McNeill, LA and Hewitson, KS and Gleadle, JM and Horsfall, LE and Oldham, NJ and Maxwell, PH and Pugh, CW and Ratcliffe, PJ and Schofield, CJ (2002) The use of dioxygen by HIF prolyl hydroxylase (PHD1). BIOORG MED CHEM LETT , 12 (12) 1547 - 1550.
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Abstract
The hypoxic response in animals is mediated by hydroxylation of proline residues in the a-subunit of hypoxia inducible factor (HIF). Hydroxylation is catalysed by prolyl-4-hydroxylases (PHD isozymes in humans) which are iron(II) and 2-oxoglutarate dependent oxygenases. Mutation of the arginine proposed to bind 2-oxoglutarate and of the 2His-1-carboxylate iron(II) binding motif in PHD 1 dramatically reduces its activity. The source of the oxygen of the product alcohol is (>95%) dioxygen. (C) 2002 Published by Elsevier Science.
| Type: | Article |
|---|---|
| Title: | The use of dioxygen by HIF prolyl hydroxylase (PHD1) |
| Keywords: | HYPOXIA-INDUCIBLE FACTOR-1, PROLINE HYDROXYLATION, CLAVAMINATE SYNTHASE, IRON-BINDING, ACTIVE-SITE, C-SYNTHASE, MUTAGENESIS, FAMILY, OXYGEN, ALPHA |
| UCL classification: | UCL > School of Life and Medical Sciences > Faculty of Medical Sciences > Medicine (Division of) |
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