Synthesis of methionine in rat liver by the B12‐independent N5‐methyltetrahydropterolyltri‐glutamate: homocysteine methyltransferase reported by Wang, Koch and Stokstad has been investigated. In agreement with their results it was found that methionine was formed by crude rat liver supernatant fraction and dialyzed mitochondrial extract on aerobic incubation with N5‐methyltetrahydropteroyltriglutamate, homocysteine and magnesium chloride. However, the folate derivative could not have been involved in this process since N5‐[14C]methyl‐tetrahydropteroyltriglutamate did not incorporate 14C into the methionine. In the supernatant fraction, methionine was formed by the transmethylation of endogenous betaine with added homocysteine. Rat liver supernatant fraction was found to contain 250 nmoles/ml betaine. In the mitochondrial extract, methionine formation occurred by proteolysis. It is concluded that a B12‐independent N5‐methyltetrahydropteroyltriglutamate: homocysteine methyltransferase does not occur in rat liver. Copyright © 1968, Wiley Blackwell. All rights reserved