1. Academic Validation
  2. Mammalian glycine N-methyltransferases. Comparative kinetic and structural properties of the enzymes from human, rat, rabbit and pig livers

Mammalian glycine N-methyltransferases. Comparative kinetic and structural properties of the enzymes from human, rat, rabbit and pig livers

  • Comp Biochem Physiol B. 1993 Nov;106(3):601-11. doi: 10.1016/0305-0491(93)90137-t.
H Ogawa 1 T Gomi M Fujioka
Affiliations

Affiliation

  • 1 Department of Biochemistry, Faculty of Medicine, Toyama Medical and Pharmaceutical University, Japan.
Abstract

1. Human liver contains a rather high level of glycine N-methyltransferase. 2. The Enzymes from human, rat, rabbit and pig livers are all tetramers and exhibit positive cooperativity toward S-adenosylmethionine and Michaelis-Menten kinetics toward glycine. The [S]0.5 values for S-adenosylmethionine and glycine of the rat Enzyme are considerably lower than those of three other Enzymes. 3. The subunit of rat glycine N-methyltransferase is shorter by two residues compared with the subunits of human, rabbit and pig glycine N-methyltransferases. Except for this difference, however, all Enzymes show a high degree of sequence homology.

Figures