Glycine N-methyltransferases: a comparison of the crystal structures and kinetic properties of recombinant human, mouse and rat enzymes

Proteins
Svetlana PakhomovaMarcia E Newcomer

Abstract

Glycine N-methyltransferases (GNMTs) from three mammalian sources were compared with respect to their crystal structures and kinetic parameters. The crystal structure for the rat enzyme was published previously. Human and mouse GNMT were expressed in Escherichia coli in order to determine their crystal structures. Mouse GNMT was crystallized in two crystal forms, a monoclinic form and a tetragonal form. Comparison of the three structures reveals subtle differences, which may relate to the different kinetic properties of the enzymes. The flexible character of several loops surrounding the active site, along with an analysis of the active site boundaries, indicates that the observed conformations of human and mouse GNMTs are more open than that of the rat enzyme. There is an increase in kcat when going from rat to mouse to human, suggesting a correlation with the increased flexibility of some structural elements of the respective enzymes.

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Citations

Jun 27, 2012·Proceedings of the National Academy of Sciences of the United States of America·Gabriel M SimonJeffrey I Gordon
Jun 2, 2009·The Journal of Biological Chemistry·Zigmund LukaConrad Wagner
Nov 14, 2012·Toxicology and Applied Pharmacology·Chia-Hung YenYi-Ming Arthur Chen
Apr 13, 2010·Trends in Biochemical Sciences·Karen Rutherford, Valerie Daggett
May 27, 2008·Biochimica Et Biophysica Acta·Zigmund LukaConrad Wagner
Jul 31, 2007·Protein Science : a Publication of the Protein Society·Zigmund LukaConrad Wagner
Jul 16, 2014·The Journal of Nutritional Biochemistry·Malav S TrivediRichard C Deth
Apr 8, 2020·The FEBS Journal·Sofia S MariasinaVladimir I Polshakov

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