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The use of dioxygen by HIF prolyl hydroxylase (PHD1)

McNeill, LA; Hewitson, KS; Gleadle, JM; Horsfall, LE; Oldham, NJ; Maxwell, PH; Pugh, CW; (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
UCL > School of Life and Medical Sciences > Faculty of Medical Sciences
UCL > School of Life and Medical Sciences > Faculty of Medical Sciences > Medicine (Division of)
URI: http://discovery.ucl.ac.uk/id/eprint/128691
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