Results 21 to 30 of about 38,220 (259)
Disaccharide phosphorylases: Structure, catalytic mechanisms and directed evolution
Synthetic and Systems Biotechnology, 2021 Disaccharide phosphorylases (DSPs) are carbohydrate-active enzymes with outstanding potential for the biocatalytic conversion of common table sugar into products with attractive properties. They are modular enzymes that form active homo-oligomers. From a
Shangshang Sun, Chun You
doaj +1 more source
Evolution of Phosphorylases from N-Acetylglucosaminide Hydrolases in Family GH3
, 2021 Glycoside phosphorylases hold great potential as catalysts for the synthesis of valuable sugars, glycosides, and glycans or for the development of energy-efficient microbial cell factories.
Jorick Franceus +4 more
semanticscholar +1 more source
Co-receptor CD8-mediated modulation of T-cell receptor functional sensitivity and epitope recognition degeneracy [PDF]
, 2013 The interaction between T-cell receptors (TCRs) and peptide epitopes is highly degenerate: a TCR is capable of interacting productively with a wide range of different peptide ligands, involving not only cross-reactivity proper (similar epitopes elicit ...
Berg, Hugo van den +3 more
core +7 more sources
Old player, new roles: defining the role of the plastidial phosphorylase. [PDF]
New PhytolSummary The plastidial phosphorylase (Pho1 or Phs1; E.C. 2.4.1.1) is a ubiquitous enzyme among plants that catalyzes the formation and degradation of glucans. Although the first report connecting Pho1 with starch metabolism came out > 80 years ago, its precise role is still a matter of debate.
Seung D, Orzechowski S, Fettke J.
europepmc +2 more sources
Journal of the American Chemical Society, 2020 Glycoside hydrolases and phosphorylases are two major classes of enzymes responsible for the cleavage of glycosidic bonds. Here we show that two GH84 O-GlcNAcase enzymes can be converted to efficient phosphorylases by a single point mutation. Noteworthy,
D. Tezé +8 more
semanticscholar +1 more source
Molecules, 2023 The complete mechanism behind starch regulation has not been fully characterized. However, significant progress can be achieved through proteomic approaches.
Junio Flores Castellanos +2 more
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Structural and catalytic analysis of two diverse uridine phosphorylases in Phytophthora capsici
Scientific Reports, 2020 Uridine phosphorylase (UP) is a key enzyme of pyrimidine salvage pathways that enables the recycling of endogenous or exogenous-supplied pyrimidines and plays an important intracellular metabolic role.
Cancan Yang +7 more
semanticscholar +1 more source
Molecules, 2021 The Glycoside Hydrolase Family 65 (GH65) is an enzyme family of inverting α-glucoside phosphorylases and hydrolases that currently contains 10 characterized enzyme specificities. However, its sequence diversity has never been studied in detail.
Emma De Beul +3 more
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Structure of purine nucleoside phosphorylase (DeoD) from Bacillus anthracis [PDF]
, 2005 Protein structures from the causative agent of anthrax (Bacillus anthracis) are being determined as part of a structural genomics programme. Amongst initial candidates for crystallographic analysis are enzymes involved in nucleotide biosynthesis, since ...
Blagova, E V +6 more
core +3 more sources
Thermodynamic reaction control of nucleoside phosphorolysis [PDF]
, 2020 Nucleoside analogs represent a class of important drugs for cancer and antiviral treatments. Nucleoside phosphorylases (NPases) catalyze the phosphorolysis of nucleosides and are widely employed for the synthesis of pentose‐1‐phosphates and nucleoside ...
Giessmann, Robert T. +4 more
core +1 more source