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The most obvious, first effects (gingival and hair problems) of absence of ascorbic acid in humans come from the resulting defect in hydroxylation of proline residues of collagen, with reduced stability of the collagen molecule, causing scurvy. Increased serum and urine levels of hydroxyproline have also been demonstrated in Paget's disease. [10]
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.
The amino acid composition of collagen is atypical for proteins, particularly with respect to its high hydroxyproline content. The most common motifs in the amino acid sequence of collagen are glycine-proline-X and glycine-X-hydroxyproline, where X is any amino acid other than glycine, proline or hydroxyproline. The average amino acid ...
The incorporation of these nonstandard amino acids is rare. For example, 25 human proteins include selenocysteine in their primary structure, [70] and the structurally characterized enzymes (selenoenzymes) employ selenocysteine as the catalytic moiety in their active sites. [71] Pyrrolysine and selenocysteine are encoded via variant codons.
2 Human genes. 3 References. ... "Hydroxyproline metabolism. III. Enzymatic synthesis of hydroxyproline from Delta1-pyrroline-3-hydroxy-5-carboxylate".
In whole blood (g/cm 3) In plasma or serum (g/cm 3) Water: Solvent 0.81-0.86 0.93-0.95 Acetoacetate: Produced in liver 8-40 × 10 −7: 4-43 × 10 −7: Acetone: product of bodyfat breakdown 3-20 × 10 −6: Acetylcholine: Neurotransmitter of the parasympathetic nervous system: 6.6-8.2 × 10 −8: Adenosine triphosphate: Energy storage total 3. ...
Prolidase deficiency generally becomes evident during infancy, but initial symptoms can first manifest anytime from birth to young adulthood. The condition results in a very diverse set symptoms, [3] the severity of which can vary significantly between patients, depending on the degree to which prolidase activity is hampered by the individual underlying mutation(s) in each case.
Serum prolidase is a highly necessary enzyme in the human body. Through its many functions, most notably collagen recycling, prolidase is widely used in the overall metabolism of humans. The reaction pathway of this enzyme is key in regulating the synthesis and degradation of collagen, a vital protein necessary for multiple aspects of the body.