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4eca
From Proteopedia
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[[Image:4eca.jpg|left|200px]] | [[Image:4eca.jpg|left|200px]] | ||
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'''ASPARAGINASE FROM E. COLI, MUTANT T89V WITH COVALENTLY BOUND ASPARTATE''' | '''ASPARAGINASE FROM E. COLI, MUTANT T89V WITH COVALENTLY BOUND ASPARTATE''' | ||
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[[Category: Palm, G J.]] | [[Category: Palm, G J.]] | ||
[[Category: Wlodawer, A.]] | [[Category: Wlodawer, A.]] | ||
| - | [[Category: | + | [[Category: Acyl-enzyme intermediate]] |
| - | [[Category: | + | [[Category: Hydrolase]] |
| - | [[Category: | + | [[Category: Threonine amidohydrolase]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 22:23:17 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 19:23, 4 May 2008
ASPARAGINASE FROM E. COLI, MUTANT T89V WITH COVALENTLY BOUND ASPARTATE
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.
About this Structure
4ECA is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
A covalently bound catalytic intermediate in Escherichia coli asparaginase: crystal structure of a Thr-89-Val mutant., Palm GJ, Lubkowski J, Derst C, Schleper S, Rohm KH, Wlodawer A, FEBS Lett. 1996 Jul 22;390(2):211-6. PMID:8706862 Page seeded by OCA on Sun May 4 22:23:17 2008
