Stimulation of human nitric oxide synthase by tetrahydrobiopterin and selective binding of the cofactor (Q28316251)

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B Heinzel

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B Mayer

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E Ambach

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G Werner-Felmayer

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H Wachter

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E R Werner

Purification of a Ca2+/calmodulin-dependent nitric oxide synthase from porcine cerebellum. Cofactor-role of tetrahydrobiopterin

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language of work or name

English

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publication date

29 June 1992

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published in

FEBS Letters

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volume

305

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issue

2

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page(s)

160-2

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cites work

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Tetrahydrobiopterin, a cofactor for rat cerebellar nitric oxide synthase, does not function as a reactant in the oxygenation of arginine

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Purification and characterization of particulate endothelium-derived relaxing factor synthase from cultured and native bovine aortic endothelial cells

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Tetrahydrobiopterin-dependent formation of nitrite and nitrate in murine fibroblasts.

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Cytokine-activated endothelial cells express an isotype of nitric oxide synthase which is tetrahydrobiopterin-dependent, calmodulin-independent and inhibited by arginine analogs with a rank-order of potency characteristic of activated macrophages

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Tetrahydrobiopterin-dependent formation of endothelium-derived relaxing factor (nitric oxide) in aortic endothelial cells

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Brain nitric oxide synthase is a biopterin- and flavin-containing multi-functional oxido-reductase.

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Parallel induction of tetrahydrobiopterin biosynthesis and indoleamine 2,3-dioxygenase activity in human cells and cell lines by interferon-gamma.

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Purification and characterization of a human NO synthase

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Biosynthesis and metabolism of tetrahydrobiopterin and molybdopterin

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THE STRUCTURE OF THE PHENYLALANINE-HYDROXYLATION COFACTOR

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Biopterin cofactor biosynthesis: GTP cyclohydrolase, neopterin and biopterin in tissues and body fluids of mammalian species

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Biosynthesis of endothelium-derived relaxing factor: a cytosolic enzyme in porcine aortic endothelial cells Ca2+-dependently converts L-arginine into an activator of soluble guanylyl cyclase

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