2-Oxoglutarate Dehydrogenase
From Proteopedia
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{{STRUCTURE_ 2jgd | PDB= 2jgd | SCENE= }} | {{STRUCTURE_ 2jgd | PDB= 2jgd | SCENE= }} | ||
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| - | + | The enzyme 2-Oxoglutarate Dehydrogenase E1o is a subunit the 2-Oxoglutarate Dehydrogenase multi enzyme complex. 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. 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 sections of parallel beta-pleated sheets these alpha and beta subunits are fused as a single polypeptide <ref name="one">PMID:17367808 </ref>. | |
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| + | E1o catalyzes the oxidative decarboxylation of alpha-ketoglutarate at its <scene name='Lucas_Evans_Sandbox/Active_site/1'>active site</scene> in the metabolic citric acid cycle by acting as a base to facilitate the decarboxylation <ref name="one" />. The main residues responsible for the catalysis are thought to be His 260, Phe 227, Gln685, His 729, Ser302, and His 298 <ref name="one" />. The overall complex (all of the sub units) help catalysis by keeping the necessary substrates for the reaction close within the enzyme so that it is more likely that the substrate will be in favorable conformation. This enzyme is also part of a larger multienzyme complex that channels 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. p.580</ref>. Not only do the subunits ferry products back and forth but each of the mers in the E1o homodimer are connected via a cavity lined with acidic residues thus increasing the dimer's ability to act as a base. | ||
==References== | ==References== | ||
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Revision as of 23:17, 31 March 2010
2-Oxoglutarate Dehydrogenase E1o
The enzyme 2-Oxoglutarate Dehydrogenase E1o is a subunit the 2-Oxoglutarate Dehydrogenase multi enzyme complex. 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. 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 sections of parallel beta-pleated sheets these alpha and beta subunits are fused as a single polypeptide [1].
E1o catalyzes the oxidative decarboxylation of alpha-ketoglutarate at its in the metabolic citric acid cycle by acting as a base to facilitate the decarboxylation [1]. The main residues responsible for the catalysis are thought to be His 260, Phe 227, Gln685, His 729, Ser302, and His 298 [1]. The overall complex (all of the sub units) help catalysis by keeping the necessary substrates for the reaction close within the enzyme so that it is more likely that the substrate will be in favorable conformation. This enzyme is also part of a larger multienzyme complex that channels the intermediates in the catalysis between subunits of the complex thus minimizing unwanted side reactions[2]. Not only do the subunits ferry products back and forth but each of the mers in the E1o homodimer are connected via a cavity lined with acidic residues thus increasing the dimer's ability to act as a base.
References
- ↑ 1.0 1.1 1.2 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
- ↑ Voet, Donald, Judith G. Voet, and Charlotte W. Pratt. Fundamentals of Biochemistry: Life at the Molecular Level. Hoboken, NJ: Wiley, 2008. p.580
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