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Biological Activity of Pseudovitamin B(12) on Cobalamin-Dependent Methylmalonyl-CoA Mutase and Methionine Synthase in Mammalian Cultured COS-7 Cells
Adenyl cobamide (commonly known as pseudovitamin B(12)) is synthesized by intestinal bacteria or ingested from edible cyanobacteria. The effect of pseudovitamin B(12) on the activities of cobalamin-dependent enzymes in mammalian cells has not been studied well. This study was conducted to investigat...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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MDPI
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7396987/ https://www.ncbi.nlm.nih.gov/pubmed/32709013 http://dx.doi.org/10.3390/molecules25143268 |
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author | Bito, Tomohiro Bito, Mariko Hirooka, Tomomi Okamoto, Naho Harada, Naoki Yamaji, Ryoichi Nakano, Yoshihisa Inui, Hiroshi Watanabe, Fumio |
author_facet | Bito, Tomohiro Bito, Mariko Hirooka, Tomomi Okamoto, Naho Harada, Naoki Yamaji, Ryoichi Nakano, Yoshihisa Inui, Hiroshi Watanabe, Fumio |
author_sort | Bito, Tomohiro |
collection | PubMed |
description | Adenyl cobamide (commonly known as pseudovitamin B(12)) is synthesized by intestinal bacteria or ingested from edible cyanobacteria. The effect of pseudovitamin B(12) on the activities of cobalamin-dependent enzymes in mammalian cells has not been studied well. This study was conducted to investigate the effects of pseudovitamin B(12) on the activities of the mammalian vitamin B(12)-dependent enzymes methionine synthase and methylmalonyl-CoA mutase in cultured mammalian COS-7 cells to determine whether pseudovitamin B(12) functions as an inhibitor or a cofactor of these enzymes. Although the hydoroxo form of pseudovitamin B(12) functions as a coenzyme for methionine synthase in cultured cells, pseudovitamin B(12) does not activate the translation of methionine synthase, unlike the hydroxo form of vitamin B(12) does. In the second enzymatic reaction, the adenosyl form of pseudovitamin B(12) did not function as a coenzyme or an inhibitor of methylmalonyl-CoA mutase. Experiments on the cellular uptake were conducted with human transcobalamin II and suggested that treatment with a substantial amount of pseudovitamin B(12) might inhibit transcobalamin II-mediated absorption of a physiological trace concentration of vitamin B(12) present in the medium. |
format | Online Article Text |
id | pubmed-7396987 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-73969872020-08-05 Biological Activity of Pseudovitamin B(12) on Cobalamin-Dependent Methylmalonyl-CoA Mutase and Methionine Synthase in Mammalian Cultured COS-7 Cells Bito, Tomohiro Bito, Mariko Hirooka, Tomomi Okamoto, Naho Harada, Naoki Yamaji, Ryoichi Nakano, Yoshihisa Inui, Hiroshi Watanabe, Fumio Molecules Article Adenyl cobamide (commonly known as pseudovitamin B(12)) is synthesized by intestinal bacteria or ingested from edible cyanobacteria. The effect of pseudovitamin B(12) on the activities of cobalamin-dependent enzymes in mammalian cells has not been studied well. This study was conducted to investigate the effects of pseudovitamin B(12) on the activities of the mammalian vitamin B(12)-dependent enzymes methionine synthase and methylmalonyl-CoA mutase in cultured mammalian COS-7 cells to determine whether pseudovitamin B(12) functions as an inhibitor or a cofactor of these enzymes. Although the hydoroxo form of pseudovitamin B(12) functions as a coenzyme for methionine synthase in cultured cells, pseudovitamin B(12) does not activate the translation of methionine synthase, unlike the hydroxo form of vitamin B(12) does. In the second enzymatic reaction, the adenosyl form of pseudovitamin B(12) did not function as a coenzyme or an inhibitor of methylmalonyl-CoA mutase. Experiments on the cellular uptake were conducted with human transcobalamin II and suggested that treatment with a substantial amount of pseudovitamin B(12) might inhibit transcobalamin II-mediated absorption of a physiological trace concentration of vitamin B(12) present in the medium. MDPI 2020-07-17 /pmc/articles/PMC7396987/ /pubmed/32709013 http://dx.doi.org/10.3390/molecules25143268 Text en © 2020 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Bito, Tomohiro Bito, Mariko Hirooka, Tomomi Okamoto, Naho Harada, Naoki Yamaji, Ryoichi Nakano, Yoshihisa Inui, Hiroshi Watanabe, Fumio Biological Activity of Pseudovitamin B(12) on Cobalamin-Dependent Methylmalonyl-CoA Mutase and Methionine Synthase in Mammalian Cultured COS-7 Cells |
title | Biological Activity of Pseudovitamin B(12) on Cobalamin-Dependent Methylmalonyl-CoA Mutase and Methionine Synthase in Mammalian Cultured COS-7 Cells |
title_full | Biological Activity of Pseudovitamin B(12) on Cobalamin-Dependent Methylmalonyl-CoA Mutase and Methionine Synthase in Mammalian Cultured COS-7 Cells |
title_fullStr | Biological Activity of Pseudovitamin B(12) on Cobalamin-Dependent Methylmalonyl-CoA Mutase and Methionine Synthase in Mammalian Cultured COS-7 Cells |
title_full_unstemmed | Biological Activity of Pseudovitamin B(12) on Cobalamin-Dependent Methylmalonyl-CoA Mutase and Methionine Synthase in Mammalian Cultured COS-7 Cells |
title_short | Biological Activity of Pseudovitamin B(12) on Cobalamin-Dependent Methylmalonyl-CoA Mutase and Methionine Synthase in Mammalian Cultured COS-7 Cells |
title_sort | biological activity of pseudovitamin b(12) on cobalamin-dependent methylmalonyl-coa mutase and methionine synthase in mammalian cultured cos-7 cells |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7396987/ https://www.ncbi.nlm.nih.gov/pubmed/32709013 http://dx.doi.org/10.3390/molecules25143268 |
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