Evidence for the slow reaction of hypoxia-inducible factor prolyl hydroxylase 2 with oxygen

• Published in: The FEBS journal Vol. 277; no. 19; pp. 4089 - 4099
• Main Authors: Flashman, Emily, Hoffart, Lee M, Hamed, Refaat B, Bollinger Jr, J. Martin, Krebs, Carsten, Schofield, Christopher J
• Format: Journal Article
• Language: English
• Published: Oxford, UK Oxford, UK : Blackwell Publishing Ltd 01.10.2010; Blackwell Publishing Ltd
• Subjects: 2-oxoglutarate; Amino Acid Sequence; Catalysis; Humans; Hypoxia; hypoxia-inducible factor; Hypoxia-Inducible Factor 1, alpha Subunit - chemistry; Hypoxia-Inducible Factor 1, alpha Subunit - metabolism; Kinetics; Magnetic Resonance Spectroscopy; Molecular Sequence Data; Oxygen; oxygenase; Peptides - metabolism; procollagen-proline dioxygenase; Procollagen-Proline Dioxygenase - chemistry; Procollagen-Proline Dioxygenase - genetics; Procollagen-Proline Dioxygenase - metabolism; prolyl hydroxylase; Recombinant Proteins - chemistry; Recombinant Proteins - metabolism; spectroscopy; Spectroscopy, Mossbauer; Substrate Specificity

The response of animals to hypoxia is mediated by the hypoxia-inducible transcription factor. Human hypoxia-inducible factor is regulated by four Fe(II)- and 2-oxoglutarate-dependent oxygenases: prolyl hydroxylase domain enzymes 1-3 catalyse hydroxylation of two prolyl-residues in hypoxia-inducible...