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  2. Osazone - Wikipedia

    en.wikipedia.org/wiki/Osazone

    Sucrose, which is nonreducing, does not form an osazone. A typical reaction showing the formation of an osazone. D-glucose reacts with phenylhydrazine to give glucosazone. The same product is obtained from fructose and mannose. General steps in osazone formation

  3. Coenzyme Q – cytochrome c reductase - Wikipedia

    en.wikipedia.org/wiki/Coenzyme_Q_–_cytochrome_c...

    Electron leakage occurs mainly at the Q o site and is stimulated by antimycin A. Antimycin A locks the b hemes in the reduced state by preventing their re-oxidation at the Q i site, which, in turn, causes the steady-state concentrations of the Q o semiquinone to rise, the latter species reacting with oxygen to form superoxide.

  4. O-linked glycosylation - Wikipedia

    en.wikipedia.org/wiki/O-linked_glycosylation

    O-GlcNAcylation and phosphorylation can occur on the same threonine and serine residues, suggesting a complex relationship between these modifications that can affect many functions of the cell. [ 6 ] [ 12 ] The modification affects processes like the cells response to cellular stress, the cell cycle, protein stability and protein turnover.

  5. Hydrazone - Wikipedia

    en.wikipedia.org/wiki/Hydrazone

    Pigment Yellow 97, a popular yellow colorant, is a hydrazone. [6]Hydrazones are the basis for various analyses of ketones and aldehydes. For example, dinitrophenylhydrazine coated onto a silica sorbent is the basis of an adsorption cartridge.

  6. Active site - Wikipedia

    en.wikipedia.org/wiki/Active_site

    The active site consists of amino acid residues that form temporary bonds with the substrate, the binding site, and residues that catalyse a reaction of that substrate, the catalytic site. Although the active site occupies only ~10–20% of the volume of an enzyme, [ 1 ] : 19 it is the most important part as it directly catalyzes the chemical ...

  7. Oxidative phosphorylation - Wikipedia

    en.wikipedia.org/wiki/Oxidative_phosphorylation

    ATP synthase, also called complex V, is the final enzyme in the oxidative phosphorylation pathway. This enzyme is found in all forms of life and functions in the same way in both prokaryotes and eukaryotes. [67] The enzyme uses the energy stored in a proton gradient across a membrane to drive the synthesis of ATP from ADP and phosphate (P i).

  8. Enzyme catalysis - Wikipedia

    en.wikipedia.org/wiki/Enzyme_catalysis

    Enzyme changes shape by induced fit upon substrate binding to form enzyme-substrate complex. Hexokinase has a large induced fit motion that closes over the substrates adenosine triphosphate and xylose. Binding sites in blue, substrates in black and Mg 2+ cofactor in yellow. (The different mechanisms of substrate binding

  9. N-linked glycosylation - Wikipedia

    en.wikipedia.org/wiki/N-linked_glycosylation

    The different types of lipid-linked oligosaccharide (LLO) precursor produced in different organisms.. N-linked glycosylation is the attachment of an oligosaccharide, a carbohydrate consisting of several sugar molecules, sometimes also referred to as glycan, to a nitrogen atom (the amide nitrogen of an asparagine (Asn) residue of a protein), in a process called N-glycosylation, studied in ...