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. [electronic resource]
- The Journal of biological chemistry Dec 2004
- 55051-9 p. digital
Publication Type: Journal Article; Research Support, Non-U.S. Gov't
0021-9258
10.1074/jbc.M410287200 doi
Alanine--chemistry Amino Acid Motifs Animals Azetidinecarboxylic Acid--chemistry Baculoviridae--metabolism Cell Line Chromatography, Liquid Culture Media, Serum-Free--pharmacology Glutamic Acid--chemistry Humans Hydroxylation Hypoxia-Inducible Factor 1, alpha Subunit Insecta Ketoglutaric Acids--chemistry Kinetics Leucine--chemistry Mass Spectrometry Methionine--chemistry Models, Chemical Peptides--chemistry Procollagen-Proline Dioxygenase--chemistry Proline--analogs & derivatives Protein Structure, Tertiary Substrate Specificity Time Factors Transcription Factors--chemistry