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27, 29-33> [73]) [73] P 4-hydroxyproline containing peptide + succinate + CO2 <27, 29-33> [73] S Asp-Leu-Asp-Leu-Glu-Met-Leu-Ala-Pro-Tyr-Ile-Pro-Met-Asp-Asp-AspPhe-Gln-Leu + 2-oxoglutarate + O2 <27, 29-33> (<27, 29-33> peptide representing hypoxia-inducible transcription factor a sequences [73]) (Reversibility: ? 2 Procollagen-proline dioxygenase S Glu-Gly-(Pro-Pro-Gly)5 + 2-oxoglutarate + O2 <1> (Reversibility: ? <1> [37]) [37] P 4-hydroxyproline containing peptide + succinate + CO2 <1> [37] S Gly-Pro8 + 2-oxoglutarate + O2 <10> (<10> 96% relative activity with respect to poly(L-proline) of MW 2000 [42, 43]) (Reversibility: ?

1> [37]) [37] P 4-hydroxyproline containing peptide + succinate + CO2 <1> [37] S Asp-Ala-Leu-Thr-Leu-Leu-Ala-Pro-Ala-Ala-Gly-Asp-Thr-Ile-Ile-Ser-LeuPhe-Gly + 2-oxoglutarate + O2 <27, 29-33> (<27, 29-33> peptide representing hypoxia-inducible transcription factor a sequences [73]) (Reversibility: ? <27, 29-33> [73]) [73] P 4-hydroxyproline containing peptide + succinate + CO2 <27, 29-33> [73] S Asp-Leu-Asp-Leu-Glu-Met-Leu-Ala-Pro-Tyr-Ile-Pro-Met-Asp-Asp-AspPhe-Gln-Leu + 2-oxoglutarate + O2 <27, 29-33> (<27, 29-33> peptide representing hypoxia-inducible transcription factor a sequences [73]) (Reversibility: ?

Additionally the sequence, the conformation and the peptide chain length influence the rate of hydroxylation [1]; <1, 3> the presence of 2-oxoglutarate is an absolute and highly specific requirement, the formation of 4-hydroxyproline is accompanied by a stoichiometric decarboxylation of 2-oxoglutarate, the oxygen of the hydroxyl group is derived from molecular oxygen, the other atom of the O2 molecule being incorporated into the succinate, the activated form of oxygen is probably superoxide [1,9]; <1> chelation to the enzyme-bound metal ion is important for proper binding of the substrate 2-oxoglutarate [5]; <1> synthetic peptides [12]) (Reversibility: ?

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