1r74: Difference between revisions

Line 4:

==Overview==

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.

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.

==Disease==

Line 18:

[[Category: Single protein]]

[[Category: Luka, Z.]]

[[Category: Newcomer, M.E.]]

[[Category: Newcomer, M E.]]

[[Category: Pakhomova, S.]]

[[Category: Wagner, C.]]

Line 26:

[[Category: human]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri~~ Feb ~~15 16~~:47:18 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:47:48 2008''

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 4: / Line 4: @@
 ==Overview==
-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.
+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.
 ==Disease==
@@ Line 18: / Line 18: @@
 [[Category: Single protein]]
 [[Category: Luka, Z.]]
-[[Category: Newcomer, M.E.]]
+[[Category: Newcomer, M E.]]
 [[Category: Pakhomova, S.]]
 [[Category: Wagner, C.]]
@@ Line 26: / Line 26: @@
 [[Category: human]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:47:18 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:47:48 2008''