title: A steady-state kinetic analysis of the prolyl-4-hydroxylase mechanism.
abstract: Published kinetic data by Kivirikko, et al. on the prolyl-4-hydroxylase reaction have been re-evaluated using the overall steady-state velocity equation in the forward and reverse directions for an ordered ter ter kinetic mechanism. Qualitatively, the published data for prolyl-4-hydroxylase appear to fit the predicted patterns for this kinetic mechanism. More kinetic data are needed to confirm these results and to quantitate the kinetic parameters but, tentatively, the order of substrate addition would appear to be alpha-ketoglutarate, oxygen, and peptide; and the order of product release would be hydroxylated peptide (or collagen), carbon dioxide, and succinate.
mesh_terms: D002245:Carbon Dioxide / Q000494:pharmacology; D003094:Collagen / Q000494:pharmacology; D007700:Kinetics; D008433:Mathematics; D011393:Procollagen-Proline Dioxygenase / Q000378:metabolism*; D013386:Succinates / Q000494:pharmacology; D019802:Succinic Acid
chemical_list: D013386:Succinates; D002245:Carbon Dioxide; D003094:Collagen; D019802:Succinic Acid; D011393:Procollagen-Proline Dioxygenase