Creatine Phosphate−Creatine Kinase in Enzymatic Synthesis of Glycoconjugates
摘要:
[GRAPHICS]Enzymatic production of glycoconjugates is hampered by expensive phosphagens such as acetyl phosphate (AcP) and phosphoenolpyruvate (PEP). Here, we introduce creatine phosphate-creatine kinase system as a novel and practical energy source in carbohydrate synthesis. This system was successfully demonstrated in the production of bioactive oligosaccharides with different sugar nucleotide regeneration systems.
Disclosed herein is a method for binding enzymes comprising reacting an amino acid and/or a protein with an excess of a urethane prepolymer, curing the resulting product and coupling an enzyme thereto by use of a carbodiimide. The product of the process is also described as well as the use thereof in analyzing blood fluids. The invention is particularly adapted to binding hexokinase and glucose-6-phosphate dehydrogenase to determine creatine phosphokinase (CPK) in human blood serum.
The disclosure concerns the enzymatic synthesis of stable analogues of nicotinamide adenine dinucleotide NAD/NADH and nicotinamide adenine dinucleotide phosphate NADP/NADPH, the so-called “carba-NADs”, i.e. analogues of NAD/NADH or NADP/NADPH, respectively, comprising a carbacyclic sugar instead of ribose.
The disclosure concerns the enzymatic synthesis of stable analogues of nicotinamide adenine dinucleotide NAD/NADH and nicotinamide adenine dinucleotide phosphate NADP/NADPH, the so-called “carba-NADs”, i.e. analogues of NAD/NADH or NADP/NADPH, respectively, comprising a carbacyclic sugar instead of ribose.
Disclosed herein are methods of screening compounds that modulate G-protein coupled receptors. The assays are performed at temperatures of between about 25° C. and 40° C.