Differences in collagen prolyl 4-hydroxylase assembly between two Caenorhabditis nematode species despite high amino acid sequence identity of the enzyme subunits.

@article{Winter2007DifferencesIC,
  title={Differences in collagen prolyl 4-hydroxylase assembly between two Caenorhabditis nematode species despite high amino acid sequence identity of the enzyme subunits.},
  author={A. J. De Winter and Katriina Keskiaho and Liisa Kukkola and G Mccormack and Marie-Anne F{\'e}lix and Johanna Myllyharju and Antony P. Page},
  journal={Matrix biology : journal of the International Society for Matrix Biology},
  year={2007},
  volume={26 5},
  pages={382-95}
}
The collagen prolyl 4-hydroxylases (P4Hs) are essential for proper extracellular matrix formation in multicellular organisms. The vertebrate enzymes are alpha(2)beta(2) tetramers, in which the beta subunits are identical to protein disulfide isomerase (PDI). Unique P4H forms have been shown to assemble from the Caenorhabditis elegans catalytic alpha subunit isoforms PHY-1 and PHY-2 and the beta subunit PDI-2. A mixed PHY-1/PHY-2/(PDI-2)(2) tetramer is the major form, while PHY-1/PDI-2 and PHY-2… CONTINUE READING