Mammalian glycine N-methyltransferases. Comparative kinetic and structural properties of the enzymes from human, rat, rabbit and pig livers.
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Ogawa H, Gomi T, Fujioka M
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.
- PubMed ID
- 8281755 [ View in PubMed]
- 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.