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Prolyl-3-hydroxylase

FIGURE 6.17 Hydroxylation of proUne residnes is catalyzed by prolyl hydroxylase. The reaction requires -ketoglntarate and ascorbic acid (vitamin C). [Pg.176]

Scurvy results from a dietary vitamin C deficiency and involves the inability to form collagen fibrils properly. This is the result of reduced activity of prolyl hydroxylase, which is vitamin C-dependent, as previously noted. Scurvy leads to lesions in the skin and blood vessels, and, in its advanced stages, it can lead to grotesque disfiguration and eventual death. Although rare in the modern world, it was a disease well known to sea-faring explorers in earlier times who did not appreciate the importance of fresh fruits and vegetables in the diet. [Pg.178]

Very few post-translational modifications have been found on tropoelastin. However, hydroxylation of 25% of the proline residues is observed [10]. The enzymatic modification of proline to hydroxyproline (Hyp) is performed by prolyl hydroxylase [11]. The purpose of this hydroxylation remains unclear and it is even proposed that Hyps in tropoelastin are a by-product of collagen hydroxylation as this occurs in the same cellular compartment [8]. [Pg.74]

Figure 28-11. The prolyl hydroxylase reaction. The substrate is a proline-rich peptide. During the course of the reaction, molecular oxygen is incorporated into both succinate and proline. Lysyl hydroxylase catalyzes an analogous reaction. Figure 28-11. The prolyl hydroxylase reaction. The substrate is a proline-rich peptide. During the course of the reaction, molecular oxygen is incorporated into both succinate and proline. Lysyl hydroxylase catalyzes an analogous reaction.
Mineral dust-induced ROMs contributes to pulmonary fibrosis, malignancy, hypersensitivity and emphysema (Doelman etctl., 1990 Kamp etui., 1992). The involvement of ROMs in pulmonary fibrotic reactions is indicated by the participation of PMN oxidants in the autoactivation of latent coUagenase (Weiss et al., 1985). Prolyl hydroxylase, a key enzyme in collagen fibril formation, has been shown to be dependent on the reaction of superoxide with prolyl residues (Myllyla et al., 1979). [Pg.250]

P. Frohna, S. Milwee, J. Pinkett, T. Lee, K. Moore-Perry, J. Chou, and R. H. Ellison in Results from a Randomized, Single-Blind, Placebo-Controlled Trial of FG-4592, a Novel Hypoxia Inducible Factor Prolyl Hydroxylase Inhibitor, in CKD Anemia, Vol. 2007, American Society of Nephrology Renal Week, San Francisco, November 2-5, 2007, Abstract SU-PO806, as abstracted in N. Agarwal and J. T. Prchal, Semin. Hematol., 2008, 45, 267. [Pg.141]

Nakayama, K., et al., Siah2 regulates stability of prolyl-hydroxylases, controls HlFla abundance and modulates physiological responses to hypoxia. Cell, 2004, 117(7), 941-52. [Pg.91]

Answer E. The patient has many signs of scurvy from a vitamin C deficiency. The diet, which contains no fruits or vegetables, provides little vitamin C, Prolyl hydroxylase requires vitamin C, and in the absence of hydroxylation, the collagen a-chains do not form stable, mature collagen. The anemia may be due to poor iron absorption in the absence of ascorbate. [Pg.152]

So what does this magical molecule do Actually, it does two things, one rather more crystalline clear than the other. The crystal clear thing that ascorbic acid does is act as coenzyme for an enzyme known as prolyl hydroxylase. This enzyme catalyzes the conversion of the amino acid proline to hydroxyproline, a major, if exotic, amino acid in the structural protein collagen ... [Pg.197]

Collagen synthesized in the absence of ascorbic acid (i.e. without hydroxyproline) cannot form its usual stable structure. Collagen is a major component of the structural and connective tissues of the body bone, cartilage, tendons, ligaments, teeth, and skin. Small wonder that things sort of fall apart in the absence of adequate ascorbic acid to support the activity of prolyl hydroxylase. [Pg.197]

Vitamin C, ascorbic acid, is a coenzyme for the enzyme prolyl hydroxylase. The action of this enzyme is critical for the formation of normal collagen, a key component of structural and connective tissues. [Pg.205]

Ascorbic acid a coenzyme for prolyl hydroxylase the preventive and cure for scurvy also known as vitamin C. [Pg.388]


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HIF prolyl hydroxylases

Hypoxia prolyl 4 hydroxylases

Hypoxia-inducible transcription factor, prolyl hydroxylase

Prolyl hydroxylase domain

Prolyl hydroxylase enzymes

Prolyl hydroxylase reaction

Prolyl hydroxylases

Prolyl-4-hydroxylase inhibition

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