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  2. Enzyme - Wikipedia

    en.wikipedia.org/wiki/Enzyme

    Enzymes can be classified by two main criteria: either amino acid sequence similarity (and thus evolutionary relationship) or enzymatic activity. Enzyme activity. An enzyme's name is often derived from its substrate or the chemical reaction it catalyzes, with the word ending in -ase.

  3. Cytochrome P450 - Wikipedia

    en.wikipedia.org/wiki/Cytochrome_P450

    Depending on the substrate and enzyme involved, P450 enzymes can catalyze any of a wide variety of reactions. A hypothetical hydroxylation is illustrated. After the hydroxylated product has been released from the active site, the enzyme returns to its original state, with a water molecule returning to occupy the distal coordination position of ...

  4. Glucose-6-phosphate dehydrogenase - Wikipedia

    en.wikipedia.org/wiki/Glucose-6-phosphate_de...

    More than 40 severe class I mutations involve mutations near the structural site, thus affecting the long term stability of these enzymes in the body, ultimately resulting in G6PD deficiency. [13] For example, two severe class I mutations, G488S and G488V, drastically increase the dissociation constant between NADP + and the structural site by ...

  5. Metabolism - Wikipedia

    en.wikipedia.org/wiki/Metabolism

    Metabolism (/ m ə ˈ t æ b ə l ɪ z ə m /, from Greek: μεταβολή metabolē, "change") is the set of life-sustaining chemical reactions in organisms.The three main functions of metabolism are: the conversion of the energy in food to energy available to run cellular processes; the conversion of food to building blocks of proteins, lipids, nucleic acids, and some carbohydrates; and the ...

  6. Leucyl aminopeptidase - Wikipedia

    en.wikipedia.org/wiki/Leucyl_aminopeptidase

    Leucyl aminopeptidases (EC 3.4.11.1, leucine aminopeptidase, LAPs, leucyl peptidase, peptidase S, cytosol aminopeptidase, cathepsin III, L-leucine aminopeptidase, leucinaminopeptidase, leucinamide aminopeptidase, FTBL proteins, proteinates FTBL, aminopeptidase II, aminopeptidase III, aminopeptidase I) are enzymes that preferentially catalyze the hydrolysis of leucine residues at the N-terminus ...

  7. Lead(II) nitrate - Wikipedia

    en.wikipedia.org/wiki/Lead(II)_nitrate

    Lead(II) is a hard acceptor; it forms stronger complexes with nitrogen and oxygen electron-donating ligands. For example, combining lead nitrate and pentaethylene glycol (shortened to EO5 in the referenced paper) in a solution of acetonitrile and methanol followed by slow evaporation produced the compound [Pb(NO 3) 2 EO5]. [19]

  8. Lead poisoning - Wikipedia

    en.wikipedia.org/wiki/Lead_poisoning

    [190] [191] [192] Lead also inhibits the enzyme ferrochelatase, another enzyme involved in the formation of heme. [26] [193] Ferrochelatase catalyzes the joining of protoporphyrin and Fe 2+ to form heme. [26] [33] Lead's interference with heme synthesis results in production of zinc protoporphyrin and the development of anemia. [194]

  9. Lead - Wikipedia

    en.wikipedia.org/wiki/Lead

    Lead (/ l ɛ d /) is a chemical element; it has symbol Pb (from Latin plumbum) and atomic number 82. It is a heavy metal that is denser than most common materials. Lead is soft and malleable, and also has a relatively low melting point. When freshly cut, lead is a shiny gray with a hint of blue. It tarnishes to a dull gray color when exposed to ...