Results 71 to 80 of about 876 (161)

Differential temporal release and lipoprotein loading in B. thetaiotaomicron bacterial extracellular vesicles

open access: yesJournal of Extracellular Vesicles, Volume 13, Issue 1, January 2024.
Abstract Bacterial extracellular vesicles (BEVs) contribute to stress responses, quorum sensing, biofilm formation and interspecies and interkingdom communication. However, the factors that regulate their release and heterogeneity are not well understood.
Rokas Juodeikis   +8 more
wiley   +1 more source

Chemically similar yet functionally distinct: Selectivity of methylmalonyl-CoA mutase among naturally diverse cobamide cofactors [PDF]

open access: yes, 2019
Vitamin B12 is predominantly associated with human health, and many people are surprised to learn that B12 is produced by bacteria. Like humans, bacteria have metabolic enzymes that require B12 as a cofactor.
Sokolovskaya, Olga Matveevna
core  

Cobamide remodeling in the freshwater microalga Chlamydomonas reinhardtii

open access: yesFEMS Microbiology Letters, 2020
ABSTRACTMicroalgae are not able to produce cobamides (Cbas, B12 vitamers) de novo. Hence, the production of catalytically active Cba-containing methionine synthase (MetH), which is present in selected representatives, is dependent on the availability of exogenous B12 vitamers.
Christoph Baum   +3 more
openaire   +3 more sources

Anaerobic biosynthesis of the lower ligand of vitamin B12 [PDF]

open access: yes, 2015
Vitamin B12 (cobalamin) is required by humans and other organisms for diverse metabolic processes, although only a subset of prokaryotes is capable of synthesizing B12 and other cobamide cofactors.
Begley, Tadhg   +12 more
core   +1 more source

A New Class of Phosphoribosyltransferases Involved in Cobamide Biosynthesis Is Found in Methanogenic Archaea and Cyanobacteria

open access: yes, 2019
Cobamides are coenzymes used by cells from all domains of life but made de novo by only some bacteria and archaea. The last steps of the cobamide biosynthetic pathway activate the corrin ring and the lower ligand base, condense the activated ...
Theodoric A. Mattes (6278864)   +3 more
core   +1 more source

Biosynthesis and utilization of structurally diverse norcobamide cofactors in the tetrachloroethene-respiring bacterium Sulfurospirillum multivorans [PDF]

open access: yes, 2018
The bacterium Sulfurospirillum multivorans synthesizes the unusual cobamide norpseudo-B12 (Np-B12) as cofactor of the tetrachloroethene reductive dehalogenase PceA de novo. Np-B12 harbors an adenine as lower base and a unique ethanolamine O-phosphate (EA-
Keller, Sebastian
core   +1 more source

Photonic management of Spirulina (Arthrospira platensis) in scalable photobioreactors to achieve biologically active unopposed vitamin B12

open access: yesDiscover Food
Dietary vitamin B12 deficiency is one of the most common micronutrient deficiencies worldwide, with over a billion individuals suffering from low levels of the vitamin.
A. Tzachor   +7 more
doaj   +1 more source

The SMUL_1544 gene product governs norcobamide biosynthesis in the tetrachloroethene-respiring bacterium Sulfurospirillum multivorans

open access: yes, 2016
The tetrachloroethene (PCE)-respiring bacterium Sulfurospirillum multivorans produces a unique cobamide, namely, norpseudo-B12, which, in comparison to other cobamides, e.g., cobalamin and pseudo-B12, lacks the methyl group in the linker moiety of the ...
Escalante-Semerena, J.   +4 more
core   +1 more source

Cobamide extraction procedures for analysis of tissue and microbiome samples [PDF]

open access: yes
The structure of cobalamin has an upper β- axial ligand group and a lower α-axial ligand base. Different groups can attach to the upper ligand to form different forms of cobalamin.
Chang, Shun
core  

Diatoms as tools for assay of total B12 activity and cyanocobalamin activity in sea water [PDF]

open access: yes, 1977
The total cobamide concentration (vitamin B12 plus B12 analogs active for some organisms) can be determined in sea water by bioassay utilizing growth of the centric diatom Bellerochea polymorpha clone 675-d.
Guillard, Robert R.L., Swift, Dorothy G.
core   +1 more source

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