Gut Commensal Bacteroidetes Encode a Novel Class of Vitamin B12-Binding Proteins [PDF]
Human gut commensal Bacteroidetes rely on multiple transport systems to acquire vitamin B12 and related cobamides for fitness in the gut. In addition to a set of conserved transport proteins, these systems also include a diverse repertoire of additional ...
E. E. Putnam +8 more
doaj +2 more sources
Cobamide-mediated enzymatic reductive dehalogenation via long-range electron transfer
Cobalamin-containing reductive dehalogenases from organohalide-respiring bacteria play a key role in the degradation of halogenated organic compounds. Here the authors proposed a catalytic mechanism for dehalogenation that relies on a long-range electron
Cindy Kunze +6 more
doaj +3 more sources
Cobamide Fingerprinting Reveals Nutritional Diversity of Vitamin B12 in Edible Shellfish
In edible shellfish, vitamin B12 content has traditionally been evaluated based on total content; however, recent studies reveal substantial diversity in corrinoid composition among species. This review integrates molecular and ecological perspectives to
Fumio Watanabe +2 more
doaj +2 more sources
Isolation of cobamides from Methanothrix soehngenii: 5-methylbenzimidazole as the ?-ligand of the predominant cobamide [PDF]
Methanothrix soehngenii was found to contain five different cobamides when grown on vitamin B12 supplemented as well as vitamin B12 free media. In both cases, it was shown by HPLC-chromatography and UV/VIS spectroscopy, that α-5-methylbenzimidazolyl-β-cyanocobamide was the predominant cobamide, accounting for 27% and 23%, respectively, of the total ...
Kohler, Hans-Peter E. (author)
openaire +3 more sources
Structure of the Methanosarcina mazei Mtr complex bound to the oxygen-stress responsive small protein MtrI [PDF]
Methanogenic archaea emit ~1 Gt of methane annually, impacting global carbon cycling and climate. Central to their energy metabolism is a membrane-bound, sodium-translocating methyltransferase complex: the N⁵-tetrahydromethanopterin:CoM-S ...
Tristan Reif-Trauttmansdorff +8 more
doaj +2 more sources
Nutrient encryption and the diversity of cobamides, siderophores, and glycans. [PDF]
Encryption makes information available only to those with the decoding key. We propose that microbes, living in a chemical environment, encrypt nutrients, thereby making them available only to those with the decoding enzymes, such as their kin. Examples of encrypted nutrients include cobamides, which are expensive to make and valuable for microbial ...
Taga ME, Ludington WB.
europepmc +3 more sources
Vitamin B12 is the only known essential human micronutrient made exclusively by prokaryotes. Kennedy and Taga introduce us to the world of cobamides-those cobalt-containing compounds, like B12, that appear to be the proprietary domain of our microbial partners.
Kennedy, Kristopher J, Taga, Michiko E
openaire +4 more sources
Evolutionarily divergent DUF4465 domains have a common vitamin B<sub>12</sub>-binding function. [PDF]
We show that DUF4465 family proteins, widespread across bacteria from gut microbiomes, hydrothermal vents, and soil, share a common vitamin B12‐binding function. These augmented β‐jellyroll proteins bind vitamin B12 via extended loops. Our findings establish sequence‐diverse DUF4465 proteins as a widespread class of B12‐binding proteins, highlighting ...
Clarke C +4 more
europepmc +2 more sources
Evidence for corrin biosynthesis in the last universal common ancestor. [PDF]
Cobalamin biosynthesis can be traced back to the last universal common ancestor. After a stage of chemical evolution of the acetyl‐CoA pathway, the enzymatic synthesis of cobalamin evolved, allowing life to be independent of the insoluble solid‐state catalysts that tethered primordial CO2 assimilation to the Earth's crust, suggesting a role for corrin ...
Modjewski LD +5 more
europepmc +2 more sources
Elevated Levels of an Enzyme Involved in Coenzyme B12 Biosynthesis Kills Escherichia coli
Cobamides are cobalt-containing cyclic tetrapyrroles involved in the metabolism of organisms from all domains of life but produced de novo only by some bacteria and archaea.
Victoria L. Jeter +1 more
doaj +1 more source

