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  2. Hydroxyproline - Wikipedia

    en.wikipedia.org/wiki/Hydroxyproline

    Hydroxyproline is produced by hydroxylation of the amino acid proline by the enzyme prolyl hydroxylase following protein synthesis (as a post-translational modification). The enzyme catalyzed reaction takes place in the lumen of the endoplasmic reticulum. Although it is not directly incorporated into proteins, hydroxyproline comprises roughly 4 ...

  3. Systemin - Wikipedia

    en.wikipedia.org/wiki/Systemin

    In 2001, biologically active hydroxyproline-rich glycopeptides were isolated from tobacco which activated the production of protease inhibitors in a similar way to systemin in tomatoes. [1] Although they are structurally unrelated to systemins, their similar function resulted in them being named hydroxyproline-rich systemins (HypSys).

  4. Procollagen-proline dioxygenase - Wikipedia

    en.wikipedia.org/wiki/Procollagen-proline_di...

    Procollagen-proline dioxygenase catalyzes the following reaction: L-proline + alpha-ketoglutaric acid + O 2 → (2S, 4R)-4-hydroxyproline + succinate + CO 2. The mechanism for the reaction is similar to that of other dioxygenases, and occurs in two distinct stages: [3] In the first, a highly reactive Fe(IV)=O species is produced.

  5. Proline - Wikipedia

    en.wikipedia.org/wiki/Proline

    Hence, the hydroxylation of proline is a critical biochemical process for maintaining the connective tissue of higher organisms. Severe diseases such as scurvy can result from defects in this hydroxylation, e.g., mutations in the enzyme prolyl hydroxylase or lack of the necessary ascorbate (vitamin C) cofactor.

  6. Hyperprolinemia - Wikipedia

    en.wikipedia.org/wiki/Hyperprolinemia

    Hyperprolinemia type II results in proline levels in the blood between 10 and 15 times higher than normal, and high levels of a related compound called pyrroline-5-carboxylate. This rare form of the disorder may appear benign at times, [ 2 ] but often involves seizures, convulsions, and intellectual disability.

  7. PEPD - Wikipedia

    en.wikipedia.org/wiki/PEPD

    Collagen, the most prevalent protein in the human body, is necessary for maintaining strong connective tissues, cellular proliferation, and wound healing, among other functions. [17] As collagen is degraded, dipeptides are released as a byproduct. Serum prolidase absorbs and digests these byproducts so they can be reused in collagen production. [8]

  8. Prolidase deficiency - Wikipedia

    en.wikipedia.org/wiki/Prolidase_deficiency

    Collagen is a structural protein found i.a. in bone, skin and connective tissues that is broken down into iminodipeptides at the end of its lifecycle. Of these dipeptides, those containing C-terminal proline or hydroxyproline would normally be broken down further by the enzyme Prolidase, recovering and thus recycling the constituent amino acids.

  9. Proline oxidase - Wikipedia

    en.wikipedia.org/wiki/Proline_oxidase

    Proline oxidase, or proline dehydrogenase, functions as the initiator of the proline cycle. Proline metabolism is especially important in nutrient stress because proline is readily available from the breakdown of extracellular matrix (ECM), and the degradation of proline through the proline cycle initiated by proline oxidase (PRODH), a mitochondrial inner membrane enzyme, can generate ATP.