Characterization of the human prolyl 4-hydroxylase tetramer and its multifunctional protein disulfide-isomerase subunit synthesized in a baculovirus expression system.

@article{Vuori1992CharacterizationOT,
  title={Characterization of the human prolyl 4-hydroxylase tetramer and its multifunctional protein disulfide-isomerase subunit synthesized in a baculovirus expression system.},
  author={Kristiina Vuori and Taina Pihlajaniemi and Minna Marttila and Kari I. Kivirikko},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={1992},
  volume={89 16},
  pages={7467-70}
}
Prolyl 4-hydroxylase (EC 1.14.11.2), an alpha 2 beta 2 tetramer, catalyzes the posttranslational formation of 4-hydroxyproline in collagens. The enzyme can easily be dissociated into its subunits, but all attempts to associate a tetramer from the dissociated subunits in vitro have been unsuccessful. Molecular cloning of the catalytically important alpha subunit has identified two types of cDNA clone due to mutually exclusive alternative splicing. The beta subunit is a highly unusual… CONTINUE READING