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Collagen prolyl 4-hydroxylase tetramers and dimers show identical decreases in Km values for peptide substrates with increasing chain length: mutation of one of the two catalytic sites in the tetramer inactivates the enzyme by more than half.
Kukkola L, Koivunen P, Pakkanen O, Page AP, Myllyharju J. Kukkola L, et al. Among authors: koivunen p. J Biol Chem. 2004 Apr 30;279(18):18656-61. doi: 10.1074/jbc.M401514200. Epub 2004 Feb 25. J Biol Chem. 2004. PMID: 14985345 Free article.
Many amino acid substitutions in a hypoxia-inducible transcription factor (HIF)-1alpha-like peptide cause only minor changes in its hydroxylation by the HIF prolyl 4-hydroxylases: substitution of 3,4-dehydroproline or azetidine-2-carboxylic acid for the proline leads to a high rate of uncoupled 2-oxoglutarate decarboxylation.
Li D, Hirsilä M, Koivunen P, Brenner MC, Xu L, Yang C, Kivirikko KI, Myllyharju J. Li D, et al. Among authors: koivunen p. J Biol Chem. 2004 Dec 31;279(53):55051-9. doi: 10.1074/jbc.M410287200. Epub 2004 Oct 12. J Biol Chem. 2004. PMID: 15485863 Free article.
210 results