2-Oxoglutarate Dehydrogenase
From Proteopedia
2-Oxoglutarate Dehydrogenase E1o
Template:STRUCTURE 2jgd 2-Oxoglutarate Dehydrogenase E1o is part of the 2-Oxoglutarate Dehydrogenase multi enzyme complex. E1o catalyzes the that catalyzes the the oxidative decarboxylation of alpha-ketoglutarate at its [1]. 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 has an cofactor that facilitates the catalysis. This enzyme is involved in the metabolic citric acid cycle. E1o is not categorized in the Structural Classification of Proteins (SCOP); hoevever, 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]. 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 alow it to react. The exzyme also is part of a larger multienzyme complex that chanells the intermediates in the catalysis between subunits of the complex thus minimizing other reactions.
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
Proteopedia Page Contributors and Editors (what is this?)
Michal Harel, David Canner, Lucas Evans, Alexander Berchansky, Joel L. Sussman