Aconitase, a two-faced protein: enzyme and iron regulatory factor.
In this brief survey, the path of development of our knowledge of the iron-sulfur enzyme aconitase [citrate(isocitrate)hydrolyase EC4.2.1.3.] is traced from its discovery in 1937. Particular emphasis is on developments in the past decade, when EPR, Mössbauer and electron nuclear double resonance spectroscopies, X-ray crystallography, and mutational analysis were applied to the problem. More recently discovered was the significant amino acid sequence identity between mitochondrial aconitase and the iron regulatory factor or iron-responsive element binding protein (IRE-BP). This has led to the realization that IRE-BP is an alternative form of cytosolic (not of mitochondrial) aconitase that is devoid of its cubane Fe-S cluster.
Beinert
H
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Department of Biochemistry, Medical College of Wisconsin, Milwaukee 53226.
Kennedy
M C
MC
D000154:Aconitate Hydratase / Q000737:chemistry* / Q000378:metabolism; D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D018360:Crystallography, X-Ray; D007501:Iron / Q000737:chemistry; D035925:Iron-Regulatory Proteins; D016601:RNA-Binding Proteins / Q000737:chemistry / Q000378:metabolism; D013057:Spectrum Analysis; D013237:Stereoisomerism
D035925:Iron-Regulatory Proteins; D016601:RNA-Binding Proteins; D007501:Iron; D000154:Aconitate Hydratase