2dpg
From Proteopedia
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==Overview== | ==Overview== | ||
| - | The catalytic mechanism of glucose 6-phosphate dehydrogenase from | + | The catalytic mechanism of glucose 6-phosphate dehydrogenase from Leuconostoc mesenteroides was investigated by replacing three amino acids, His-240, Asp-177, and His 178, with asparagine, using site-directed mutagenesis. Each of the mutant enzymes was purified to homogeneity and characterized by substrate binding studies and steady-state kinetic analyses. The three-dimensional structure of the H240N glucose 6-phosphate dehydrogenase was determined at 2.5 A resolution. The results support a mechanism in which His-240 acts as the general base that abstracts the proton from the C1-hydroxyl group of glucose 6-phosphate, and the carboxylate group of Asp-177 stabilizes the positive charge that forms on His-240 in the transition state. The results also confirm the postulated role of His-178 in binding the phosphate moiety of glucose 6-phosphate. |
==About this Structure== | ==About this Structure== | ||
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[[Category: Leuconostoc mesenteroides]] | [[Category: Leuconostoc mesenteroides]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Adams, M | + | [[Category: Adams, M J.]] |
[[Category: Gover, S.]] | [[Category: Gover, S.]] | ||
| - | [[Category: Naylor, C | + | [[Category: Naylor, C E.]] |
[[Category: Paludin, S.]] | [[Category: Paludin, S.]] | ||
[[Category: NAP]] | [[Category: NAP]] | ||
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[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:01:11 2008'' |
Revision as of 15:01, 21 February 2008
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COMPLEX OF INACTIVE MUTANT (H240->N) OF GLUCOSE 6-PHOSPHATE DEHYDROGENASE FROM LEUCONOSTOC MESENTEROIDES WITH NADP+
Overview
The catalytic mechanism of glucose 6-phosphate dehydrogenase from Leuconostoc mesenteroides was investigated by replacing three amino acids, His-240, Asp-177, and His 178, with asparagine, using site-directed mutagenesis. Each of the mutant enzymes was purified to homogeneity and characterized by substrate binding studies and steady-state kinetic analyses. The three-dimensional structure of the H240N glucose 6-phosphate dehydrogenase was determined at 2.5 A resolution. The results support a mechanism in which His-240 acts as the general base that abstracts the proton from the C1-hydroxyl group of glucose 6-phosphate, and the carboxylate group of Asp-177 stabilizes the positive charge that forms on His-240 in the transition state. The results also confirm the postulated role of His-178 in binding the phosphate moiety of glucose 6-phosphate.
About this Structure
2DPG is a Single protein structure of sequence from Leuconostoc mesenteroides with as ligand. Active as Glucose-6-phosphate 1-dehydrogenase, with EC number 1.1.1.49 Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
On the mechanism of the reaction catalyzed by glucose 6-phosphate dehydrogenase., Cosgrove MS, Naylor C, Paludan S, Adams MJ, Levy HR, Biochemistry. 1998 Mar 3;37(9):2759-67. PMID:9485426
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