2-Oxoglutarate Dehydrogenase
From Proteopedia
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{{STRUCTURE_ 2jgd | PDB= 2jgd | SCENE= }} | {{STRUCTURE_ 2jgd | PDB= 2jgd | SCENE= }} | ||
| - | 2-Oxoglutarate Dehydrogenase E1o is part of the 2-Oxoglutarate Dehydrogenase multi enzyme complex. E1o catalyzes | + | 2-Oxoglutarate Dehydrogenase E1o is part of the 2-Oxoglutarate Dehydrogenase multi enzyme complex. E1o catalyzes the oxidative decarboxylation of alpha-ketoglutarate at its |
| - | <scene name='Lucas_Evans_Sandbox/Active_site/1'>active site</scene> | + | <scene name='Lucas_Evans_Sandbox/Active_site/1'>active site</scene> in the metabolic citric acid cycle. This subunit is a homo-dimer and one of three enzymes that make up the multi-enzyme complex of 2-Oxoglutarate Dehydrogenase. Each of the <scene name='Lucas_Evans_Sandbox/Monomer/2'>monomers</scene> that make up the homo-dimer have an <scene name='Lucas_Evans_Sandbox/Amp1/1'>adenosine monophosphate</scene> cofactor that facilitates the catalysis. This enzyme catalyzes the oxidative decarboxylation by keeping the necessary substrates for the reaction close within the enzyme so that it is more likely that the substrate will be in a conformation that will allow it to react. This enzyme is also part of a larger multienzyme complex that chanells the intermediates in the catalysis between subunits of the complex thus minimizing unwanted side reactions<ref>Voet, Donald, Judith G. Voet, and Charlotte W. Pratt. Fundamentals of Biochemistry: Life at the Molecular Level. Hoboken, NJ: Wiley, 2008. </ref>. E1o is not categorized in the Structural Classification of Proteins (SCOP); however, the <scene name='Lucas_Evans_Sandbox/Secondary_structure/2'>secondary structure</scene> of one of the dimers shows that this enzyme has large sections of alpha-helices followed by a large section of parallel beta-pleated sheets these alpha and beta subunits are fused as a single polypeptide <ref>PMID:17367808</ref>. |
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==References== | ==References== | ||
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Revision as of 22:52, 1 March 2010
2-Oxoglutarate Dehydrogenase E1o
Template:STRUCTURE 2jgd 2-Oxoglutarate Dehydrogenase E1o is part of the 2-Oxoglutarate Dehydrogenase multi enzyme complex. E1o catalyzes the oxidative decarboxylation of alpha-ketoglutarate at its in the metabolic citric acid cycle. This subunit is a homo-dimer and one of three enzymes that make up the multi-enzyme complex of 2-Oxoglutarate Dehydrogenase. Each of the that make up the homo-dimer have an cofactor that facilitates the catalysis. This enzyme catalyzes the oxidative decarboxylation by keeping the necessary substrates for the reaction close within the enzyme so that it is more likely that the substrate will be in a conformation that will allow it to react. This enzyme is also part of a larger multienzyme complex that chanells the intermediates in the catalysis between subunits of the complex thus minimizing unwanted side reactions[1]. E1o is not categorized in the Structural Classification of Proteins (SCOP); however, the of one of the dimers shows that this enzyme has large sections of alpha-helices followed by a large section of parallel beta-pleated sheets these alpha and beta subunits are fused as a single polypeptide [2].
References
- ↑ Voet, Donald, Judith G. Voet, and Charlotte W. Pratt. Fundamentals of Biochemistry: Life at the Molecular Level. Hoboken, NJ: Wiley, 2008.
- ↑ Frank RA, Price AJ, Northrop FD, Perham RN, Luisi BF. Crystal structure of the E1 component of the Escherichia coli 2-oxoglutarate dehydrogenase multienzyme complex. J Mol Biol. 2007 May 4;368(3):639-51. Epub 2007 Feb 7. PMID:17367808 doi:10.1016/j.jmb.2007.01.080
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