2dpg: Difference between revisions

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[[Image:2dpg.~~jpg~~|left|200px]]

[[Image:2dpg.png|left|200px]]

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~~'''~~COMPLEX OF INACTIVE MUTANT (H240->N) OF GLUCOSE 6-PHOSPHATE DEHYDROGENASE FROM LEUCONOSTOC MESENTEROIDES WITH NADP+~~'''~~

===COMPLEX OF INACTIVE MUTANT (H240->N) OF GLUCOSE 6-PHOSPHATE DEHYDROGENASE FROM LEUCONOSTOC MESENTEROIDES WITH NADP+===

~~==Overview==~~

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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.~~

The line below this paragraph, {{ABSTRACT_PUBMED_9485426}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 9485426 is the PubMed ID number.

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==About this Structure==

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[[Category: Nadp/nad]]

[[Category: Oxidoreductase]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sun May 4 00~~:54:48 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 01:36:18 2008''

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-[[Image:2dpg.jpg|left|200px]]
+{{Seed}}
+[[Image:2dpg.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_2dpg|  PDB=2dpg  |  SCENE=  }}
-'''COMPLEX OF INACTIVE MUTANT (H240->N) OF GLUCOSE 6-PHOSPHATE DEHYDROGENASE FROM LEUCONOSTOC MESENTEROIDES WITH NADP+'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_9485426}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 9485426 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_9485426}}
 ==About this Structure==
@@ Line 30: / Line 34: @@
 [[Category: Nadp/nad]]
 [[Category: Oxidoreductase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 00:54:48 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 01:36:18 2008''