Folate polyglutamate synthetase activity in the cobalamin-inactivated rat.
Exposure to N2O inactivates cob[I]alamin and interferes with the activity of methionine synthetase, of which cob[I]alamin is a coenzyme. Less directly, it stops the formation of folate polyglutamate from tetrahydrofolates. Studies on the activity of folate polyglutamate synthetase in rat liver in vivo were carried out. The synthetase activity increased after exposure to N2O for up to 48 h, but longer exposure was accompanied by a return of activity to baseline values. The rise in synthetase activity was prevented by supplying methionine, 5'-methylthioadenosine or 5-formyltetrahydrofolate. The fall in folate polyglutamate synthetase activity after 48 h was accompanied by a restoration of hepatic synthesis of folate polyglutamate despite continuation of N2O exposure.
D019732:Amide Synthases; D000818:Animals; D008025:Ligases / Q000378:metabolism*; D008099:Liver / Q000187:drug effects / Q000201:enzymology*; D008297:Male; D009609:Nitrous Oxide / Q000494:pharmacology; D011624:Pteroylpolyglutamic Acids / Q000096:biosynthesis; D051381:Rats; D011919:Rats, Inbred Strains; D014805:Vitamin B 12 / Q000494:pharmacology*
D011624:Pteroylpolyglutamic Acids; D008025:Ligases; D019732:Amide Synthases; C024383:pteroylpolyglutamate synthase; D009609:Nitrous Oxide; D014805:Vitamin B 12