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The requirement for cobalt in vitamin B 12 : A paradigm for protein metalation.
- Source :
-
Biochimica et biophysica acta. Molecular cell research [Biochim Biophys Acta Mol Cell Res] 2021 Jan; Vol. 1868 (1), pp. 118896. Date of Electronic Publication: 2020 Oct 21. - Publication Year :
- 2021
-
Abstract
- Vitamin B <subscript>12</subscript> , cobalamin, is a cobalt-containing ring-contracted modified tetrapyrrole that represents one of the most complex small molecules made by nature. In prokaryotes it is utilised as a cofactor, coenzyme, light sensor and gene regulator yet has a restricted role in assisting only two enzymes within specific eukaryotes including mammals. This deployment disparity is reflected in another unique attribute of vitamin B <subscript>12</subscript> in that its biosynthesis is limited to only certain prokaryotes, with synthesisers pivotal in establishing mutualistic microbial communities. The core component of cobalamin is the corrin macrocycle that acts as the main ligand for the cobalt. Within this review we investigate why cobalt is paired specifically with the corrin ring, how cobalt is inserted during the biosynthetic process, how cobalt is made available within the cell and explore the cellular control of cobalt and cobalamin levels. The partitioning of cobalt for cobalamin biosynthesis exemplifies how cells assist metalation.<br /> (Copyright © 2020 The Authors. Published by Elsevier B.V. All rights reserved.)
- Subjects :
- Animals
Bacterial Proteins biosynthesis
Bacterial Proteins genetics
Cobalt chemistry
Coenzymes genetics
Coenzymes metabolism
Corrinoids genetics
Humans
Ligands
Tetrapyrroles metabolism
Vitamin B 12 chemistry
Vitamin B 12 genetics
Cobalt metabolism
Symbiosis genetics
Tetrapyrroles chemistry
Vitamin B 12 metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 1879-2596
- Volume :
- 1868
- Issue :
- 1
- Database :
- MEDLINE
- Journal :
- Biochimica et biophysica acta. Molecular cell research
- Publication Type :
- Academic Journal
- Accession number :
- 33096143
- Full Text :
- https://doi.org/10.1016/j.bbamcr.2020.118896