Regulation of monkey liver serine hydroxymethyltransferase by nicotinamide nucleotide.
The positive homotropic binding of tetrahydrofolate to monkey liver serine hydroxymethyltransferase was abolished on preincubating the enzyme with NADH and NADPH. NAD+ was a negative heterotropic effector, whereas NADP+ was without effect. The allosteric effects of nicotinamide nucleotides on the serine hydroxymethyltransferase, reported for the first time, lead to a better understanding of the regulation of the metabolic interconversion of folate coenzymes.
D000818:Animals; D012696:Glycine Hydroxymethyltransferase / Q000378:metabolism*; D000882:Haplorhini; D008099:Liver / Q000201:enzymology*; D008255:Macaca radiata; D009243:NAD / Q000494:pharmacology*; D009249:NADP / Q000494:pharmacology*; D013763:Tetrahydrofolates / Q000378:metabolism; D014166:Transferases / Q000378:metabolism*
D013763:Tetrahydrofolates; D009243:NAD; D009249:NADP; D014166:Transferases; D012696:Glycine Hydroxymethyltransferase