Aromatic residues within the substrate-binding cleft of Bacillus circulans chitinase A1 are essential for hydrolysis of crystalline chitin. - Wikidata - awgldk - TriplyDB

Aromatic residues within the substrate-binding cleft of Bacillus circulans chitinase A1 are essential for hydrolysis of crystalline chitin.

Aromatic residues within the substrate-binding cleft of Bacillus circulans chitinase A1 are essential for hydrolysis of crystalline chitin.

http://www.wikidata.org/entity/Q38351265

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Kinetic and crystallographic analyses of the catalytic domain of chitinase from Pyrococcus furiosus- the role of conserved residues in the active site 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 and inhibitor binding properties of plant class V chitinases: the cycad enzyme exhibits unique structural and functional features Sequence and structural analysis of the chitinase insertion domain reveals two conserved motifs involved in chitin-binding Multiple functions of aromatic-carbohydrate interactions in a processive cellulase examined with molecular simulation The effects of the surface-exposed residues on the binding and hydrolytic activities of Vibrio carchariae chitinase A.Structure, dynamics, and specificity of endoglucanase D from Clostridium cellulovorans A new chitinase-producer strain Streptomyces glauciniger WICC-A03: isolation and identification as a biocontrol agent for plants phytopathogenic fungi.Costs and benefits of processivity in enzymatic degradation of recalcitrant polysaccharides.Chitin research revisited.Transglycosylation by a chitinase from Enterobacter cloacae subsp. cloacae generates longer chitin oligosaccharides Kinetics of cellobiohydrolase (Cel7A) variants with lowered substrate affinity.Mutation of a conserved tryptophan in the chitin-binding cleft of Serratia marcescens chitinase A enhances transglycosylation.Transglycosylation by chitinase D from Serratia proteamaculans improved through altered substrate interactions.Characterization of two Listeria innocua chitinases of different sizes that were expressed in Escherichia coli.Isolation and molecular characterization of chitinase-deficient Bacillus licheniformis strains capable of deproteinization of shrimp shell waste to obtain highly viscous chitin.Effects of C-terminal domain truncation on enzyme properties of Serratia marcescens chitinase C.Structural Features of a Bacteroidetes-Affiliated Cellulase Linked with a Polysaccharide Utilization Locus.Proteolytic release of the intramolecular chaperone domain confers processivity to endosialidase F.Characterization of a Bacillus thuringiensis chitinase that binds to cellulose and chitin.Substrate binding modes and anomer selectivity of chitinase A from Vibrio harveyi.Aromatic residues in the catalytic center of chitinase A from Serratia marcescens affect processivity, enzyme activity, and biomass converting efficiency.Stomach Chitinase from Japanese Sardine Sardinops melanostictus: Purification, Characterization, and Molecular Cloning of Chitinase Isozymes with a Long Linker.Effect of C-terminal truncation on enzyme properties of recombinant amylopullulanase from Thermoanaerobacter pseudoethanolicus.Structural prediction of a novel chitinase from the psychrophilic Glaciozyma antarctica PI12 and an analysis of its structural properties and function.Biochemical characteristics of C-terminal region of recombinant chitinase from Bacillus licheniformis: implication of necessity for enzyme properties.Kinetic evidence related to substrate-assisted catalysis of family 18 chitinases.Structural insights into marine carbohydrate degradation by family GH16 κ-carrageenases.Biochemical characterization of two truncated forms of amylopullulanase from Thermoanaerobacterium saccharolyticum NTOU1 to identify its enzymatically active region.

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P2860

Aromatic residues within the substrate-binding cleft of Bacillus circulans chitinase A1 are essential for hydrolysis of crystalline chitin.

http://www.wikidata.org/entity/Q38351265

description

2003 nî lūn-bûn

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2003年の論文

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2003年学术文章

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2003年学术文章

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2003年学术文章

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2003年学术文章

@zh-my

2003年学术文章

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2003年學術文章

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2003年學術文章

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2003年學術文章

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name

Aromatic residues within the s ...... rolysis of crystalline chitin.

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Aromatic residues within the s ...... rolysis of crystalline chitin.

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Aromatic residues within the s ...... rolysis of crystalline chitin.

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P2860

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P1433

Biochemical Journal

P1476

Aromatic residues within the s ...... rolysis of crystalline chitin.

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P2093

Junji Sugiyama

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Masayuki Hashimoto

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Naoki Nikaidou

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Tadayuki Toratani

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Takamasa Nonaka

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Takeshi Watanabe

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Urara Sato

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Yuichiro Kezuka

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Yumiko Ariga

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P2860

A classification of glycosyl hydrolases based on amino acid sequence similarities

New families in the classification of glycosyl hydrolases based on amino acid sequence similarities

Cleavage of structural proteins during the assembly of the head of bacteriophage T4

Solution structure of the chitin-binding domain of Bacillus circulans WL-12 chitinase A1

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

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

Solution structure of the fibronectin type III domain from Bacillus circulans WL-12 chitinase A1

Expression and characterization of active site mutants of hevamine, a chitinase from the rubber tree Hevea brasiliensis

Crystal structure of a bacterial chitinase at 2.3 A resolution

How to measure and predict the molar absorption coefficient of a protein

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237-244

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scholarly article

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10.1042/BJ20030419

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P433

Pt 1

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P478

376

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2003-11-01T00:00:00Z

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12930197

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P932

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