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  2. Hydroxyproline - Wikipedia

    en.wikipedia.org/wiki/Hydroxyproline

    Hydroxyproline is found in few proteins other than collagen. For this reason, hydroxyproline content has been used as an indicator to determine collagen and/or gelatin amount. However, the mammalian proteins elastin and argonaute 2 have collagen-like domains in which hydroxyproline is formed.

  3. 3-Hydroxypropionate bicycle - Wikipedia

    en.wikipedia.org/wiki/3-Hydroxypropionate_bicycle

    The 3-hydroxypropionate bicycle, also known as the 3-hydroxypropionate pathway, is a process that allows some bacteria to generate 3-hydroxypropionate using carbon dioxide. [2] It is divided into two parts or reactions.

  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. O-linked glycosylation - Wikipedia

    en.wikipedia.org/wiki/O-linked_glycosylation

    This is important in their protective function as it lubricates the tracts so bacteria cannot bind and infect the body. Changes in mucins are important in numerous diseases, including cancer and inflammatory bowel disease. Absence of O-glycans on mucin proteins changes their 3D shape dramatically and often prevents correct function. [1] [9]

  7. Glycosylation - Wikipedia

    en.wikipedia.org/wiki/Glycosylation

    The N-linked glycosylation process occurs in eukaryotes in the lumen of the endoplasmic reticulum and widely in archaea, but very rarely in bacteria. In addition to their function in protein folding and cellular attachment, the N-linked glycans of a protein can modulate a protein's function, in some cases acting as an on/off switch.

  8. 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.

  9. Pyrroline-5-carboxylate reductase - Wikipedia

    en.wikipedia.org/wiki/Pyrroline-5-carboxylate...

    Adams E; Goldstone A (1960). "Hydroxyproline metabolism. III. Enzymatic synthesis of hydroxyproline from Delta1-pyrroline-3-hydroxy-5-carboxylate".