4eca: Difference between revisions
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==About this Structure== | ==About this Structure== | ||
4ECA is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]]. Active as [[http://en.wikipedia.org/wiki/ | 4ECA is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]]. Active as [[http://en.wikipedia.org/wiki/Asparaginase Asparaginase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.1 3.5.1.1]]. Structure known Active Sites: AS, BS, CS and DS. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=4ECA OCA]]. | ||
==Reference== | ==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8706862 8706862] | 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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8706862 8706862] | ||
[[Category: Asparaginase]] | |||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: threonine amidohydrolase]] | [[Category: threonine amidohydrolase]] | ||
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 10:39:17 2007'' | ||
Revision as of 11:34, 30 October 2007
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ASPARAGINASE FROM E. COLI, MUTANT T89V WITH COVALENTLY BOUND ASPARTATE
OverviewOverview
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 StructureAbout this Structure
4ECA is a [Single protein] structure of sequence from [Escherichia coli]. Active as [Asparaginase], with EC number [3.5.1.1]. Structure known Active Sites: AS, BS, CS and DS. Full crystallographic information is available from [OCA].
ReferenceReference
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 Tue Oct 30 10:39:17 2007