Characterization of a novel Caenorhabditis elegans prolyl 4-hydroxylase with a unique substrate specificity and restricted expression in the pharynx and excretory duct.

@article{Keskiaho2008CharacterizationOA,
  title={Characterization of a novel Caenorhabditis elegans prolyl 4-hydroxylase with a unique substrate specificity and restricted expression in the pharynx and excretory duct.},
  author={Katriina Keskiaho and Liisa Kukkola and Antony P. Page and A. J. De Winter and Jussi T. Vuoristo and Raija T. Sormunen and Ritva Nissi and P{\"a}ivi H Riihimaa and Johanna Myllyharju},
  journal={The Journal of biological chemistry},
  year={2008},
  volume={283 16},
  pages={10679-89}
}
Collagen prolyl 4-hydroxylases (C-P4Hs) have a critical role in collagen synthesis, since 4-hydroxyproline residues are necessary for folding of the triple-helical molecules. Vertebrate C-P4Hs are alpha(2)beta(2) tetramers in which the beta subunit is identical to protein-disulfide isomerase (PDI). Three isoforms of the catalytic alpha subunit, PHY-1, PHY-2, and PHY-3, have been characterized from Caenorhabditis elegans, PHY-1 and PHY-2 being responsible for the hydroxylation of cuticle… CONTINUE READING