Involvement of Vitamin B6 in the Dethiomethylation of Methionine by Rumen Microorganisms1

Merricks, D. L.; Salsbury, R. L.

doi:10.1128/aem.28.1.106-111.1974

Cited by 16 publications

(4 citation statements)

References 7 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…One involves deamination of methionine by l -methionine γ-lyase (Mgl), and the other, cystathionine lyase, or C–S lyase. Mgl is absent in mammals but has been demonstrated in plants, parasitic protozoa, as well as numerous bacteria including those in the rumen, those used in food fermentation, and soil bacteria (Table ), playing a key function that converts methionine into α-ketobutyrate, MT, and ammonia (reviewed in refs − ). Tokoro and colleagues suggest that mgl genes and their proteins were likely derived from Archaea by horizontal gene transfer…”

Section: Microbial–mammalian Co-metabolism Of Methioninementioning

confidence: 99%

Metabolic Fingerprint of Dimethyl Sulfone (DMSO₂) in Microbial–Mammalian Co-metabolism

Slupsky

2014

J. Proteome Res.

View full text Add to dashboard Cite

There is growing awareness that intestinal microbiota alters the energy harvesting capacity of the host and regulates metabolism. It has been postulated that intestinal microbiota are able to degrade unabsorbed dietary components and transform xenobiotic compounds. The resulting microbial metabolites derived from the gastrointestinal tract can potentially enter the circulation system, which, in turn, affects host metabolism. Yet, the metabolic capacity of intestinal microbiota and its interaction with mammalian metabolism remains largely unexplored. Here, we review a metabolic pathway that integrates the microbial catabolism of methionine with mammalian metabolism of methanethiol (MT), dimethyl sulfide (DMS), and dimethyl sulfoxide (DMSO), which together provide evidence that supports the microbial origin of dimethyl sulfone (DMSO2) in the human metabolome. Understanding the pathway of DMSO2 co-metabolism expends our knowledge of microbial-derived metabolites and motivates future metabolomics-based studies on ascertaining the metabolic consequences of intestinal microbiota on human health, including detoxification processes and sulfur xenobiotic metabolism.

show abstract

Section: Microbial–mammalian Co-metabolism Of Methioninementioning

confidence: 99%

Metabolic Fingerprint of Dimethyl Sulfone (DMSO₂) in Microbial–Mammalian Co-metabolism

Slupsky

2014

J. Proteome Res.

View full text Add to dashboard Cite

show abstract

“…(Tanaka et al. 1976; Esaki and Soda 1987), rumen bacteria (Merricks and Salsbury 1974), Aeromonas sp. (Esaki and Soda 1987), and brevibacterium (Dias and Weimer 1998) have been found to produce Hcy γ‐lyase.…”

Section: Introductionmentioning

confidence: 99%

Isolation of a homocysteine γ-lyase-producing bacterium and study of its enzyme production conditions

Zhao

Jia

et al. 2008

J Appl Microbiol

View full text Add to dashboard Cite

Aim: To investigate the possibility of finding a new homocysteine (Hcy) γ‐lyase with the desired properties for Hcy measurement in bacteria. Methods and Results: Through a process of enrichment, the Hcy γ‐lyase‐producing bacterium strain N2‐1 was isolated from soil. Based upon its morphological, physiological, and biochemical characteristics, as well as its 16S rDNA sequence and phylogenetic tree analysis, this isolate belongs to the genus Serratia. The effects of pH, aeration, inducers, carbon (C) and nitrogen (N) sources on enzyme production were studied. Methionine, yeast extract, and glucose were selected as the optimal inducer, C and N sources, respectively. Maximum production of Hcy γ‐lyase was obtained when the isolate was cultured at 30°C at pH 6·5 for about 36 h in the optimum medium. Results also showed that this Hcy γ‐lyase has relatively high specificity towards Hcy. Conclusions: Because of its high specificity for Hcy, this bacterial Hcy γ‐lyase has the potential application in Hcy determination. Significance and Impact of the Study: In addition to isolating a bacterium that produces Hcy γ‐lyase suitable for Hcy determination, this study also indicates that the bacterium could be a source for production of Hcy γ‐lyase for clinical applications.

show abstract

“…(Wiesendanger & Nisman, 1953), Pseudomonas sp. (Miwatani et al, 1954;Kallio & Larson, 1955;Ito et al, 1975;Tanaka et al, 1977), some rumen bacteria (Merricks & Salsbury, 1974) and Aeromonas sp. (Nakayama et al, 1984).…”

Section: Introductionmentioning

confidence: 99%

Purification and characterization of methionine γ-lyase from Trichomonas vaginalis

Lockwood

Coombs

1991

Biochemical Journal

View full text Add to dashboard Cite

Methionine gamma-lyase (EC 4.4.1.11) was purified to homogeneity from the anaerobic protozoan parasite Trichomonas vaginalis by a series of f.p.l.c. procedures. The enzyme catalyses alpha gamma- and alpha beta-elimination reactions of a number of derivatives of methionine and cysteine. It also catalyses gamma-replacement reactions of the thiomethyl group of methionine, homocysteine and ethionine to yield the corresponding S-substituted homocysteine derivative. The enzyme is pyridoxal 5'-phosphate-dependent, has a native molecular mass of approx. 160 kDa and consists of four apparently identical subunits of molecular mass 43-45 kDa. The absorption spectrum of the enzyme is typical of those obtained for other pyridoxal 5'-phosphate-dependent enzymes, and the holoenzyme can be resolved to the apoenzyme by incubation with hydroxylamine and reconstituted by addition of the cofactor. The enzyme activity is significantly affected by carbonyl and thiol reagents, is competitively inhibited by a number of substrate analogues and is completely inactivated by the suicide inhibitor DL-propargylglycine. The T. vaginalis enzyme is similar, in terms of activity and properties, to the enzymes found in a number of species of bacteria that metabolize methionine under anaerobic conditions. It is suggested that methionine catabolism may be of particular importance to the survival of T. vaginalis under microaerophilic conditions in its host.

show abstract

Involvement of Vitamin B6 in the Dethiomethylation of Methionine by Rumen Microorganisms1

Cited by 16 publications

References 7 publications

Metabolic Fingerprint of Dimethyl Sulfone (DMSO₂) in Microbial–Mammalian Co-metabolism

Metabolic Fingerprint of Dimethyl Sulfone (DMSO₂) in Microbial–Mammalian Co-metabolism

Isolation of a homocysteine γ-lyase-producing bacterium and study of its enzyme production conditions

Purification and characterization of methionine γ-lyase from Trichomonas vaginalis

Contact Info

Product

Resources

About

Involvement of Vitamin B6 in the Dethiomethylation of Methionine by Rumen Microorganisms1

Cited by 16 publications

References 7 publications

Metabolic Fingerprint of Dimethyl Sulfone (DMSO2) in Microbial–Mammalian Co-metabolism

Metabolic Fingerprint of Dimethyl Sulfone (DMSO2) in Microbial–Mammalian Co-metabolism

Isolation of a homocysteine γ-lyase-producing bacterium and study of its enzyme production conditions

Purification and characterization of methionine γ-lyase from Trichomonas vaginalis

Contact Info

Product

Resources

About

Metabolic Fingerprint of Dimethyl Sulfone (DMSO₂) in Microbial–Mammalian Co-metabolism

Metabolic Fingerprint of Dimethyl Sulfone (DMSO₂) in Microbial–Mammalian Co-metabolism