Mutation of a conserved tryptophan in the chitin-binding cleft of Serratia marcescens chitinase A enhances transglycosylation. - Wikidata - awgldk - TriplyDB

Mutation of a conserved tryptophan in the chitin-binding cleft of Serratia marcescens chitinase A enhances transglycosylation.

Mutation of a conserved tryptophan in the chitin-binding cleft of Serratia marcescens chitinase A enhances transglycosylation.

http://www.wikidata.org/entity/Q38316554

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Hallmarks of Processivity in Glycoside Hydrolases from Crystallographic and Computational Studies of the Serratia marcescens Chitinases Crystal structure and chitin oligosaccharide-binding mode of a 'loopful' family GH19 chitinase from rye, Secale cereale, seeds Structure of chitinase D from Serratia proteamaculans reveals the structural basis of its dual action of hydrolysis and transglycosylation Crystal structures and inhibitor binding properties of plant class V chitinases: the cycad enzyme exhibits unique structural and functional features A plant class V chitinase from a cycad (Cycas revoluta): biochemical characterization, cDNA isolation, and posttranslational modification.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.Optimum substrate size and specific anomer requirements for the reducing-end glycoside hydrolase di-N-acetylchitobiase.Chemoenzymatic synthesis of N-linked neoglycoproteins through a chitinase-catalyzed transglycosylation.Characterization of two novel bacterial type A exo-chitobiose hydrolases having C-terminal 5/12-type carbohydrate-binding modules.Modulation of the transglycosylation activity of plant family GH18 chitinase by removing or introducing a tryptophan side chain.Transglycosylation by chitinase D from Serratia proteamaculans improved through altered substrate interactions.Glycosynthesis in a waterworld: new insight into the molecular basis of transglycosylation in retaining glycoside hydrolases.Strategy in manipulating transglycosylation activity of glycosyl hydrolase for oligosaccharide production.The chitinase C gene PsChiC from Pseudomonas sp. and its synergistic effects on larvicidal activity.Aromatic residues in the catalytic center of chitinase A from Serratia marcescens affect processivity, enzyme activity, and biomass converting efficiency.Eliminating hydrolytic activity without affecting the transglycosylation of a GH1 β-glucosidase Introducing transgalactosylation activity into a family 42 β-galactosidase.Mutation strategies for obtaining chitooligosaccharides with longer chains by transglycosylation reaction of family GH18 chitinase.

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P2860

Mutation of a conserved tryptophan in the chitin-binding cleft of Serratia marcescens chitinase A enhances transglycosylation.

http://www.wikidata.org/entity/Q38316554

description

2006 nî lūn-bûn

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2006年の論文

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2006年論文

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2006年論文

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2006年論文

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2006年論文

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2006年論文

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2006年论文

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2006年论文

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2006年论文

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name

Mutation of a conserved trypto ...... A enhances transglycosylation.

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type

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Mutation of a conserved trypto ...... A enhances transglycosylation.

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Mutation of a conserved trypto ...... A enhances transglycosylation.

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Bioscience, Biotechnology, and Biochemistry

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Mutation of a conserved trypto ...... A enhances transglycosylation.

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Brian A Halloran

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Edward J Meehan

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Liqing Chen

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Mikhail F Alexeyev

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Nathan N Aronson

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Xiaoyin E Zhou

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Yujun Wang

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P2860

Glycoside hydrolases and glycosyltransferases. Families, modules, and implications for genomics

Structures of chitobiase mutants complexed with the substrate Di-N-acetyl-d-glucosamine: the catalytic role of the conserved acidic pair, aspartate 539 and glutamate 540

Structural basis for the substrate specificity of endo-beta-N-acetylglucosaminidase F(3)

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

High resolution structural analyses of mutant chitinase A complexes with substrates provide new insight into the mechanism of catalysis

The structure of an allosamidin complex with the Coccidioides immitis chitinase defines a role for a second acid residue in substrate-assisted mechanism

Family 18 chitinase–oligosaccharide substrate interaction: subsite preference and anomer selectivity of Serratia marcescens chitinase A

Structure of the D142N mutant of the family 18 chitinase ChiB from Serratia marcescens and its complex with allosamidin

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

Crystal structure of a bacterial chitinase at 2.3 A resolution

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243-251

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scholarly article

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10.1271/BBB.70.243

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1

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70

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2006-01-01T00:00:00Z

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16428843

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