Sandbox Reserved 1094
From Proteopedia
(Difference between revisions)
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== Evolutionary conservation == | == Evolutionary conservation == | ||
The different structures conserved evolutionary can be observed according to the scale following. | The different structures conserved evolutionary can be observed according to the scale following. | ||
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[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Check<jmol> | Check<jmol> | ||
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Depending on several conditions, it can dimerize to form tetramers. Each monomer in the complex has a substrate binding site that binds to G6P, and a catalytic coenzyme binding site that binds to NADP+/NADPH using the Rossman fold. | Depending on several conditions, it can dimerize to form tetramers. Each monomer in the complex has a substrate binding site that binds to G6P, and a catalytic coenzyme binding site that binds to NADP+/NADPH using the Rossman fold. | ||
| - | This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. | + | This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. |
</StructureSection> | </StructureSection> | ||
== References == | == References == | ||
<references/> | <references/> | ||
| - | 3. Ravera S., Calzia D., Morelli A. et Panfoli I. 2010. Oligomerization studies of Leuconostoc mesenteroides G6PD activity after SDS-PAGE and blotting. Molekuliarnaia Biologiia. 44(3):472-6. | ||
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| - | 4. Cosgrove MS., Naylor C., Paludan S., Adams MJ. et Levy HR. 1998. On the mechanism of the reaction catalyzed by glucose 6-phosphate dehydrogenase. Biochemistry. 37(9):2759-67. | ||
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| - | 5. Cosgrove MS., Loh SN., Ha JH. et Levy HR. 2002. The catalytic mechanism of glucose 6-phosphate dehydrogenases: assignment and 1H NMR spectroscopy pH titration of the catalytic histidine residue in the 109 kDa Leuconostoc mesenteroides enzyme. Biochemistry. 41(22):6939-45. | ||
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| - | 6. Rowland P, Basak AK, Gover S, Levy HR, Adams MJ. The three-dimensional structure of glucose 6-phosphate dehydrogenase from Leuconostoc | ||
| - | mesenteroides refined at 2.0 A resolution. Structure. 1994 Nov 15;2(11):1073-87. | ||
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== Proteopedia page contributors and editors == | == Proteopedia page contributors and editors == | ||
DONATI Quentin, LOGEREAU Lucie, PROST Loana | DONATI Quentin, LOGEREAU Lucie, PROST Loana | ||
Revision as of 14:52, 14 January 2020
| This Sandbox is Reserved from 25/11/2019, through 30/9/2020 for use in the course "Structural Biology" taught by Bruno Kieffer at the University of Strasbourg, ESBS. This reservation includes Sandbox Reserved 1091 through Sandbox Reserved 1115. |
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Glucose-6-Phosphate Dehydrogenase from Leuconostoc mesenteroides
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References
- ↑ Ravera S, Calzia D, Morelli A, Panfoli I. Oligomerization studies of Leuconostoc mesenteroides G6PD activity after SDS-PAGE and blotting. Mol Biol (Mosk). 2010 May-Jun;44(3):472-6. PMID:20608171
- ↑ Cosgrove MS, Naylor C, Paludan S, Adams MJ, Levy HR. On the mechanism of the reaction catalyzed by glucose 6-phosphate dehydrogenase. Biochemistry. 1998 Mar 3;37(9):2759-67. PMID:9485426 doi:10.1021/bi972069y
- ↑ Cosgrove MS, Loh SN, Ha JH, Levy HR. The catalytic mechanism of glucose 6-phosphate dehydrogenases: assignment and 1H NMR spectroscopy pH titration of the catalytic histidine residue in the 109 kDa Leuconostoc mesenteroides enzyme. Biochemistry. 2002 Jun 4;41(22):6939-45. doi: 10.1021/bi0255219. PMID:12033926 doi:http://dx.doi.org/10.1021/bi0255219
- ↑ Rowland P, Basak AK, Gover S, Levy HR, Adams MJ. The three-dimensional structure of glucose 6-phosphate dehydrogenase from Leuconostoc mesenteroides refined at 2.0 A resolution. Structure. 1994 Nov 15;2(11):1073-87. PMID:7881907
Proteopedia page contributors and editors
DONATI Quentin, LOGEREAU Lucie, PROST Loana

