Autocatalysed oxidative modifications to 2-oxoglutarate dependent oxygenases.

Autocatalysed oxidative modifications to 2-oxoglutarate dependent oxygenases.

Čájet eará veršuvnnaid (2)

Ferrous iron and 2-oxoglutarate-dependent oxygenases and related enzymes catalyse a range of oxidative reactions, possibly the widest of any enzyme family. Their catalytic flexibility is proposed to be related to their nonhaem iron-binding site, which utilizes two or three protein-based ligands. A p...

Bibliográfalaš dieđut
Váldodahkkit:	Mantri, M, Zhang, Z, McDonough, M, Schofield, C
Materiálatiipa:	Journal article
Giella:	English
Almmustuhtton:	2012

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Autocatalysed oxidative modifications to 2-oxoglutarate dependent oxygenases
Dahkki: Mantri, M, et al.
Almmustuhtton: (2012)

Autocatalysed oxidative modifications to 2-oxoglutarate dependent oxygenases
Dahkki: Mantri, M, et al.
Almmustuhtton: (2012)

Inhibition of 2-oxoglutarate dependent oxygenases.
Dahkki: Rose, N, et al.
Almmustuhtton: (2011)

Structural studies on human 2-oxoglutarate dependent oxygenases.
Dahkki: McDonough, M, et al.
Almmustuhtton: (2010)

Oxidation by 2-oxoglutarate oxygenases: non-haem iron systems in catalysis and signalling.
Dahkki: Hewitson, K, et al.
Almmustuhtton: (2005)

2-oxoglutarate-dependent oxygenases
Dahkki: Islam, M, et al.
Almmustuhtton: (2018)

Role of the jelly-roll fold in substrate binding by 2-oxoglutarate oxygenases.
Dahkki: Aik, W, et al.
Almmustuhtton: (2012)

Mechanistic studies on 2-oxoglutarate dependent oxygenases
Dahkki: Schofield, C, et al.
Almmustuhtton: (1999)

The 2-oxoglutarate-dependent oxygenase JMJD6 catalyses oxidation of lysine residues to give 5S-hydroxylysine residues.
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Almmustuhtton: (2011)

Structural and stereoelectronic insights into oxygenase catalyzed formation of ethylene from 2-oxoglutarate
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Almmustuhtton: (2017)

Structural and mechanistic studies on 2-oxoglutarate-dependent oxygenases and related enzymes.
Dahkki: Schofield, C, et al.
Almmustuhtton: (1999)

Structural studies on 2-oxoglutarate oxygenases and related double-stranded beta-helix fold proteins.
Dahkki: Clifton, I, et al.
Almmustuhtton: (2006)

A fluorescence-based assay for 2-oxoglutarate-dependent oxygenases.
Dahkki: McNeill, L, et al.
Almmustuhtton: (2005)

Biochemical and structural investigations clarify the substrate selectivity of the 2-oxoglutarate oxygenase JMJD6.
Dahkki: Islam, MS, et al.
Almmustuhtton: (2019)

Expanding chemical biology of 2-oxoglutarate oxygenases.
Dahkki: Loenarz, C, et al.
Almmustuhtton: (2008)

The role of iron and 2-oxoglutarate oxygenases in signalling.
Dahkki: Hewitson, K, et al.
Almmustuhtton: (2003)

Mechanistic studies on 2-oxoglutarate dependent oxygenases
Dahkki: Szollossi, A
Almmustuhtton: (2012)

Crystallographic studies on 2-oxoglutarate dependent oxygenases
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Crystal structure of the 2-oxoglutarate- and Fe(II)-dependent lysyl hydroxylase JMJD6.
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Crystal Structure of the 2-Oxoglutarate- and Fe(II)-Dependent Lysyl Hydroxylase JMJD6.
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Mechanistic studies on the application of DNA aptamers as inhibitors of 2-oxoglutarate-dependent oxygenases.
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Inhibitor scaffolds for 2-oxoglutarate-dependent histone lysine demethylases.
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Inhibitor scaffolds for 2-oxoglutarate-dependent histone lysine demethylases.
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Structure of proline 3-hydroxylase. Evolution of the family of 2-oxoglutarate dependent oxygenases.
Dahkki: Clifton, I, et al.
Almmustuhtton: (2001)

Functional and inhibition studies on 2-oxoglutarate-dependent oxygenases
Dahkki: Thalhammer, A
Almmustuhtton: (2012)

2-Oxoglutarate oxygenases are inhibited by a range of transition metals.
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Almmustuhtton: (2010)

NMR studies on 2-oxoglutarate oxygenases
Dahkki: Leung, IKH
Almmustuhtton: (2013)

Inhibition of JMJD6 by 2-oxoglutarate mimics
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Almmustuhtton: (2021)

Physiological and biochemical aspects of hydroxylations and demethylations catalyzed by human 2-oxoglutarate oxygenases.
Dahkki: Loenarz, C, et al.
Almmustuhtton: (2011)

The potential of 2-oxoglutarate oxygenases acting on nucleic acids as therapeutic targets
Dahkki: Thalhammer, A, et al.
Almmustuhtton: (2012)

The potential of 2-oxoglutarate oxygenases acting on nucleic acids as therapeutic targets
Dahkki: Thalhammer, A, et al.
Almmustuhtton: (2012)

A photoreactive small-molecule probe for 2-oxoglutarate oxygenases.
Dahkki: Rotili, D, et al.
Almmustuhtton: (2011)

Reporter ligand NMR screening method for 2-oxoglutarate oxygenase inhibitors.
Dahkki: Leung, I, et al.
Almmustuhtton: (2013)

Roles of 2-oxoglutarate oxygenases and isopenicillin N synthase in ß-lactam biosynthesis
Dahkki: Rabe, P, et al.
Almmustuhtton: (2018)

Fluorinated derivatives of pyridine-2,4-dicarboxylate are potent inhibitors of human 2-oxoglutarate dependent oxygenases
Dahkki: Brewitz, L, et al.
Almmustuhtton: (2021)

Studies on deacetoxycephalosporin C synthase support a consensus mechanism for 2-oxoglutarate dependent oxygenases.
Dahkki: Tarhonskaya, H, et al.
Almmustuhtton: (2014)

Reducing agent-mediated nonenzymatic conversion of 2‐oxoglutarate to succinate: implications for oxygenase assays
Dahkki: Khan, A, et al.
Almmustuhtton: (2020)

Incorporation of oxygen into the succinate co-product of iron(II) and 2-oxoglutarate dependent oxygenases from bacteria, plants and humans.
Dahkki: Welford, R, et al.
Almmustuhtton: (2005)

2-Oxoglutarate derivatives can selectively enhance or inhibit the activity of human oxygenases
Dahkki: Nakashima, Y, et al.
Almmustuhtton: (2021)