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. (Jul 1921). "An Unidentified Base among the Hydrolytic Products of Gelatin". Proc Natl Acad Sci U S A. 7 (7): 185–6. Bibcode:1921PNAS....7..185V. doi:10.1073/pnas.7.7.185. PMC 1084845. PMID 16586836.
  2. ^ Hydroxylysine at University of Oulu
  3. ^ de Lorenzo, V.; et al. (Feb 1986). "Aerobactin biosynthesis and transport genes of plasmid ColV-K30 in Escherichia coli K-12". J. Bacteriol. 165 (2): 570–8. doi:10.1128/jb.165.2.570-578.1986. PMC 214457. PMID 2935523.

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