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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. Some snail poisons, conotoxins, contain hydroxyproline, but lack collagen-like sequences. [2]
The amino acid composition of collagen is atypical for proteins, particularly with respect to its high hydroxyproline content. The most common motifs in collagen's amino acid sequence are glycine-proline-X and glycine-X-hydroxyproline, where X is any amino acid other than glycine, proline or hydroxyproline.
Extensin hydroxyproline is uniquely glycosylated with short chains of L-arabinose [8] that further rigidify [9] and increase hydrophilicity. Generally the serine has a single galactose attached. Generally the serine has a single galactose attached.
In enzymology, a 4-hydroxyproline epimerase (EC 5.1.1.8) is an enzyme that catalyzes the chemical reaction trans -4-hydroxy-L-proline ⇌ {\displaystyle \rightleftharpoons } cis -4-hydroxy-D-proline Hence, this enzyme has one substrate , trans-4-hydroxy-L-proline , and one product , cis-4-hydroxy-D-proline .
"4-Hydroxyproline, or hydroxyproline (C5H9O3N), is an uncommon amino acid" "Hydroxyproline is a major component of the protein collagen" and under Collagen: "Collagen is the main protein of connective tissue in animals and the most abundant protein in mammals,[1] making up about 25% of the whole-body protein content."
In 1954, Ramachandran & Kartha (13, 14) advanced a structure for the collagen triple helix on the basis of fiber diffraction data. It consists of a triple helix made of the repetitious amino acid sequence glycine-X-Y, where X and Y are frequently proline or hydroxyproline. [2] [3] Collagen folded into a triple helix is known as tropocollagen.
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In nature, proline, hydroxyproline, pipecolic acid and sarcosine are well-known secondary amino acids. Proline is the only proteinogenic secondary amino acids. Other secondary amino acids are non-proteinogenic amino acids. In protein, hydroxyproline is incorporated into protein by hydroxylation of proline.
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