Hydroxylysine Explained

Hydroxylysine (Hyl) is an amino acid with the molecular formula C6H14N2O3. It was first discovered in 1921 by Donald Van Slyke as the 5-hydroxylysine form.[1] It arises from a post-translational hydroxy modification of lysine. It is most widely known as a component of collagen.[2]

It is biosynthesized from lysine via oxidation by lysyl hydroxylase enzymes. The most common form is the (5R) stereoisomer found in collagen. However, the enzyme JMJD6 has recently been shown to be a lysyl hydroxylase which modifies an RNA splicing factor producing the (5S) stereoisomer. Additionally, in E. coli, there has been at least one lysine N-hydroxylase enzyme identified, named IucD.[3]

References

  1. Van Slyke . DD. . Hiller . A. . An Unidentified Base among the Hydrolytic Products of Gelatin. . Proc Natl Acad Sci U S A . 7 . 7 . 185–6 . Jul 1921 . 10.1073/pnas.7.7.185. 16586836 . 1084845. 1921PNAS....7..185V . free .
  2. http://herkules.oulu.fi/isbn9514267990/html/x319.html Hydroxylysine
  3. de Lorenzo . V.. Aerobactin biosynthesis and transport genes of plasmid ColV-K30 in Escherichia coli K-12. . J. Bacteriol. . 165 . 2 . 570–8 . Feb 1986 . 2935523 . 214457. etal. 10.1128/jb.165.2.570-578.1986.