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AconitaseAconitase
Aconitase (PDB 2b3x) catalyzes the reversible isomerization of citrate and isocitrate.
Mechanism of AconitaseMechanism of Aconitase
Template:STRUCTURE 2b3x Aconitase contains . This iron sulfur cluster does not participate in redox as most do, but coordinates the OH goup of citrate to facilitate its elimination.[1] It is as this . The rest of the active site is made up of residues . [2]
Stage 1: DehydrationStage 1: Dehydration
First, dehydration of citrate causes a proton and OH group to be removed from only the 'lower arm'.[3] This forms a cis-Aconitate intermediate.
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Stage 2: RehydrationStage 2: Rehydration
The second main stage of the reaction is the rehydration of the cis-Aconitate intermediate. This forms isocitrate. It is catalyzed in a stereospecific way such that only one isocitrate stereoisomer is formed. [4]
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Thus, the overall reaction that aconitase catalyzes is:
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ReferencesReferences
- ↑ Dupuy J, Volbeda A, Carpentier P, Darnault C, Moulis JM, Fontecilla-Camps JC. Crystal structure of human iron regulatory protein 1 as cytosolic aconitase. Structure. 2006 Jan;14(1):129-39. PMID:16407072 doi:10.1016/j.str.2005.09.009
- ↑ Beinert, H., Kennedy, M. C., Stout, C.D. “Aconitase as Iron−Sulfur Protein, Enzyme, and Iron-Regulatory Protein.” Chem. Rev. 1996, 96, 2335−2373.
- ↑ Voet, Donald, Judith G. Voet, and Charlotte W. Pratt. Fundamentals of Biochemistry Life at the Molecular Level. New York: John Wiley & Sons, 2008. p. 578. Print.
- ↑ Voet, Donald, Judith G. Voet, and Charlotte W. Pratt. Fundamentals of Biochemistry Life at the Molecular Level. New York: John Wiley & Sons, 2008. p. 579. Print.
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