Regulation of monkey liver serine hydroxymethyltransferase by nicotinamide nucleotide

Abstract

The positive homotropic binding of tetrahydrofolate to monkey liver serine hydroxy-methyltransferase 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.