2dpg: Difference between revisions

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==Overview==

The catalytic mechanism of glucose 6-phosphate dehydrogenase from, Leuconostoc mesenteroides was investigated by replacing three amino acids, His-240, Asp-177, and His 178, with asparagine, using site-directed, mutagenesis. Each of the mutant enzymes was purified to homogeneity and, characterized by substrate binding studies and steady-state kinetic, analyses. The three-dimensional structure of the H240N glucose 6-phosphate, dehydrogenase was determined at 2.5 A resolution. The results support a, mechanism in which His-240 acts as the general base that abstracts the, proton from the C1-hydroxyl group of glucose 6-phosphate, and the, carboxylate group of Asp-177 stabilizes the positive charge that forms on, His-240 in the transition state. The results also confirm the postulated, role of His-178 in binding the phosphate moiety of glucose 6-phosphate.

The catalytic mechanism of glucose 6-phosphate dehydrogenase from Leuconostoc mesenteroides was investigated by replacing three amino acids, His-240, Asp-177, and His 178, with asparagine, using site-directed mutagenesis. Each of the mutant enzymes was purified to homogeneity and characterized by substrate binding studies and steady-state kinetic analyses. The three-dimensional structure of the H240N glucose 6-phosphate dehydrogenase was determined at 2.5 A resolution. The results support a mechanism in which His-240 acts as the general base that abstracts the proton from the C1-hydroxyl group of glucose 6-phosphate, and the carboxylate group of Asp-177 stabilizes the positive charge that forms on His-240 in the transition state. The results also confirm the postulated role of His-178 in binding the phosphate moiety of glucose 6-phosphate.

==About this Structure==

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[[Category: Leuconostoc mesenteroides]]

[[Category: Single protein]]

[[Category: Adams, M.J.]]

[[Category: Adams, M J.]]

[[Category: Gover, S.]]

[[Category: Naylor, C.E.]]

[[Category: Naylor, C E.]]

[[Category: Paludin, S.]]

[[Category: NAP]]

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[[Category: oxidoreductase]]

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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:01:11 2008''

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@@ Line 4: / Line 4: @@
 ==Overview==
-The catalytic mechanism of glucose 6-phosphate dehydrogenase from, Leuconostoc mesenteroides was investigated by replacing three amino acids, His-240, Asp-177, and His 178, with asparagine, using site-directed, mutagenesis. Each of the mutant enzymes was purified to homogeneity and, characterized by substrate binding studies and steady-state kinetic, analyses. The three-dimensional structure of the H240N glucose 6-phosphate, dehydrogenase was determined at 2.5 A resolution. The results support a, mechanism in which His-240 acts as the general base that abstracts the, proton from the C1-hydroxyl group of glucose 6-phosphate, and the, carboxylate group of Asp-177 stabilizes the positive charge that forms on, His-240 in the transition state. The results also confirm the postulated, role of His-178 in binding the phosphate moiety of glucose 6-phosphate.
+The catalytic mechanism of glucose 6-phosphate dehydrogenase from Leuconostoc mesenteroides was investigated by replacing three amino acids, His-240, Asp-177, and His 178, with asparagine, using site-directed mutagenesis. Each of the mutant enzymes was purified to homogeneity and characterized by substrate binding studies and steady-state kinetic analyses. The three-dimensional structure of the H240N glucose 6-phosphate dehydrogenase was determined at 2.5 A resolution. The results support a mechanism in which His-240 acts as the general base that abstracts the proton from the C1-hydroxyl group of glucose 6-phosphate, and the carboxylate group of Asp-177 stabilizes the positive charge that forms on His-240 in the transition state. The results also confirm the postulated role of His-178 in binding the phosphate moiety of glucose 6-phosphate.
 ==About this Structure==
@@ Line 14: / Line 14: @@
 [[Category: Leuconostoc mesenteroides]]
 [[Category: Single protein]]
-[[Category: Adams, M.J.]]
+[[Category: Adams, M J.]]
 [[Category: Gover, S.]]
-[[Category: Naylor, C.E.]]
+[[Category: Naylor, C E.]]
 [[Category: Paludin, S.]]
 [[Category: NAP]]
@@ Line 24: / Line 24: @@
 [[Category: oxidoreductase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb  3 10:37:38 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:01:11 2008''