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Hydroxyproline is a major component of the protein collagen, [3] comprising roughly 13.5% of mammalian collagen. Hydroxyproline and proline play key roles for collagen stability. [4] They permit the sharp twisting of the collagen helix. [5]
Furthermore, proline is rarely found in α and β structures as it would reduce the stability of such structures, because its side chain α-nitrogen can only form one nitrogen bond. Additionally, proline is the only amino acid that does not form a red-purple colour when developed by spraying with ninhydrin for uses in chromatography. Proline ...
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.
Procollagen-proline dioxygenase, commonly known as prolyl hydroxylase, is a member of the class of enzymes known as alpha-ketoglutarate-dependent hydroxylases. These enzymes catalyze the incorporation of oxygen into organic substrates through a mechanism that requires alpha-Ketoglutaric acid , Fe 2+ , and ascorbate .
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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".
Sometimes our fur babies make demands about what they want, and like kids, won't stop pestering us until they get what they want. If you're like my family, you probably give in to them ...