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  2. Alcohol dehydrogenase - Wikipedia

    en.wikipedia.org/wiki/Alcohol_dehydrogenase

    The main alcohol dehydrogenase in yeast is larger than the human one, consisting of four rather than just two subunits. It also contains zinc at its catalytic site. Together with the zinc-containing alcohol dehydrogenases of animals and humans, these enzymes from yeasts and many bacteria form the family of "long-chain"-alcohol dehydrogenases.

  3. Trypsinization - Wikipedia

    en.wikipedia.org/wiki/Trypsinization

    Trypsinization is the process of cell dissociation using trypsin, a proteolytic enzyme which breaks down proteins, to dissociate adherent cells from the vessel in which they are being cultured. When added to cell culture, trypsin breaks down the proteins that enable the cells to adhere to the vessel.

  4. Phosphoribosylanthranilate isomerase - Wikipedia

    en.wikipedia.org/wiki/Phosphoribosylanthranilate...

    In enzymology, a phosphoribosylanthranilate isomerase (PRAI) (EC 5.3.1.24) is an enzyme that catalyzes the third step of the synthesis of the amino acid tryptophan. [1]This enzyme participates in the phenylalanine, tyrosine and tryptophan biosynthesis pathway, also known as the aromatic amino acid biosynthesis pathway

  5. Tryptophan - Wikipedia

    en.wikipedia.org/wiki/Tryptophan

    Tryptophan ball and stick model spinning. Tryptophan (symbol Trp or W) [3] is an α-amino acid that is used in the biosynthesis of proteins.Tryptophan contains an α-amino group, an α-carboxylic acid group, and a side chain indole, making it a polar molecule with a non-polar aromatic beta carbon substituent.

  6. trp operon - Wikipedia

    en.wikipedia.org/wiki/Trp_operon

    Structure of the trp operon. The trp operon is a group of genes that are transcribed together, encoding the enzymes that produce the amino acid tryptophan in bacteria. The trp operon was first characterized in Escherichia coli, and it has since been discovered in many other bacteria. [1]

  7. Tryptophan synthase - Wikipedia

    en.wikipedia.org/wiki/Tryptophan_synthase

    Tryptophan synthase or tryptophan synthetase is an enzyme (EC 4.2.1.20) that catalyzes the final two steps in the biosynthesis of tryptophan. [1] [2] It is commonly found in Eubacteria, [3] Archaebacteria, [4] Protista, [5] Fungi, [6] and Plantae. [7] However, it is absent from Animalia. [8] It is typically found as an α2β2 tetramer.

  8. Shikimate pathway - Wikipedia

    en.wikipedia.org/wiki/Shikimate_pathway

    The fifth enzyme involved is the shikimate kinase, an enzyme that catalyzes the ATP-dependent phosphorylation of shikimate to form shikimate 3-phosphate (shown in the figure below). [ 1 ] [ 2 ] Shikimate 3-phosphate is then coupled with phosphoenol pyruvate to give 5-enolpyruvylshikimate-3-phosphate via the enzyme 5-enolpyruvylshikimate-3 ...

  9. Trypsin - Wikipedia

    en.wikipedia.org/wiki/Trypsin

    Trypsin is an enzyme in the first section of the small intestine that starts the digestion of protein molecules by cutting long chains of amino acids into smaller pieces. It is a serine protease from the PA clan superfamily, found in the digestive system of many vertebrates, where it hydrolyzes proteins.