Mammalian glycine N-methyltransferases. Comparative kinetic and structural properties of the enzymes from human, rat, rabbit and pig livers
- PMID: 8281755
- DOI: 10.1016/0305-0491(93)90137-t
Mammalian glycine N-methyltransferases. Comparative kinetic and structural properties of the enzymes from human, rat, rabbit and pig livers
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.
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