期刊
PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS
卷 57, 期 2, 页码 331-337出版社
WILEY
DOI: 10.1002/prot.20209
关键词
glycine N-methyltransferase; X-ray crystallography; conformations; kinetics
资金
- NIDDK NIH HHS [DK15289] Funding Source: Medline
- NIGMS NIH HHS [GM55420] Funding Source: Medline
- PHS HHS [DJ54859] Funding Source: Medline
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 k(cat) when going from rat to mouse to human, suggesting a correlation with the increased flexibility of some structural elements of the respective enzymes. (C) 2004 Wiley-Liss, Inc.
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