Isolation of a Δ7-cholesterol desaturase from Tetrahymena thermophila

Cell-free preparations of Tetrahymena thermophila catalyze the direct desaturation of cholesterol to Δ7-dehydrocholesterol (provitamin D3). The activity was isolated in the microsomal fraction from Tetrahymena homogenates. Δ7-Desaturase activity was stimulated fivefold by the addition of 6 mM ATP. O...

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Publicado:	2000
Materias:	adenosine triphosphate delta 7 cholesterol desaturase nicotinamide adenine dinucleotide nicotinamide adenine dinucleotide phosphate protozoal protein reduced nicotinamide adenine dinucleotide reduced nicotinamide adenine dinucleotide phosphate unclassified drug cholesterol lathosterol delta 5 dehydrogenase lathosterol delta-5-dehydrogenase oxidoreductase article biotechnology biotransformation chemical reaction kinetics dairy industry enzyme activity enzyme isolation nonhuman Tetrahymena thermophila animal culture medium enzymology growth, development and aging isolation and purification metabolism microsome Ciliophora Protozoa Animals Cholesterol Culture Media Microsomes Oxidoreductases Oxidoreductases Acting on CH-CH Group Donors
Acceso en línea:	https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_01757598_v53_n5_p591_Valcarce http://hdl.handle.net/20.500.12110/paper_01757598_v53_n5_p591_Valcarce
Aporte de:	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

id	paper:paper_01757598_v53_n5_p591_Valcarce
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spelling	paper:paper_01757598_v53_n5_p591_Valcarce2023-06-08T15:18:58Z Isolation of a Δ7-cholesterol desaturase from Tetrahymena thermophila adenosine triphosphate delta 7 cholesterol desaturase nicotinamide adenine dinucleotide nicotinamide adenine dinucleotide phosphate protozoal protein reduced nicotinamide adenine dinucleotide reduced nicotinamide adenine dinucleotide phosphate unclassified drug cholesterol lathosterol delta 5 dehydrogenase lathosterol delta-5-dehydrogenase oxidoreductase article biotechnology biotransformation chemical reaction kinetics dairy industry enzyme activity enzyme isolation nonhuman Tetrahymena thermophila animal culture medium enzymology growth, development and aging isolation and purification metabolism microsome Ciliophora Protozoa Tetrahymena thermophila Tetrahymena thermophila Animals Cholesterol Culture Media Microsomes Oxidoreductases Oxidoreductases Acting on CH-CH Group Donors Tetrahymena thermophila Cell-free preparations of Tetrahymena thermophila catalyze the direct desaturation of cholesterol to Δ7-dehydrocholesterol (provitamin D3). The activity was isolated in the microsomal fraction from Tetrahymena homogenates. Δ7-Desaturase activity was stimulated fivefold by the addition of 6 mM ATP. Other cofactors assayed, including NAD, NADP, NADH or NADPH, had no significant effect. The activity was found in microsomes prepared from stationary-phase cultures of the ciliate, grown either with or without added cholesterol, thus indicating that it is constitutively expressed in T. thermophila cells. 2000 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_01757598_v53_n5_p591_Valcarce http://hdl.handle.net/20.500.12110/paper_01757598_v53_n5_p591_Valcarce
institution	Universidad de Buenos Aires
institution_str	I-28
repository_str	R-134
collection	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic	adenosine triphosphate delta 7 cholesterol desaturase nicotinamide adenine dinucleotide nicotinamide adenine dinucleotide phosphate protozoal protein reduced nicotinamide adenine dinucleotide reduced nicotinamide adenine dinucleotide phosphate unclassified drug cholesterol lathosterol delta 5 dehydrogenase lathosterol delta-5-dehydrogenase oxidoreductase article biotechnology biotransformation chemical reaction kinetics dairy industry enzyme activity enzyme isolation nonhuman Tetrahymena thermophila animal culture medium enzymology growth, development and aging isolation and purification metabolism microsome Ciliophora Protozoa Tetrahymena thermophila Tetrahymena thermophila Animals Cholesterol Culture Media Microsomes Oxidoreductases Oxidoreductases Acting on CH-CH Group Donors Tetrahymena thermophila
spellingShingle	adenosine triphosphate delta 7 cholesterol desaturase nicotinamide adenine dinucleotide nicotinamide adenine dinucleotide phosphate protozoal protein reduced nicotinamide adenine dinucleotide reduced nicotinamide adenine dinucleotide phosphate unclassified drug cholesterol lathosterol delta 5 dehydrogenase lathosterol delta-5-dehydrogenase oxidoreductase article biotechnology biotransformation chemical reaction kinetics dairy industry enzyme activity enzyme isolation nonhuman Tetrahymena thermophila animal culture medium enzymology growth, development and aging isolation and purification metabolism microsome Ciliophora Protozoa Tetrahymena thermophila Tetrahymena thermophila Animals Cholesterol Culture Media Microsomes Oxidoreductases Oxidoreductases Acting on CH-CH Group Donors Tetrahymena thermophila Isolation of a Δ7-cholesterol desaturase from Tetrahymena thermophila
topic_facet	adenosine triphosphate delta 7 cholesterol desaturase nicotinamide adenine dinucleotide nicotinamide adenine dinucleotide phosphate protozoal protein reduced nicotinamide adenine dinucleotide reduced nicotinamide adenine dinucleotide phosphate unclassified drug cholesterol lathosterol delta 5 dehydrogenase lathosterol delta-5-dehydrogenase oxidoreductase article biotechnology biotransformation chemical reaction kinetics dairy industry enzyme activity enzyme isolation nonhuman Tetrahymena thermophila animal culture medium enzymology growth, development and aging isolation and purification metabolism microsome Ciliophora Protozoa Tetrahymena thermophila Tetrahymena thermophila Animals Cholesterol Culture Media Microsomes Oxidoreductases Oxidoreductases Acting on CH-CH Group Donors Tetrahymena thermophila
description	Cell-free preparations of Tetrahymena thermophila catalyze the direct desaturation of cholesterol to Δ7-dehydrocholesterol (provitamin D3). The activity was isolated in the microsomal fraction from Tetrahymena homogenates. Δ7-Desaturase activity was stimulated fivefold by the addition of 6 mM ATP. Other cofactors assayed, including NAD, NADP, NADH or NADPH, had no significant effect. The activity was found in microsomes prepared from stationary-phase cultures of the ciliate, grown either with or without added cholesterol, thus indicating that it is constitutively expressed in T. thermophila cells.
title	Isolation of a Δ7-cholesterol desaturase from Tetrahymena thermophila
title_short	Isolation of a Δ7-cholesterol desaturase from Tetrahymena thermophila
title_full	Isolation of a Δ7-cholesterol desaturase from Tetrahymena thermophila
title_fullStr	Isolation of a Δ7-cholesterol desaturase from Tetrahymena thermophila
title_full_unstemmed	Isolation of a Δ7-cholesterol desaturase from Tetrahymena thermophila
title_sort	isolation of a δ7-cholesterol desaturase from tetrahymena thermophila
publishDate	2000
url	https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_01757598_v53_n5_p591_Valcarce http://hdl.handle.net/20.500.12110/paper_01757598_v53_n5_p591_Valcarce
_version_	1768543080279965696

Isolation of a Δ7-cholesterol desaturase from Tetrahymena thermophila

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