Aconitase: Difference between revisions
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In most organims, there is a cytosolic enzyme with an ACO domain (cAc), and in eukaryotes, a second copy of it was introduced with mitochondria (mAc). Plants developed even more copies in mitochondria. | In most organims, there is a cytosolic enzyme with an ACO domain (cAc), and in eukaryotes, a second copy of it was introduced with mitochondria (mAc). Plants developed even more copies in mitochondria. | ||
<applet load='Morph_2ipy-2b3x.pdb.gz' scene='Aconitase/2ipy-total/2' size='400' frame='true' align='right' caption="" />A specialty of cAc is that in mammals it has developed a <scene name='Aconitase/2ipy-total/2'>second function</scene> as inhibitor of <scene name='Aconitase/2ipy-rna/1'>those mRNA</scene> that carry an <scene name='Aconitase/2ipy-rna-ire/1'>iron-regulatory element (IRE)</scene>. Therefore, the cytosolic cAc is named IREBP for IRE-binding protein when this function is talked about. Only one of the two functions is active, depending on whether <scene name='Aconitase/2b3x-cluster/1'>the (4Fe4S) cofactor</scene> is present in the molecule: it's essential for <scene name='Aconitase/2b3x-total/1'>the ACO function</scene>. You can see, by <scene name='Aconitase/Morph/ | <applet load='Morph_2ipy-2b3x.pdb.gz' scene='Aconitase/2ipy-total/2' size='400' frame='true' align='right' caption="" />A specialty of cAc is that in mammals it has developed a <scene name='Aconitase/2ipy-total/2'>second function</scene> as inhibitor of <scene name='Aconitase/2ipy-rna/1'>those mRNA</scene> that carry an <scene name='Aconitase/2ipy-rna-ire/1'>iron-regulatory element (IRE)</scene>. Therefore, the cytosolic cAc is named IREBP for IRE-binding protein when this function is talked about. Only one of the two functions is active, depending on whether <scene name='Aconitase/2b3x-cluster/1'>the (4Fe4S) cofactor</scene> is present in the molecule: it's essential for <scene name='Aconitase/2b3x-total/1'>the ACO function</scene>. You can see, by <scene name='Aconitase/Morph/2'>looking at the morph</scene>, how much the enzyme structure differs between those two functions. | ||
<!--== Available structures == | <!--== Available structures == | ||
Revision as of 10:37, 18 February 2009
Aconitase (ACO) is an enzymatic domain that confers the ability to catalyse the equilibrium
- citrate = aconitate + H2O = isocitrate
This reaction is part of the citrate (TCA-, Krebs-)cycle.
In most organims, there is a cytosolic enzyme with an ACO domain (cAc), and in eukaryotes, a second copy of it was introduced with mitochondria (mAc). Plants developed even more copies in mitochondria.
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A specialty of cAc is that in mammals it has developed a second function as inhibitor of those mRNA that carry an iron-regulatory element (IRE). Therefore, the cytosolic cAc is named IREBP for IRE-binding protein when this function is talked about. Only one of the two functions is active, depending on whether the (4Fe4S) cofactor is present in the molecule: it's essential for the ACO function. You can see, by looking at the morph, how much the enzyme structure differs between those two functions.
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Anthony Noles, Ralf Stephan, Alexander Berchansky, David Canner, Eran Hodis, Angel Herraez, Jaime Prilusky, Michal Harel, Joel L. Sussman
