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Hence, this enzyme has one substrate, trans-4-hydroxy-L-proline, and one product, cis-4-hydroxy-D-proline. This enzyme belongs to the family of isomerases, specifically those racemases and epimerases acting on amino acids and derivatives. The systematic name of this enzyme class is 4-hydroxyproline 2-epimerase.
Other hydroxyprolines also exist in nature. The most notable ones are 2,3-cis-, 3,4-trans-, and 3,4-dihydroxyproline, which occurs in diatom cell walls [12] and are postulated to have a role in silica deposition. Hydroxyproline is also found in the walls of oomycetes, fungus-like protists related to diatoms.
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.
Proline (symbol Pro or P) [4] is an organic acid classed as a proteinogenic amino acid (used in the biosynthesis of proteins), although it does not contain the amino group-NH 2 but is rather a secondary amine .
4-Hydroxynonenal, or 4-hydroxy-2E-nonenal or 4-hydroxy-2-nonenal or 4-HNE or HNE, (C 9 H 16 O 2), is an α,β-unsaturated hydroxyalkenal that is produced by lipid peroxidation in cells. 4-HNE is the primary α,β-unsaturated hydroxyalkenal formed in this process. It is a colorless oil.
In enzymology, a proline racemase (EC 5.1.1.4) is an enzyme that catalyzes the chemical reaction. L-proline D-proline. Hence, this enzyme has two substrates, L- and D-proline, and two products, D- and L- proline. This enzyme belongs to the family of proline racemases acting on free amino acids.
Ramaswamy SG (1983). "Conversion of 3-hydroxyproline to proline in the rat requires reduced pyridine-nucleotides". Fed. Proc. 42: 2232. Visser WF, Verhoeven-Duif NM, de Koning TJ (June 2012). "Identification of a human trans-3-hydroxy-L-proline dehydratase, the first characterized member of a novel family of proline racemase-like enzymes".
They also found that it retained its highly selective nature, capable of receiving mostly D-enantiomers after mutation, with yields in excess of 95%. [5] A heat-stable variant of D-amino acid dehydrogenase was found in the bacterium Rhodothermus marinus JCM9785. This variant is involved in the catabolism of trans-4-hydroxy-L-proline. [11]