costs and benefits of processi ...... recalcitrant polysaccharides.

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Costs and benefits of processi ...... recalcitrant polysaccharides.

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Costs and benefits of processi ...... recalcitrant polysaccharides.

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Costs and benefits of processi ...... recalcitrant polysaccharides.

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Costs and benefits of processi ...... recalcitrant polysaccharides.

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Proceedings of the National Academy of Sciences of the United States of America

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Costs and benefits of processi ...... f recalcitrant polysaccharides

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Bjørnar Synstad

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Gert Vriend

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Jannicke B Cederkvist

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Kjell M Vårum

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Morten Sørlie

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P2860

Structure of a two-domain chitotriosidase from Serratia marcescens at 1.9-A resolution

Structural insights into the catalytic mechanism of a family 18 exo-chitinase

Structural basis for ligand binding and processivity in cellobiohydrolase Cel6A from Humicola insolens

Engineering the exo-loop of Trichoderma reesei cellobiohydrolase, Cel7A. A comparison with Phanerochaete chrysosporium Cel7D

Three-dimensional structure of cellobiohydrolase II from Trichoderma reesei

Stereochemistry of chitin hydrolysis by a plant chitinase/lysozyme and X-ray structure of a complex with allosamidin: evidence for substrate assisted catalysis

The three-dimensional crystal structure of the catalytic core of cellobiohydrolase I from Trichoderma reesei

High-resolution crystal structures reveal how a cellulose chain is bound in the 50 A long tunnel of cellobiohydrolase I from Trichoderma reesei

Structures and mechanisms of glycosyl hydrolases

The path forward for biofuels and biomaterials

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10.1073/PNAS.0608909103

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48

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103

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Gustav Vaaje-Kolstad

Vincent G H Eijsink

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2006-11-20T00:00:00Z

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6680874

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polysaccharides

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