Catalytic Mechanism of a Novel Glycoside Hydrolase Family 16 "Elongating" β-Transglycosylase.

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Catalytic Mechanism of a Novel Glycoside Hydrolase Family 16 "Elongating" β-Transglycosylase.

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2016 nî lūn-bûn

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2016年の論文

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2016年学术文章

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2016年学术文章

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2016年学术文章

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2016年学术文章

@zh-my

2016年学术文章

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2016年學術文章

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2016年學術文章

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2016年學術文章

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name

Catalytic Mechanism of a Novel ...... longating" β-Transglycosylase.

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Item

label

Catalytic Mechanism of a Novel ...... longating" β-Transglycosylase.

@en

prefLabel

Catalytic Mechanism of a Novel ...... longating" β-Transglycosylase.

@en

P1476

Catalytic Mechanism of a Novel ...... Elongating" β-Transglycosylase

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P2093

Liming Zhao

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Qiaojuan Yan

http://www.w3.org/2001/XMLSchema#string

Shaoqing Yang

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Xin You

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Zhengqiang Jiang

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P2860

MolProbity: all-atom structure validation for macromolecular crystallography

PHENIX: a comprehensive Python-based system for macromolecular structure solution

Amylosucrase, a glucan-synthesizing enzyme from the alpha-amylase family

Oligosaccharide and sucrose complexes of amylosucrase. Structural implications for the polymerase activity

Crystal structure of a family 16 endoglucanase from the hyperthermophile Pyrococcus furiosus--structural basis of substrate recognition

X-ray crystal structures of Phanerochaete chrysosporium Laminarinase 16A in complex with products from lichenin and laminarin hydrolysis

Synthesis of cyclic beta-glucan using laminarinase 16A glycosynthase mutant from the basidiomycete Phanerochaete chrysosporium

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

The -Glucanase ZgLamA from Zobellia galactanivorans Evolved a Bent Active Site Adapted for Efficient Degradation of Algal Laminarin

Structural and mutagenetic analyses of a 1,3-1,4-β-glucanase from Paecilomyces thermophila

P304

1666-1678

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P31

scholarly article

P356

10.1074/JBC.M116.762419

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P407

English

P433

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P478

292

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P50

Zhen Qin

P577

2016-12-12T00:00:00Z

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P698

27956553

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P932

5290943

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