1kee
From Proteopedia
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[[Image:1kee.jpg|left|200px]] | [[Image:1kee.jpg|left|200px]] | ||
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| - | | | + | {{STRUCTURE_1kee| PDB=1kee | SCENE= }} |
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'''Inactivation of the Amidotransferase Activity of Carbamoyl Phosphate Synthetase by the Antibiotic Acivicin''' | '''Inactivation of the Amidotransferase Activity of Carbamoyl Phosphate Synthetase by the Antibiotic Acivicin''' | ||
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==Reference== | ==Reference== | ||
Inactivation of the amidotransferase activity of carbamoyl phosphate synthetase by the antibiotic acivicin., Miles BW, Thoden JB, Holden HM, Raushel FM, J Biol Chem. 2002 Feb 8;277(6):4368-73. Epub 2001 Nov 29. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11729189 11729189] | Inactivation of the amidotransferase activity of carbamoyl phosphate synthetase by the antibiotic acivicin., Miles BW, Thoden JB, Holden HM, Raushel FM, J Biol Chem. 2002 Feb 8;277(6):4368-73. Epub 2001 Nov 29. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11729189 11729189] | ||
| - | [[Category: Carbamoyl-phosphate synthase (glutamine-hydrolyzing)]] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: Raushel, F M.]] | [[Category: Raushel, F M.]] | ||
[[Category: Thoden, J B.]] | [[Category: Thoden, J B.]] | ||
| - | [[Category: | + | [[Category: Antibiotic]] |
| - | [[Category: | + | [[Category: Atp grasp]] |
| - | [[Category: | + | [[Category: Channeling]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 22:38:23 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 19:38, 2 May 2008
Inactivation of the Amidotransferase Activity of Carbamoyl Phosphate Synthetase by the Antibiotic Acivicin
Overview
Carbamoyl phosphate synthetase (CPS) from Escherichia coli catalyzes the formation of carbamoyl phosphate from 2 mol of ATP, bicarbonate, and glutamine. CPS was inactivated by the glutamine analog, acivicin. In the presence of ATP and bicarbonate the second-order rate constant for the inactivation of the glutamine-dependent activities was 4.0 x 10(4) m(-1) s(-1). In the absence of ATP and bicarbonate the second-order rate constant for inactivation of CPS was reduced by a factor of 200. The enzyme was protected against inactivation by the inclusion of glutamine in the reaction mixture. The ammonia-dependent activities were unaffected by the incubation of CPS with acivicin. These results are consistent with the covalent labeling of the glutamine-binding site located within the small amidotransferase subunit. The binding of ATP and bicarbonate to the large subunit of CPS must also induce a conformational change within the amidotransferase domain of the small subunit that enhances the nucleophilic character of the thiol group required for glutamine hydrolysis. The acivicin-inhibited enzyme was crystallized, and the three-dimensional structure was determined by x-ray diffraction techniques. The thiol group of Cys-269 was covalently attached to the dihydroisoxazole ring of acivicin with the displacement of a chloride ion.
About this Structure
1KEE is a Protein complex structure of sequences from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Inactivation of the amidotransferase activity of carbamoyl phosphate synthetase by the antibiotic acivicin., Miles BW, Thoden JB, Holden HM, Raushel FM, J Biol Chem. 2002 Feb 8;277(6):4368-73. Epub 2001 Nov 29. PMID:11729189 Page seeded by OCA on Fri May 2 22:38:23 2008
