The first successful expression of recombinant human C-P4H in E. coli was reported
almost simultaneously by us (article I of this thesis) and another group (Kersteen et al.
2004), the articles being published online in December and November 2004, respectively.
Kersteen et al. generated a bicistronic vector with both subunits under control of the same
T7lac promoter and used E. coli Origami cells for expression. A related but structurally
different enzyme, a Dactylosporangium proline 4-hydroxylase, has been also successfully
expressed in E. coli with the aim to use it in industrial micorobial production of trans-4-
hydroxy-L-proline from free L-proline (Shibasaki et al. 2000a). In contrast to the human
C-P4H, the Dactylosporangium proline 4-hydroxylase is a small monomeric 31-kDa
polypeptide and does not hydroxylate prolines in peptide linkages (Shibasaki et al. 1999).