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Gene Review

MTR  -  5-methyltetrahydrofolate-homocysteine...

Sus scrofa

 
 
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Disease relevance of MTR

 

High impact information on MTR

 

Biological context of MTR

  • Pigs were exposed to 15% nitrous oxide for varying intervals of up to 7 days or studied at varying intervals of recovery in air after 7 days nitrous oxide inhalation, and the rate of inactivation or resynthesis of methionine synthase was related to the corresponding AdoMet/AdoHcy ratios [6].
 

Anatomical context of MTR

  • The recovery pattern of methionine synthase was broadly linear but was slower in the spinal cord (0.10 +/- 0.03% per hr; mean +/- SEM) than in any other tissue examined including brain (0.35 +/- 0.04% per hr) [6].
 

Associations of MTR with chemical compounds

 

Other interactions of MTR

References

  1. Purification and kinetic mechanism of a mammalian methionine synthase from pig liver. Chen, Z., Crippen, K., Gulati, S., Banerjee, R. J. Biol. Chem. (1994) [Pubmed]
  2. Effects of the disruption of transmethylation in the central nervous system: an animal model. Scott, J.M., Molloy, A.M., Kennedy, D.G., Kennedy, S., Weir, D.G. Acta Neurol. Scand., Suppl. (1994) [Pubmed]
  3. Folate deficiency disturbs hepatic methionine metabolism and promotes liver injury in the ethanol-fed micropig. Halsted, C.H., Villanueva, J.A., Devlin, A.M., Niemelä, O., Parkkila, S., Garrow, T.A., Wallock, L.M., Shigenaga, M.K., Melnyk, S., James, S.J. Proc. Natl. Acad. Sci. U.S.A. (2002) [Pubmed]
  4. Ethanol feeding of micropigs alters methionine metabolism and increases hepatocellular apoptosis and proliferation. Halsted, C.H., Villanueva, J., Chandler, C.J., Stabler, S.P., Allen, R.H., Muskhelishvili, L., James, S.J., Poirier, L. Hepatology (1996) [Pubmed]
  5. Purification of soluble cytochrome b5 as a component of the reductive activation of porcine methionine synthase. Chen, Z., Banerjee, R. J. Biol. Chem. (1998) [Pubmed]
  6. The relationship between the activity of methionine synthase and the ratio of S-adenosylmethionine to S-adenosylhomocysteine in the brain and other tissues of the pig. Molloy, A.M., Orsi, B., Kennedy, D.G., Kennedy, S., Weir, D.G., Scott, J.M. Biochem. Pharmacol. (1992) [Pubmed]
  7. Characterization of nonradioactive assays for cobalamin-dependent and cobalamin-independent methionine synthase enzymes. Drummond, J.T., Jarrett, J., González, J.C., Huang, S., Matthews, R.G. Anal. Biochem. (1995) [Pubmed]
  8. Assays of methylenetetrahydrofolate reductase and methionine synthase activities by monitoring 5-methyltetrahydrofolate and tetrahydrofolate using high-performance liquid chromatography with fluorescence detection. Huang, L., Zhang, J., Hayakawa, T., Tsuge, H. Anal. Biochem. (2001) [Pubmed]
  9. Folylpolyglutamates as substrates and inhibitors of folate-dependent enzymes. Matthews, R.G., Ghose, C., Green, J.M., Matthews, K.D., Dunlap, R.B. Adv. Enzyme Regul. (1987) [Pubmed]
 
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