Ontology highlight
ABSTRACT:
SUBMITTER: Pinkas DM
PROVIDER: S-EPMC3337207 | biostudies-literature | 2011 Apr
REPOSITORIES: biostudies-literature
Pinkas Daniel M DM Ding Sheng S Raines Ronald T RT Barron Annelise E AE
ACS chemical biology 20110114 4
Prolyl 4-hydroxylases are ascorbate-dependent oxygenases that play key roles in a variety of eukaryotic biological processes including oxygen sensing, siRNA regulation, and collagen folding. They perform their functions by catalyzing the post-translational hydroxylation of specific proline residues on target proteins to form (2S,4R)-4-hydroxyproline. Thus far, the study of these post-translational modifications has been limited by the lack of a prokaryotic recombinant expression system for produ ...[more]