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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| Acceso en línea: | http://hdl.handle.net/20.500.12110/paper_01757598_v53_n5_p591_Valcarce |
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todo:paper_01757598_v53_n5_p591_Valcarce2023-10-03T15:07:55Z Isolation of a Δ7-cholesterol desaturase from Tetrahymena thermophila Valcarce, G. Florin-Christensen, J. Nudel, C. 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. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar 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 Valcarce, G. Florin-Christensen, J. Nudel, C. 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. |
| format |
JOUR |
| author |
Valcarce, G. Florin-Christensen, J. Nudel, C. |
| author_facet |
Valcarce, G. Florin-Christensen, J. Nudel, C. |
| author_sort |
Valcarce, G. |
| 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 |
| url |
http://hdl.handle.net/20.500.12110/paper_01757598_v53_n5_p591_Valcarce |
| work_keys_str_mv |
AT valcarceg isolationofad7cholesteroldesaturasefromtetrahymenathermophila AT florinchristensenj isolationofad7cholesteroldesaturasefromtetrahymenathermophila AT nudelc isolationofad7cholesteroldesaturasefromtetrahymenathermophila |
| _version_ |
1807315804810641408 |