Probing the molecular mechanisms in copper amine oxidases by generating heterodimers.

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Oxygen Activation Switch in the Copper Amine Oxidase of Escherichia coli

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Q58775896-17DF512C-A009-4C31-91A4-F1F8EC836143

P2860

Probing the molecular mechanisms in copper amine oxidases by generating heterodimers.

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2015年論文

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name

Probing the molecular mechanisms in copper amine oxidases by generating heterodimers.

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Probing the molecular mechanisms in copper amine oxidases by generating heterodimers.

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Probing the molecular mechanisms in copper amine oxidases by generating heterodimers.

@en

Probing the molecular mechanisms in copper amine oxidases by generating heterodimers.

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Probing the molecular mechanisms in copper amine oxidases by generating heterodimers.

@en

Probing the molecular mechanisms in copper amine oxidases by generating heterodimers.

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ChemBioChem

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Probing the molecular mechanisms in copper amine oxidases by generating heterodimers.

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P2093

Mark A Smith

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Peter F Knowles

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Thembaninkosi G Gaule

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P2860

Conserved tyrosine-369 in the active site of Escherichia coli copper amine oxidase is not essential

The crystal structure of Pichia pastoris lysyl oxidase

Crystal structure of a quinoenzyme: copper amine oxidase of Escherichia coli at 2 A resolution

Crystal structure of a eukaryotic (pea seedling) copper-containing amine oxidase at 2.2 A resolution

Catalytic mechanism of the quinoenzyme amine oxidase from Escherichia coli: exploring the reductive half-reaction

Crystal structures of the copper-containing amine oxidase from Arthrobacter globiformis in the holo and apo forms: implications for the biogenesis of topaquinone

Heterodimers of wild-type and subunit interface mutant enzymes of glutathione S-transferase A1-1: interactive or independent active sites?

Role of the interactions between the active site base and the substrate Schiff base in amine oxidase catalysis. Evidence from structural and spectroscopic studies of the 2-hydrazinopyridine adduct of Escherichia coli amine oxidase.

Direct demonstration of half-of-the-sites reactivity in the dimeric cytochrome bc1 complex: enzyme with one inactive monomer is fully active but unable to activate the second ubiquinol oxidation site in response to ligand binding at the ubiquinone r

Structure of human semicarbazide-sensitive amine oxidase/vascular adhesion protein-1.

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559-564

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scholarly article

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10.1002/CBIC.201402653

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Arwen Pearson

Michael J. McPherson

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3090556

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2015-01-21T00:00:00Z

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271275881

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1988525984

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25607656

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4497604

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96189/