Danica S. Butler

Structural studies of substrate and product complexes of 5-aminolaevulinic acid dehydratase from humans, Escherichia coli and the hyperthermophile Pyrobaculum calidifontis Acta Crystallographica Section D Structural Biology

N.L. Mills-Davies, Danica S. Butler, Ed Norton, Damien Thompson et autres

A number of X-ray analyses of an enzyme involved in a key early stage of tetrapyrrole biosynthesis are reported. Two structures of human 5-aminolaevulinate dehydratase (ALAD), native and recombinant, have been determined at 2.8 Å resolution, showing that the enzyme adopts an …

Structural studies of substrate and product complexes of 5-aminolaevulinic acid dehydratase from humans,Escherichia coliand the hyperthermophilePyrobaculum calidifontis

N.L. Mills-Davies, Danica S. Butler, Ed Norton, Darren A. Thompson et autres

A number of X-ray analyses of an enzyme involved in a key early stage of tetrapyrrole biosynthesis are reported. Two structures of human 5-aminolaevulinate dehydratase (ALAD), native and recombinant, have been determined at 2.8 Å resolution, showing that the enzyme adopts an …

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X-Ray Diffraction Images For Human Recombinant 5-Aminolevulinic Acid Dehydratase (Alad).

Danica S. Butler, P.T. Erskine, Jon Cooper, Peter M. Shoolingin‐Jordan

X-ray diffraction images for recominant human 5-aminolevulinic acid dehydratase (ALAD) collected at ESRF (Grenoble) beam line ID14-2 using an ADSC Quantum 4 detector to a resolution of 2.8 Å. A series of 1 ̊ oscillation images were recorded with an exposure time …

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X-ray structure of human recombinant 5-aminolaevulinic acid dehydratase (hrALAD).

Danica S. Butler, P.T. Erskine, J.B. Cooper, Peter M. Shoolingin‐Jordan

Analysis of Jmjd6 Cellular Localization and Testing for Its Involvement in Histone Demethylation

Phillip Hahn, Ivonne Wegener, Alison Burrells, Jens Böse et autres

BACKGROUND: Methylation of residues in histone tails is part of a network that regulates gene expression. JmjC domain containing proteins catalyze the oxidative removal of methyl groups on histone lysine residues. Here, we report studies to test the involvement of Jumonji domain-containing …

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Crystal Structure of the 2-Oxoglutarate- and Fe(II)-Dependent Lysyl Hydroxylase JMJD6

Monica Mantri, Tobias J. Krojer, Eleanor A. L. Bagg, Celia J. Webby et autres

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Jmjd6 Catalyses Lysyl-Hydroxylation of U2AF65, a Protein Associated with RNA Splicing

Celia J. Webby, Alexander Wolf, Natalia Gromak, Mathias Dreger et autres

The finding that the metazoan hypoxic response is regulated by oxygen-dependent posttranslational hydroxylations, which regulate the activity and lifetime of hypoxia-inducible factor (HIF), has raised the question of whether other hydroxylases are involved in the regulation of gene expression. We reveal that …

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Synthesis and use of isotope-labelled substrates for a mechanistic study on human α-methylacyl-CoA racemase 1A (AMACR; P504S)

Daniel J. Darley, Danica S. Butler, Samuel J. Prideaux, Thomas W. Thornton et autres

Alpha-Methylacyl-CoA racemase (AMACR) is an important enzyme for the metabolism of branched-chain lipids and drugs. The enzyme is over-expressed in prostate and other cancers. AMACR 1A, the major splice variant, was purified from recombinant E. coli cells as a His-tag protein. Purified …

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Crystal structures of histone demethylase JMJD2A reveal basis for substrate specificity

Stanley S. Ng, K.L. Kavanagh, M.A. McDonough, Danica S. Butler et autres

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Structural and Mechanistic Studies on the Inhibition of the Hypoxia-inducible Transcription Factor Hydroxylases by Tricarboxylic Acid Cycle Intermediates

Kirsty S. Hewitson, Benoît M. R. Liénard, M.A. McDonough, Ian J. Clifton et autres

In humans both the levels and activity of the alpha-subunit of the hypoxia-inducible transcription factor (HIF-alpha) are regulated by its post-translation hydroxylation as catalyzed by iron- and 2-oxoglutarate (2OG)-dependent prolyl and asparaginyl hydroxylases (PHD1-3 and factor-inhibiting HIF (FIH), respectively). One consequence of …

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Structure of Human Phytanoyl-CoA 2-Hydroxylase Identifies Molecular Mechanisms of Refsum Disease*

M.A. McDonough, K.L. Kavanagh, Danica S. Butler, Timothy Searls et autres

Refsum disease (RD), a neurological syndrome characterized by adult onset retinitis pigmentosa, anosmia, sensory neuropathy, and phytanic acidaemia, is caused by elevated levels of phytanic acid. Many cases of RD are associated with mutations in phytanoyl-CoA 2-hydroxylase (PAHX), an Fe(II) and 2-oxoglutarate …

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Studies on the specificity of unprocessed and mature forms of phytanoyl-CoA 2-hydroxylase and mutation of the iron binding ligands

Timothy Searls, Danica S. Butler, Winnie Chien, Mridul Mukherji et autres

The mature form of phytanoyl-coenzyme A 2-hydroxylase (PAHX), a nonheme Fe(II)- and 2-oxoglutarate-dependent oxygenase, catalyzes the alpha-hydroxylation of phytanoyl-CoA within peroxisomes. Mutations in PAHX result in some forms of adult Refsum's disease. Unprocessed PAHX (pro-PAHX) contains an N-terminal peroxisomal targeting sequence that …

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