Steric and conformational features of the aconitase mechanism

@article{Lauble1995StericAC,
  title={Steric and conformational features of the aconitase mechanism},
  author={Hanspeter Lauble and Charles David Stout},
  journal={Proteins: Structure},
  year={1995},
  volume={22}
}
Crystal structures of mitochondrial aconitase with α‐methylisocitrate and with sulfate bound have been solved and refined at 2.0 Å resolution with R factors of 18.2 and 16.8%, respectively. The steric factors and conformational effects observed in both new structures support the proposed mechanism for the overall reaction catalyzed by aconitase. The alternate substrate α;methylisocitrate is derived from α;methyl‐cis‐aconitate during crystallization and is observed to bind in the active site in… Expand
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The structure of activated pig heart aconitase [citrate(isocitrate) hydro-lyase, EC 4.2.1.3] containing a [4Fe-4S] cluster has been refined at 2.5-A resolution to a crystallographic residual ofExpand
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Publisher Summary This chapter describes an iron–sulfur enzyme—aconitase. Although the presence and function of the Krebs cycle enzyme aconitase has been known for over 50 years, it is only recentlyExpand
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