Results 131 to 140 of about 32,747,610 (220)

Natural Variation in Brachypodium distachyon Primarily Links Lignin Reinforcement to Rhizoctonia solani Resistance

Plant, Cell &Environment, EarlyView.
Rozi Fernanda, Niranjan Mahadevan, Megumi Watanabe, Nanami Sakata, Hidenori Matsui, Kazuhiro Toyoda, Yuki Ichinose, Yoshiteru Noutoshi   +7 more
wiley   +1 more source

Additional file 1: of Functional diversification of horizontally acquired glycoside hydrolase family 45 (GH45) proteins in Phytophaga beetles

, 2019
Table S1 to S4; Figs. S1 to S10 (legends included). (DOCX 22341 kb)
Busch, AndrĂŠ, Danchin, Etienne, Pauchet, Yannick   +2 more
openaire   +1 more source

Molecular Cloning, Characterization, and Application of a Novel Multifunctional Isoamylase (MIsA) from Myxococcus sp. Strain V11

Foods
A novel multifunctional isoamylase, MIsA from Myxococcus sp. strain V11, was expressed in Escherichia coli BL21(DE3). Sequence alignment revealed that MIsA is a typical isoamylase that belongs to glycoside hydrolase family 13 (GH 13).
Siting Feng, Weiqi Zhang, Jun Liu, Yusen Hu, Jialei Wu, Guorong Ni, Fei Wang   +6 more
doaj   +1 more source

Structural determinants of cold activity and glucose tolerance of a family 1 glycoside hydrolase ( GH1 ) from Antarctic Marinomonas sp. ef1

The FEBS Journal
Cold‐active enzymes support life at low temperatures due to their ability to maintain high activity in the cold and can be useful in several biotechnological applications. Although information on the mechanisms of enzyme cold adaptation is still too limited to devise general rules, it appears that very diverse structural and ...
Louise Jane Gourlay, Marco Mangiagalli, Elisabetta Moroni, Marina Lotti, Marco Nardini   +4 more
openaire   +5 more sources

Reaction Mechanism of Glycoside Hydrolase Family 116 Utilizes Perpendicular Protonation [PDF]

Retaining glycoside hydrolases use acid/base catalysis with an enzymatic acid/base protonating the glycosidic bond oxygen to facilitate leaving-group departure alongside attack by a catalytic nucleophile to form a covalent intermediate.
Piniello, Beatriz, Davies, Gideon J., Ketudat Cairns, James R., Pengthaisong, Salila, Rovira i Virgili, Carme   +4 more
core   +1 more source

Computational Studies of Glycoside, Carboxylic Ester, and Thioester Hydrolase Mechanisms: A Review

, 2015
This article is a review of computational work over the last ∼15 years to elucidate the catalytic mechanisms of three major enzyme classes: glycoside hydrolases, carboxylic ester hydrolases, and thioesterases.
Carme Rovira (1275285), Peter J. Reilly (1499431)   +1 more
core   +1 more source

Advancements in the Heterologous Expression of Sucrose Phosphorylase and Its Molecular Modification for the Synthesis of Glycosylated Products

Molecules
Sucrose phosphorylase (SPase), a member of the glycoside hydrolase GH13 family, possesses the ability to catalyze the hydrolysis of sucrose to generate α-glucose-1-phosphate and can also glycosylate diverse substrates, showcasing a wide substrate ...
Hongyu Zhang, Leting Zhu, Zixuan Zhou, Danyun Wang, Jinshan Yang, Suying Wang, Tingting Lou   +6 more
doaj   +1 more source

How a Glycoside Hydrolase Recognizes a Helical Polyglucan.

, 2017
International audienceSimilarly to other biopolymers, linear polysaccharides can form double- or triple-helical structures. How enzymes recognize and manage this quaternary structure is an unresolved question. In this issue of Structure, Pluvinage et al.
Garron, Marie-Line, Henrissat, Bernard, Marie-Line Garron, Bernard Henrissat   +3 more
core   +1 more source

Advancements in the Engineering Modification of Sucrose Phosphorylase

Crystals
Sucrose phosphorylase (SPase) is a member of the glycoside hydrolase family 13, catalyzing the reversible phosphorolysis of sucrose to produce α–glucose–1–phosphate and exhibiting transglycosylation activity toward multiple substrates. Its wide substrate
Shuru Ma, Hongyu Zhang, Tingting Lou, Suying Wang   +3 more
doaj   +1 more source

Structures, kinetics, and modeling of glycoside hydrolase family 44 endoglucanases from Clostridium acetobutylicum and Ruminococcus flavefaciens FD-1

, 2018
Glycoside hydrolases (GH) are enzymes that hydrolyze glycosidic bonds between carbohydrates. Family 44 contains endo- and xylo- glucanases capable of hydrolyzing cellulose and hemicelluose. Two members produced by Clostridium acetobutylicum and Ruminococcus flavefaciens FD-1 are the subjects of characterization work in this dissertation.
openaire   +3 more sources