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Biochemical characterization and low-resolution SAXS structure of two-domain endoglucanase BlCel9 from Bacillus licheniformis
(Springer, 2019-02-01)
Lignocellulose feedstock constitutes the most abundant carbon source in the biosphere; however, its recalcitrance remains a challenge for microbial conversion into biofuel and bioproducts. Bacillus licheniformis is a ...
Discovery of processive catalysis by an exo-hydrolase with a pocket-shaped active site
(Nature Publishing Group, 2019-12)
Substrates associate and products dissociate from enzyme catalytic sites rapidly, which hampers investigations of their trajectories. The high-resolution structure of the native Hordeum exo-hydrolase HvExoI isolated from ...
Functional demonstrations of starch binding domains present in Ostreococcus tauri starch synthases isoforms
(BioMed Central, 2015-10)
Abstract Background: Starch‑binding domains are key modules present in several enzymes involved in polysaccharide metabolism. These non‑catalytic modules have already been described as essential for starch‑binding and the ...
Small-angle X-ray scattering and structural modeling of full-length: Cellobiohydrolase I from Trichoderma harzianum
(2013-08-01)
Cellobiohydrolases hydrolyze cellulose releasing cellobiose units. They are very important for a number of biotechnological applications, such as, for example, production of cellulosic ethanol and cotton fiber processing. ...
Small-angle X-ray scattering and structural modeling of full-length: Cellobiohydrolase I from Trichoderma harzianum
(2013-08-01)
Cellobiohydrolases hydrolyze cellulose releasing cellobiose units. They are very important for a number of biotechnological applications, such as, for example, production of cellulosic ethanol and cotton fiber processing. ...
Structural basis for branching-enzyme activity of glycoside hydrolase family 57: Structure and stability studies of a novel branching enzyme from the hyperthermophilic archaeon Thermococcus Kodakaraensis KOD1
(Wiley-Blackwell, 2011-02-01)
Branching enzymes (BEs) catalyze the formation of branch points in glycogen and amylopectin by cleavage of alpha-1,4 glycosidic bonds and subsequent transfer to a new alpha-1,6 position. BEs generally belong to glycoside ...
Structural basis for branching-enzyme activity of glycoside hydrolase family 57: Structure and stability studies of a novel branching enzyme from the hyperthermophilic archaeon Thermococcus Kodakaraensis KOD1
(Wiley-Blackwell, 2011-02-01)
Branching enzymes (BEs) catalyze the formation of branch points in glycogen and amylopectin by cleavage of alpha-1,4 glycosidic bonds and subsequent transfer to a new alpha-1,6 position. BEs generally belong to glycoside ...
An acetylation site in lectin domain modulates the biological activity of polypeptide GalNAc-transferase-2
(De Gruyter, 2012-12)
Polypeptide GalNAc-transferases (ppGalNAc-Ts) are a family of enzymes that catalyze the initiation of mucintype O -glycosylation. All ppGalNAc-T family members contain a common (QXW) 3 motif, which is present in the R-type ...
Key events in microvascular damage induced by snake venom hemorrhagic metalloproteinases
(2011-08-24)
Hemorrhage is one of the most significant effects in envenomings induced by viperid snakebites. Damage to the microvasculature, induced by snake venom metalloproteinases (SVMPs), is the main event responsible for this ...