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- W4285126557 abstract "Cobamides (Cbas) are the largest coenzymes known and are used by cells in all domains of life. These molecules are characterized by a central cobalt-containing tetrapyrrole ring with two opposing axial ligands on the α and β faces of the ring. All biologically active forms of Cbas have a 5'-deoxyadenosyl group as the upper (Coβ) ligand that is covalently attached to the cobalt ion of the ring. In contrast, the lower ligand is a nucleobase of diverse chemical structure; however, nucleobases are usually derivatives of benzimidazole or purine. Phenol and p-cresol can also serve as the nucleobase, but they cannot form a coordination bond with the cobalt ion of the ring because they lack a free pair of electrons. The Cba incorporating 5,6-dimethylbenzimidazole (DMB) is known as cobalamin (Cbl), and the coenzymic form of cobalamin is known as adenosylcobalamin (AdoCbl). A common vitamer of cobalamin has a cyano group as the upper ligand. This vitamer is known as cyanocobalamin (CNCbl), which is commercially marketed as vitamin B12. Here, we describe a combination of chemical hydrolysis of cobalamin with the enzymatic dephosphorylation of the resulting α-R-3'-phosphate to yield α-R, which we enzymically convert to the pathway intermediate α-R-5'-phosphate (α-RP). The methods describe herein can be readily scaled up to generate large amounts of α-RP." @default.
- W4285126557 created "2022-07-14" @default.
- W4285126557 creator A5030129561 @default.
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- W4285126557 date "2022-01-01" @default.
- W4285126557 modified "2023-09-28" @default.
- W4285126557 title "A method for the isolation of α-ribazole from vitamin B12, and its enzymatic conversion to α-ribazole 5′-phosphate" @default.
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- W4285126557 doi "https://doi.org/10.1016/bs.mie.2021.11.024" @default.
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