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Aconitase

Mechanism of Aconitase

Template:STRUCTURE 2b3x

Stage 1: Dehydration

Aconitase (PDB 2b3x) catalyzes the reversible isomerization of citrate and isocitrate. First, dehydration of citrate causes a proton and OH group to be removed from only the 'lower arm'.[1] This forms a cis-Aconitate intermediate.

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Aconitase contains 4Fe-4S iron-sulfur cluster. This iron sulfur cluster does not participate in redox as most do, but coordinates the OH goup of citrate to facilitate its elimination.[2]

Stage 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. [3]

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Thus, the overall reaction that aconitase catalyzes is:

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References

  1. 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.
  2. 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
  3. 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.

External Links

Aconitase on Wikipedia

Aconitase on Proteopedia


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