4eca

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{{STRUCTURE_4eca| PDB=4eca | SCENE= }}
{{STRUCTURE_4eca| PDB=4eca | SCENE= }}
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'''ASPARAGINASE FROM E. COLI, MUTANT T89V WITH COVALENTLY BOUND ASPARTATE'''
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===ASPARAGINASE FROM E. COLI, MUTANT T89V WITH COVALENTLY BOUND ASPARTATE===
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==Overview==
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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.
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{{ABSTRACT_PUBMED_8706862}}
==About this Structure==
==About this Structure==
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[[Category: Hydrolase]]
[[Category: Hydrolase]]
[[Category: Threonine amidohydrolase]]
[[Category: Threonine amidohydrolase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 22:23:17 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jul 3 13:35:20 2008''

Revision as of 10:35, 3 July 2008

Image:4eca.png

Template:STRUCTURE 4eca

ASPARAGINASE FROM E. COLI, MUTANT T89V WITH COVALENTLY BOUND ASPARTATE

Template:ABSTRACT PUBMED 8706862

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

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