Vitamin B 12
A cobalt-containing coordination compound produced by intestinal micro-organisms and found also in soil and water. Higher plants do not concentrate vitamin B 12 from the soil and so are a poor source of the substance as compared with animal tissues. INTRINSIC FACTOR is important for the assimilation of vitamin B 12.
Pentosyltransferases
Nicotinamide-Nucleotide Adenylyltransferase
Nicotinamide Mononucleotide
Methylmalonyl-CoA Mutase
Transcobalamins
Propanediol Dehydratase
Neoplasms
Salmonella enterica
Salmonella typhimurium
Salmonella
A genus of gram-negative, facultatively anaerobic, rod-shaped bacteria that utilizes citrate as a sole carbon source. It is pathogenic for humans, causing enteric fevers, gastroenteritis, and bacteremia. Food poisoning is the most common clinical manifestation. Organisms within this genus are separated on the basis of antigenic characteristics, sugar fermentation patterns, and bacteriophage susceptibility.
Colitis, Ischemic
Galaxies
Spherocytes
Crohn Disease
A chronic transmural inflammation that may involve any part of the DIGESTIVE TRACT from MOUTH to ANUS, mostly found in the ILEUM, the CECUM, and the COLON. In Crohn disease, the inflammation, extending through the intestinal wall from the MUCOSA to the serosa, is characteristically asymmetric and segmental. Epithelioid GRANULOMAS may be seen in some patients.
Gastroenterology
Colitis
Halobacteriales
Archaea
One of the three domains of life (the others being BACTERIA and Eukarya), formerly called Archaebacteria under the taxon Bacteria, but now considered separate and distinct. They are characterized by: (1) the presence of characteristic tRNAs and ribosomal RNAs; (2) the absence of peptidoglycan cell walls; (3) the presence of ether-linked lipids built from branched-chain subunits; and (4) their occurrence in unusual habitats. While archaea resemble bacteria in morphology and genomic organization, they resemble eukarya in their method of genomic replication. The domain contains at least four kingdoms: CRENARCHAEOTA; EURYARCHAEOTA; NANOARCHAEOTA; and KORARCHAEOTA.
Haloferax
Halobacteriaceae
A family of extremely halophilic archaea found in environments with high salt concentrations, such as salt lakes, evaporated brines, or salted fish. Halobacteriaceae are either obligate aerobes or facultative anaerobes and are divided into at least twenty-six genera including: HALOARCULA; HALOBACTERIUM; HALOCOCCUS; HALOFERAX; HALORUBRUM; NATRONOBACTERIUM; and NATRONOCOCCUS.
Haloferax mediterranei
Pregnancy
Rh-Hr Blood-Group System
Erythroblastosis, Fetal
A condition characterized by the abnormal presence of ERYTHROBLASTS in the circulation of the FETUS or NEWBORNS. It is a disorder due to BLOOD GROUP INCOMPATIBILITY, such as the maternal alloimmunization by fetal antigen RH FACTORS leading to HEMOLYSIS of ERYTHROCYTES, hemolytic anemia (ANEMIA, HEMOLYTIC), general edema (HYDROPS FETALIS), and SEVERE JAUNDICE IN NEWBORN.
Rh Isoimmunization
Identity Crisis
Multiple Sclerosis
An autoimmune disorder mainly affecting young adults and characterized by destruction of myelin in the central nervous system. Pathologic findings include multiple sharply demarcated areas of demyelination throughout the white matter of the central nervous system. Clinical manifestations include visual loss, extra-ocular movement disorders, paresthesias, loss of sensation, weakness, dysarthria, spasticity, ataxia, and bladder dysfunction. The usual pattern is one of recurrent attacks followed by partial recovery (see MULTIPLE SCLEROSIS, RELAPSING-REMITTING), but acute fulminating and chronic progressive forms (see MULTIPLE SCLEROSIS, CHRONIC PROGRESSIVE) also occur. (Adams et al., Principles of Neurology, 6th ed, p903)
Diarrhea
Multiple Sclerosis, Relapsing-Remitting
The most common clinical variant of MULTIPLE SCLEROSIS, characterized by recurrent acute exacerbations of neurologic dysfunction followed by partial or complete recovery. Common clinical manifestations include loss of visual (see OPTIC NEURITIS), motor, sensory, or bladder function. Acute episodes of demyelination may occur at any site in the central nervous system, and commonly involve the optic nerves, spinal cord, brain stem, and cerebellum. (Adams et al., Principles of Neurology, 6th ed, pp903-914)
Methylmalonic Acid
Folic Acid
Vitamin B 12 Deficiency
A nutritional condition produced by a deficiency of VITAMIN B 12 in the diet, characterized by megaloblastic anemia. Since vitamin B 12 is not present in plants, humans have obtained their supply from animal products, from multivitamin supplements in the form of pills, and as additives to food preparations. A wide variety of neuropsychiatric abnormalities is also seen in vitamin B 12 deficiency and appears to be due to an undefined defect involving myelin synthesis. (From Cecil Textbook of Medicine, 19th ed, p848)
Diet, Vegetarian
Temperature
Thermodynamics
A rigorously mathematical analysis of energy relationships (heat, work, temperature, and equilibrium). It describes systems whose states are determined by thermal parameters, such as temperature, in addition to mechanical and electromagnetic parameters. (From Hawley's Condensed Chemical Dictionary, 12th ed)
Binding of Cob(II)alamin to the adenosylcobalamin-dependent ribonucleotide reductase from Lactobacillus leichmannii. Identification of dimethylbenzimidazole as the axial ligand. (1/283)
The ribonucleoside triphosphate reductase (RTPR) from Lactobacillus leichmannii catalyzes the reduction of nucleoside 5'-triphosphates to 2'-deoxynucleoside 5'-triphosphates and uses coenzyme B12, adenosylcobalamin (AdoCbl), as a cofactor. Use of a mechanism-based inhibitor, 2'-deoxy-2'-methylenecytidine 5'-triphosphate, and isotopically labeled RTPR and AdoCbl in conjunction with EPR spectroscopy has allowed identification of the lower axial ligand of cob(II)alamin when bound to RTPR. In common with the AdoCbl-dependent enzymes catalyzing irreversible heteroatom migrations and in contrast to the enzymes catalyzing reversible carbon skeleton rearrangements, the dimethylbenzimidazole moiety of the cofactor is not displaced by a protein histidine upon binding to RTPR. (+info)The reaction of the substrate analog 2-ketoglutarate with adenosylcobalamin-dependent glutamate mutase. (2/283)
Glutamate mutase is one of several adenosylcobalamin-dependent enzymes that catalyze unusual rearrangements that proceed through a mechanism involving free radical intermediates. The enzyme exhibits remarkable specificity, and so far no molecules other than L-glutamate and L-threo-3-methylaspartate have been found to be substrates. Here we describe the reaction of glutamate mutase with the substrate analog, 2-ketoglutarate. Binding of 2-ketoglutarate (or its hydrate) to the holoenzyme elicits a change in the UV-visible spectrum consistent with the formation of cob(II)alamin on the enzyme. 2-ketoglutarate undergoes rapid exchange of tritium between the 5'-position of the coenzyme and C-4 of 2-ketoglutarate, consistent with the formation of a 2-ketoglutaryl radical analogous to that formed with glutamate. Under aerobic conditions this leads to the slow inactivation of the enzyme, presumably through reaction of free radical species with oxygen. Despite the formation of a substrate-like radical, no rearrangement of 2-ketoglutarate to 3-methyloxalacetate could be detected. The results indicate that formation of the C-4 radical of 2-ketoglutarate is a facile process but that it does not undergo further reactions, suggesting that this may be a useful substrate analog with which to investigate the mechanism of coenzyme homolysis. (+info)Methanol:coenzyme M methyltransferase from Methanosarcina barkeri -- substitution of the corrinoid harbouring subunit MtaC by free cob(I)alamin. (3/283)
Methyl-coenzyme M formation from coenzyme M and methanol in Methanosarcina barkeri is catalysed by an enzyme system composed of three polypeptides MtaA, MtaB and MtaC, the latter of which harbours a corrinoid prosthetic group. We report here that MtaC can be substituted by free cob(I)alamin which is methylated with methanol in an MtaB-catalysed reaction and demethylated with coenzyme M in an MtaA-catalysed reaction. Methyl transfer from methanol to coenzyme M was found to proceed at a relatively high specific activity at micromolar concentrations of cob(I)alamin. This finding was surprising because the methylation of cob(I)alamin catalysed by MtaB alone and the demethylation of methylcob(III)alamin catalysed by MtaA alone exhibit apparent Km for cob(I)alamin and methylcob(III)alamin of above 1 mm. A possible explanation is that MtaA positively affects the MtaB catalytic efficiency and vice versa by decreasing the apparent Km for their corrinoid substrates. Activation of MtaA by MtaB was methanol-dependent. In the assay for methanol:coenzyme M methyltransferase activity cob(I)alamin could be substituted by cob(I)inamide which is devoid of the nucleotide loop. Substitution was, however, only possible when the assays were supplemented with imidazole: approximately 1 mm imidazole being required for half-maximal activity. Methylation of cob(I)inamide with methanol was found to be dependent on imidazole but not on the demethylation of methylcob(III)inamide with coenzyme M. The demethylation reaction was even inhibited by imidazole. The structure and catalytic mechanism of the MtaABC complex are compared with the cobalamin-dependent methionine synthase. (+info)Adenosylcobalamin-mediated methyl transfer by toluate cis-dihydrodiol dehydrogenase of the TOL plasmid pWW0. (4/283)
We identified and characterized a methyl transfer activity of the toluate cis-dihydrodiol (4-methyl-3,5-cyclohexadiene-cis-1, 2-diol-1-carboxylic acid) dehydrogenase of the TOL plasmid pWW0 towards toluene cis-dihydrodiol (3-methyl-4,5-cyclohexadiene-cis-1, 2-diol). When the purified enzyme from the recombinant Escherichia coli containing the xylL gene was incubated with toluene cis-dihydrodiol in the presence of NAD+, the end products differed depending on the presence of adenosylcobalamin (coenzyme B12). The enzyme yielded catechol in the presence of adenosylcobalamin, while it gave 3-methylcatechol in the absence of the cofactor. Adenosylcobalamin was transformed to methylcobalamin as a result of the enzyme reaction, which indicates that the methyl group of the substrate was transferred to adenosylcobalamin. Other derivatives of the cobalamin such as aquo (hydroxy)- and cyanocobalamin did not mediate the methyl transfer reaction. The dehydrogenation and methyl transfer reactions were assumed to occur concomitantly, and the methyl transfer reaction seemed to depend on the dehydrogenation. To our knowledge, the enzyme is the first dehydrogenase that shows a methyl transfer activity as well. (+info)Co-ordinate variations in methylmalonyl-CoA mutase and methionine synthase, and the cobalamin cofactors in human glioma cells during nitrous oxide exposure and the subsequent recovery phase. (5/283)
We investigated the co-ordinate variations of the two cobalamin (Cbl)-dependent enzymes, methionine synthase (MS) and methylmalonyl-CoA mutase (MCM), and measured the levels of their respective cofactors, methylcobalamin (CH3Cbl) and adenosylcobalamin (AdoCbl) in cultured human glioma cells during nitrous oxide exposure and during a subsequent recovery period of culture in a nitrous oxide-free atmosphere (air). In agreement with published data, MS as the primary target of nitrous oxide was inactivated rapidly (initial rate of 0.06 h(-1)), followed by reduction of CH3Cbl (to <20%). Both enzyme activity and cofactor levels recovered rapidly when the cells were subsequently cultured in air, but the recovery was completely blocked by the protein-synthesis inhibitor, cycloheximide. During MS inactivation, there was a reduction of cellular AdoCbl and holo-MCM activity (measured in the absence of exogenous AdoCbl) to about 50% of pre-treatment levels. When the cells were transferred to air, both AdoCbl and holo-MCM activity recovered, albeit more slowly than the MS system. Notably, the regain of the holo-MCM and AdoCbl was enhanced rather than inhibited by cycloheximide. These findings confirm irreversible damage of MS by nitrous oxide; hence, synthesis of the enzyme is required to restore its activity. In contrast, restoration of holo-MCM activity is only dependent on repletion of the AdoCbl cofactor. We also observed a synchronous fluctuation in AdoCbl and the much larger hydroxycobalamin pool during the inactivation and recovery phase, suggesting that the loss and repletion of AdoCbl reflect changes in intracellular Cbl homoeostasis. Our data demonstrate that the nitrous oxide-induced changes in MS and CH3Cbl are associated with reversible changes in both MCM holoactivity and the AdoCbl level, suggesting co-ordinate distribution of Cbl cofactors during depletion and repletion. (+info)Identification and expression of the genes encoding a reactivating factor for adenosylcobalamin-dependent glycerol dehydratase. (6/283)
Adenosylcobalamin-dependent glycerol dehydratase undergoes inactivation by glycerol, the physiological substrate, during catalysis. In permeabilized cells of Klebsiella pneumoniae, the inactivated enzyme is reactivated in the presence of ATP, Mg2+, and adenosylcobalamin. We identified the two open reading frames as the genes for a reactivating factor for glycerol dehydratase and designated them gdrA and gdrB. The reactivation of the inactivated glycerol dehydratase by the gene products was confirmed in permeabilized recombinant Escherichia coli cells coexpressing GdrA and GdrB proteins with glycerol dehydratase. (+info)Structure and dynamics of the B12-binding subunit of glutamate mutase from Clostridium cochlearium. (7/283)
Glutamate mutase (Glm) is an adenosylcobamide-dependent enzyme that catalyzes the reversible rearrangement of (2S)-glutamate to (2S, 3S)-3-methylaspartate. The active enzyme from Clostridium cochlearium consists of two subunits (of 53.6 and 14.8 kDa) as an alpha2beta2 tetramer, whose assembly is mediated by coenzyme B12. The smaller of the protein components, GlmS, has been suggested to be the B12-binding subunit. Here we report the solution structure of GlmS, determined from a heteronuclear NMR-study, and the analysis of important dynamical aspects of this apoenzyme subunit. The global fold and dynamic behavior of GlmS in solution are similar to those of the corresponding subunit MutS from C. tetanomorphum, which has previously been investigated using NMR-spectroscopy. Both solution structures of the two Glm B12-binding subunits share striking similarities with that determined by crystallography for the B12-binding domain of methylmalonyl CoA mutase (Mcm) from Propionibacterium shermanii, which is B12 bound. In the crystal structure a conserved histidine residue was found to be coordinated to cobalt, displacing the endogenous axial ligand of the cobamide. However, in GlmS and MutS the sequence motif, Asp-x-His-x-x-Gly, which includes the cobalt-coordinating histidine residue, and a predicted alpha-helical region following the motif, are present as an unstructured and highly mobile loop. In the absence of coenzyme, the B12-binding site apparently is only partially formed. By comparing the crystal structure of Mcm with the solution structures of B12-free GlmS and MutS, a consistent picture on the mechanism of B12 binding has been obtained. Important elements of the binding site only become structured upon binding B12; these include the cobalt-coordinating histidine residue, and an alpha helix that forms one side of the cleft accommodating the nucleotide 'tail' of the coenzyme. (+info)Isolation of acetate auxotrophs of the methane-producing archaeon Methanococcus maripaludis by random insertional mutagenesis. (8/283)
To learn more about autotrophic growth of methanococci, we isolated nine conditional mutants of Methanococcus maripaludis after transformation of the wild type with a random library in pMEB.2, a suicide plasmid bearing the puromycin-resistance cassette pac. These mutants grew poorly in mineral medium and required acetate or complex organic supplements such as yeast extract for normal growth. One mutant, JJ104, was a leaky acetate auxotroph. A plasmid, pWDK104, was recovered from this mutant by electroporation of a plasmid preparation into Escherichia coli. Transformation of wild-type M. maripaludis with pWDK104 produced JJ104-1, a mutant with the same phenotype as JJ104, thus establishing that insertion of pWDK104 into the genome was responsible for the phenotype. pWDK104 contained portions of the methanococcal genes encoding an ABC transporter closely related to MJ1367-MJ1368 of M. jannaschii. Because high levels of molybdate, tungstate, and selenite restored growth to wild-type levels, this transporter may be specific for these oxyanions. A second acetate auxotroph, JJ117, had an absolute growth requirement for either acetate or cobalamin, and wild-type growth was observed only in the presence of both. Cobinamide, 5', 6'-dimethylbenzimidazole, and 2-aminopropanol did not replace cobalamin. This phenotype was correlated with tandem insertions in the genome but not single insertions and appeared to have resulted from an indirect effect on cobamide metabolism. Plasmids rescued from other mutants contained portions of ORFs denoted in M. jannaschii as endoglucanase (MJ0555), transketolase (MJ0681), thiamine biosynthetic protein thiI (MJ0931), and several hypothetical proteins (MJ1031, MJ0835, and MJ0835.1). (+info)
Identification and expression of the genes encoding a reactivating factor for adenosylcobalamin-dependent glycerol dehydratase<...
RCSB PDB
- 1C9K: THE THREE DIMENSIONAL STRUCTURE OF ADENOSYLCOBINAMIDE KINASE/ ADENOSYLCOBINAMIDE PHOSPHATE...
Thermolysis of coenzymes B12 at physiological temperatures: activation parameters for cobalt-carbon bond homolysis and a...
This Week in Science | Science
Sequence Similarity
- 1JHA: Structural Investigation of the Biosynthesis of Alternative Lower Ligands for Cobamides...
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Coenzyme b12 | Article about Coenzyme b12 by The Free Dictionary
Allergy Research Group B12 Adenosylcobalamin 3,000 mcg 60 Lozenges - Swanson®
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Adenosyl capsule: buy adenosyl capsule 10 capsules pack online at best price in india | 1mg
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Biodistribution of radiolabeled adenosylcobalamin in patients diagnosed with various malignancies
PE Adenosyl/Hydroxy B12 liquid (30 ml)
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Adenosyl/Hydroxy B12 90 Caps
Designated organic active ingredient containing (doai) > Ester doai > Z-c(=o)-o-y wherein z is hydrogen or an organic radical...
cob(II)alamin reductase - oi
ENZYME entry 5.4.99.61
NWMN RS11195 - AureoWiki
cobalt-precorrin-5B (C1)-methyltransferase(EC 2.1.1.195) - Creative Enzymes
Manufacturers confidence has seen sharpest fall for 28 years, warns CBI | Daily Mail Online
Bangungot - Sintomas at Sanhi | Mediko.ph
Sakit sa Buto - Sintomas, Sanhi, at Uri | Mediko.ph
Publicaţii
Structures of the human GTPase MMAA and vitamin B12-dependent methylmalonyl-CoA mutase and insight into their complex formation...
Evidence for axial coordination of 5,6-dimethylbenzimidazole to the cobalt atom of adenosylcobalamin bound to diol dehydratase<...
One pathway can incorporate either adenine or dimethylbenzimidazole as an α-axial ligand of B<sub>12</sub> cofactors in...
The mechanism of action of coenzyme B12. I: Mechanism of action of coenzyme B12. Hydrogen transfer in the isomerization of beta...
Generation and reactions of organic radical cations in zeolites<...
B12 Liquid
Nutraceuticals Drug - Adenosylcobalamin, Ferrous Ascorbate & Foilc Acid Soft Gel Capsules Manufacturer from Sonipat
Adsorption and Organization of the Organic Radical 3-Carboxyproxyl on a Cu(110) Surface : A Combined STM, RAIRS, and DFT Study
PURITAN PRIDE METHYLCOBALAMIN B-12 5000MCG - Jollys Pharmacy Online Store
Methylcobalamin & Pregabalin Capsules
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Methyl B-12 by ProHealth (Sublingual Methylcobalamin B12 Supplements) - ProHealth.com
Adenosyl/Hydroxy Vitamin B12 for Energy, Mood and Nerve Health
Propanediol/glycerol dehydratase, small subunit (IPR003207) | InterPro | EMBL-EBI
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coenzyme B6
arsonic acid
Psyche
Methylcobalamin I.M. and S.C. injections equivalance to sublingual form | Phoenix Rising ME / CFS Forums
French Vegetables Quiz - By cob579cob
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ENZYME entry 2.4.2.21
400 தொண்டர்களுக்கு ஆண்மையிழப்பு சிகிச்சை- குர்மீத்துக்கு சி.பி.ஐ கிடுக்கிப்பிடி! | CBI questions Ram Rahim on forced...
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Vitamin B12
Perlman D (1959). "Microbial synthesis of cobamides". Advances in Applied Microbiology. 1: 87-122. doi:10.1016/S0065-2164(08) ...
Ribonucleoside-triphosphate reductase
Blakley RL (May 1965). "Cobamides and ribonucleotide reduction. I. Cobamide stimulation of ribonucleotide reduction in extracts ...
Nicotinate-nucleotide-dimethylbenzimidazole phosphoribosyltransferase
"Structural investigation of the biosynthesis of alternative lower ligands for cobamides by nicotinate mononucleotide: 5,6- ...
List of MeSH codes (D03)
... cobamides MeSH D03.383.129.578.840.437.777.560 - hydroxocobalamin MeSH D03.383.129.578.840.500 - porphyrins MeSH D03.383. ... cobamides MeSH D03.549.909.437.777.560 - hydroxocobalamin MeSH D03.549.909.500 - porphyrins MeSH D03.549.909.500.250 - ...
List of MeSH codes (D04)
... cobamides MeSH D04.345.783.437.777.560 - hydroxocobalamin MeSH D04.345.783.500 - porphyrins MeSH D04.345.783.500.250 - ...
RCSB PDB
- 1JHA: Structural Investigation of the Biosynthesis of Alternative Lower Ligands for Cobamides by...
UFZ - Publikationsverzeichnis - Helmholtz-Zentrum für Umweltforschung UFZ
Biodistribution of radiolabeled adenosylcobalamin in patients diagnosed with various malignancies
Vitamin B12 - Wikipedia
Salmonella enterica synthesizes 5,6-dimethylbenzimidazolyl-(DMB)-α-riboside. Why some Firmicutes do not require the canonical...
Vitamin B12-Mediated Restoration of Defective Anaerobic Growth Leads to Reduced Biofilm Formation in Pseudomonas aeruginosa |...
Production of Vitamin B12 Analogues in Patients with Small-Bowel Bacterial Overgrowth | Annals of Internal Medicine | American...
Cobamides ([AdeJCNCba, [2-Me Ade] CNCba, [CN]2Cbi and factor E) were found in the intestinal contents in three of the four ... Thus bacterial production of cobamides, both de novo and from ingested CN-Cbl bound to intrinsic factor, occurs in humans with ... We investigated the presence of vitamin B12 analogues (cobamides) and the bacterial conversion of 57Co-B12 (vitamin B12 ... Radioactivity of cobamide zones from duplicate chromatograms showed bacterial conversion of (57Co)-CN-Cbl into cobamides. ...
Brandt Steps Down as GI Chief | Einstein/Montefiore Department of Medicine | Albert Einstein College of Medicine
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Research Brief 276: Novel Cobamide Structure May Hold Clues for More Effective Biological Degradation of Chlorinated Compounds ...
A majority of organisms, including humans, require cobamides for normal functioning. Vitamin B12 is the best-known member of ... Enzymes that depend on cobamides fulfill essential metabolic functions in most organisms, including mammals. As a result, a ... The researchers previously discovered that changes to the lower base structure of cobamides influence the bioremediation ... Understanding the biological and geochemical conditions that support the production of specific cobamides, which efficiently ...
The Good Ol' Grignard | In the Pipeline
Vitamin B12: Vital Nutrient for Good Health - The Weston A. Price Foundation
Journal of Bacteriology | National Agricultural Library
Metabolism of halophilic archaea | SpringerLink
Fluorinated Vitamin B12 Analogs Are Cofactors of Corrinoid-Dependent Enzymes: a 19F-Labeled Nuclear Magnetic Resonance Probe...
The phenol-containing cobamides contributed up to 90% of the protein-bound cobamides of the 1,300 to 1,900 nmol of corrinoid ... Hence, it is possible to use 19F-labeled nuclear magnetic resonance spectroscopy for analyses of protein-bound cobamides. ... Phenol and, presumably, 4-fluorophenol were specifically incorporated into these cobamides, since phenol was not metabolized ...
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Northwestern University - Research Output
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- University of Illinois at Urbana-Champaign
Thermolysis of coenzymes B12 at physiological temperatures: activation parameters for cobalt-carbon bond homolysis and a...
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- University of Illinois at Urbana-Champaign
Anderson, T., Birman, K., Broberg, R., Caesar, M., Comer, D., Cotton, C., Freedman, M. J., Haeberlen, A., Ives, Z. G., Krishnamurthy, A., Lehr, W., Loo, B. T., Mazières, D., Nicolosi, A., Smith, J. M., Stoica, I., Van Renesse, R., Walfish, M., Weatherspoon, H. & Yoo, C. S., Jul 2014, In : Computer Communication Review. 44, 3, p. 81-86 6 p.. Research output: Contribution to journal › Article › peer-review ...
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- Albert Einstein College of Medicine
Syntheses and characterization of vitamin B12-Pt(II) conjugates and their adenosylation in an enzymatic assay - Zurich Open...
This Week in Science | Science
Cobamides are required for many processes, from catabolism of carbon sources to nucleotide biosynthesis, and are needed by a ... Availability of cobamides is patchy and habitat specific, and nonspecific scavenging may not be adequate to obtain a specific ... Taking as an example a diverse and interesting family of enzyme cofactors-the cobalt-containing cobamides, which include ... Therefore, a variety of mutualisms have evolved to deliver and import specific structural variants of cobamides between ...
Analogs5
- Vitamin B12 belongs to a family of structurally-diverse cofactors with over a dozen natural analogs, collectively referred to as cobamides. (usda.gov)
- Some bacteria employ a mechanism called cobamide remodeling, a process in which cobamides are converted into other analogs, to ensure that compatible. (usda.gov)
- They found these B12 sources contain B12 analogs called cobamides, which may block the absorption of the body's bio-available B12 and increase the body's need for the nutrient. (lifespa.com)
- But plant foods said to contain B12 actually contain B12 analogs called cobamides that block intake of and increase the need for true B12. (theppk.com)
- However, these plant foods actually contain B12 analogs called cobamides, which are thought to compete with B12 and block its intake, therefore actually increasing the need for B12. (betteryou.com)
Humans1
- Thus bacterial production of cobamides, both de novo and from ingested CN-Cbl bound to intrinsic factor, occurs in humans with bacterial overgrowth states and results in a significant loss of vitamin B12 to the host. (annals.org)
Bacteria2
- One class of nutrients, cobamides (the family of enzyme cofactors that includes vitamin B12), is widely used for a variety of microbial metabolic functions, but these structurally diverse cofactors are synthesized by only a subset of bacteria and archaea. (bvsalud.org)
- The phylogenetically diverse group of reductively dehalogenating bacteria utilizes cobamides (B 12 vitamers) as cofactors of the key enzyme in their energy metabolism, the respiratory reductive dehalogenase. (uni-jena.de)
Substances1
- Cobamides are substances that act as a foil to B12 absorption, and they are produced by unhealthy bacterial overgrowth and imbalance in the intestines. (saveourbones.com)
Intestinal1
- We investigated the presence of vitamin B12 analogues (cobamides) and the bacterial conversion of 57 Co-B12 (vitamin B12 cyanocobalamin, [ 57 Co]-CN-Cbl) into cobamides in the intestinal contents of four patients with bacterial overgrowth. (annals.org)
Cofactors2
- Cobamides are members of the vitamin B 12 family of cofactors that function in a variety of metabolic processes and are synthesized only by prokaryotes. (northwestern.edu)
- abstract = "Cobamides are members of the vitamin B12 family of cofactors that function in a variety of metabolic processes and are synthesized only by prokaryotes. (northwestern.edu)
Cobamide2
- Radioactivity of cobamide zones from duplicate chromatograms showed bacterial conversion of ( 57 Co)-CN-Cbl into cobamides. (annals.org)
- N-OXIDE OF PURINE-COBAMIDES: 1-N-OXI-2-METHYL-ADENINE-COBAMIDE AND 1-N-OXI-ADENINE-COBAMIDE Simulations of delta check rule performance to detect specimen mislabeling using historical laboratory data. (levaquin2020.site)
Corrinoid2
- The phenol-containing cobamides contributed up to 90% of the protein-bound cobamides of the 1,300 to 1,900 nmol of corrinoid per g of dry cell material formed. (asm.org)
- Despite bearing a rather large metal complex on the beta-axial position, the cobamides in 5 and 7 are recognized by the corrinoid adenosyltransferase enzyme that catalyzes the formation of the organometallic C-Co bond present in adenosylcobalamin after release of the Pt(II) complexes. (uzh.ch)
Enzyme1
- GTP:adenosylcobinamide-phosphate (AdoCbi-P) guanylyl transferase (CobY) is an enzyme that transfers the GMP moiety of GTP to AdoCbi yielding AdoCbi-GDP in the late steps of the assembly of Ado-cobamides in archaea. (nih.gov)
Intake1
- Cobamides can block your intake of B12 and increase your need for the real thing. (pilatesfitness.co.uk)