Sandbox Reserved 1094

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Its regulation depends on the concentration of substrate and coenzyme, rate limiting step in pentose phosphate pathway<ref>PMID: 12033926</ref>.
Its regulation depends on the concentration of substrate and coenzyme, rate limiting step in pentose phosphate pathway<ref>PMID: 12033926</ref>.
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== Optimal activity conditions ==
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Optimum pH for its activity is 5.4 - 8.9.
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Optimum pH is 5.4 - 8.9.
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== Evolutionary conservation ==
== Evolutionary conservation ==

Revision as of 15:04, 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

Caption for this structure

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References

  1. ↑ 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
  2. ↑ GeneID:29577449
  3. ↑ 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
  4. ↑ 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
  5. ↑ 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

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DONATI Quentin, LOGEREAU Lucie, PROST Loana

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