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Strained Conformations of Nucleosides in Active Sites of Nucleoside Phosphorylases

open access: yesBiomolecules, 2020
Nucleoside phosphorylases catalyze the reversible phosphorolysis of nucleosides to heterocyclic bases, giving α-d-ribose-1-phosphate or α-d-2-deoxyribose-1-phosphate. These enzymes are involved in salvage pathways of nucleoside biosynthesis. The level of
Irina A. Il’icheva   +2 more
doaj   +2 more sources

Discovery and Biotechnological Exploitation of Glycoside-Phosphorylases. [PDF]

open access: yesInt J Mol Sci, 2022
Among carbohydrate active enzymes, glycoside phosphorylases (GPs) are valuable catalysts for white biotechnologies, due to their exquisite capacity to efficiently re-modulate oligo- and poly-saccharides, without the need for costly activated sugars as ...
Li A   +6 more
europepmc   +2 more sources

In vitro and in vivo exploration of the cellobiose and cellodextrin phosphorylases panel in Ruminiclostridium cellulolyticum: implication for cellulose catabolism

open access: yesBiotechnology for Biofuels, 2019
Background In anaerobic cellulolytic micro-organisms, cellulolysis results in the action of several cellulases gathered in extracellular multi-enzyme complexes called cellulosomes.
Nian Liu   +7 more
doaj   +2 more sources

Insights to improve the activity of glycosyl phosphorylases from Ruminococcus albus 8 with cello-oligosaccharides [PDF]

open access: yesFrontiers in Chemistry, 2023
The phosphorolysis of cello-oligosaccharides is a critical process played in the rumen by Ruminococcus albus to degrade cellulose. Cellodextrins, made up of a few glucosyl units, have gained lots of interest by their potential applications.
Alem Storani   +2 more
doaj   +2 more sources

Efficient Biocatalytic Synthesis of Dihalogenated Purine Nucleoside Analogues Applying Thermodynamic Calculations [PDF]

open access: yesMolecules, 2020
The enzymatic synthesis of nucleoside analogues has been shown to be a sustainable and efficient alternative to chemical synthesis routes. In this study, dihalogenated nucleoside analogues were produced by thermostable nucleoside phosphorylases in ...
Heba Yehia   +9 more
doaj   +3 more sources

Nucleoside Phosphorylases make N7-xanthosine [PDF]

open access: yesNature Communications
Modern, highly evolved nucleoside-processing enzymes are known to exhibit perfect regioselectivity over the glycosylation of purine nucleobases at N9. We herein report an exception to this paradigm.
Sarah Westarp   +9 more
doaj   +2 more sources

Can Crystal Symmetry and Packing Influence the Active Site Conformation of Homohexameric Purine Nucleoside Phosphorylases?

open access: yesCroatica Chemica Acta, 2016
It is generaly believed that enzymes retain most of their functionality in the crystal form due to the large solvent content of protein crystals. This is facilitated by the fact that their natural environment in solution is not too far from the one found
Marija Luić, Zoran Štefanić
doaj   +2 more sources

Bacterial Purine Nucleoside Phosphorylases from Mesophilic and Thermophilic Sources: Characterization of Their Interaction with Natural Nucleosides and Modified Arabinofuranoside Analogues [PDF]

open access: yesBiomolecules
The enzymatic synthesis of nucleoside derivatives is an important alternative to multi-step chemical methods traditionally used for this purpose. Despite several undeniable advantages of the enzymatic approach, there are a number of factors limiting its ...
Irina A. Bychek   +7 more
doaj   +2 more sources

Engineering a Bifunctional Fusion Purine/Pyrimidine Nucleoside Phosphorylase for the Production of Nucleoside Analogs [PDF]

open access: yesBiomolecules
Nucleoside phosphorylases (NPs) are pivotal enzymes in the salvage pathway, catalyzing the reversible phosphorolysis of nucleosides to produce nucleobases and α-D-ribose 1-phosphate.
Daniel Hormigo   +4 more
doaj   +2 more sources

Discovery of two β-1,2-mannoside phosphorylases showing different chain-length specificities from Thermoanaerobacter sp. X-514.

open access: yesPLoS ONE, 2014
We characterized Teth514_1788 and Teth514_1789, belonging to glycoside hydrolase family 130, from Thermoanaerobacter sp. X-514. These two enzymes catalyzed the synthesis of 1,2-β-oligomannan using β-1,2-mannobiose and d-mannose as the optimal acceptors ...
Kazuhiro Chiku   +6 more
doaj   +2 more sources

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