4eca: Difference between revisions

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==Overview==

Escherichia coli asparaginase II catalyzes the hydrolysis of L-asparagine, to L-aspartate via a threonine-bound acyl-enzyme intermediate. A nearly, inactive mutant in which one of the active site threonines, Thr-89, was, replaced by valine was constructed, expressed, and crystallized. Its, structure, solved at 2.2 A resolution, shows high overall similarity to, the wild-type enzyme, but an aspartyl moiety is covalently bound to, Thr-12, resembling a reaction intermediate. Kinetic analysis confirms the, deacylation deficiency, which is also explained on a structural basis. The, previously identified oxyanion hole is described in more detail.

Escherichia coli asparaginase II catalyzes the hydrolysis of L-asparagine to L-aspartate via a threonine-bound acyl-enzyme intermediate. A nearly inactive mutant in which one of the active site threonines, Thr-89, was replaced by valine was constructed, expressed, and crystallized. Its structure, solved at 2.2 A resolution, shows high overall similarity to the wild-type enzyme, but an aspartyl moiety is covalently bound to Thr-12, resembling a reaction intermediate. Kinetic analysis confirms the deacylation deficiency, which is also explained on a structural basis. The previously identified oxyanion hole is described in more detail.

==About this Structure==

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[[Category: Single protein]]

[[Category: Lubkowski, J.]]

[[Category: Palm, G.J.]]

[[Category: Palm, G J.]]

[[Category: Wlodawer, A.]]

[[Category: acyl-enzyme intermediate]]

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[[Category: threonine amidohydrolase]]

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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:13:09 2008''

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@@ Line 4: / Line 4: @@
 ==Overview==
-Escherichia coli asparaginase II catalyzes the hydrolysis of L-asparagine, to L-aspartate via a threonine-bound acyl-enzyme intermediate. A nearly, inactive mutant in which one of the active site threonines, Thr-89, was, replaced by valine was constructed, expressed, and crystallized. Its, structure, solved at 2.2 A resolution, shows high overall similarity to, the wild-type enzyme, but an aspartyl moiety is covalently bound to, Thr-12, resembling a reaction intermediate. Kinetic analysis confirms the, deacylation deficiency, which is also explained on a structural basis. The, previously identified oxyanion hole is described in more detail.
+Escherichia coli asparaginase II catalyzes the hydrolysis of L-asparagine to L-aspartate via a threonine-bound acyl-enzyme intermediate. A nearly inactive mutant in which one of the active site threonines, Thr-89, was replaced by valine was constructed, expressed, and crystallized. Its structure, solved at 2.2 A resolution, shows high overall similarity to the wild-type enzyme, but an aspartyl moiety is covalently bound to Thr-12, resembling a reaction intermediate. Kinetic analysis confirms the deacylation deficiency, which is also explained on a structural basis. The previously identified oxyanion hole is described in more detail.
 ==About this Structure==
@@ Line 15: / Line 15: @@
 [[Category: Single protein]]
 [[Category: Lubkowski, J.]]
-[[Category: Palm, G.J.]]
+[[Category: Palm, G J.]]
 [[Category: Wlodawer, A.]]
 [[Category: acyl-enzyme intermediate]]
@@ Line 21: / Line 21: @@
 [[Category: threonine amidohydrolase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb  3 10:52:51 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:13:09 2008''