New Aconitase Enzymes Discovered: AtAcnX and TkAcnX
Scientists have recently discovered two new aconitase enzymes, AtAcnX and TkAcnX, offering fresh insights into the evolution and diversity of this enzyme superfamily. The study, published in 2023, sheds light on the unique features and functions of these digestive enzymes.
AtAcnX and TkAcnX, first identified this year, possess distinct iron-sulfur clusters. AtAcnX contains a planar [2Fe-2S] cluster, while TkAcnX has a cuboidal [3Fe-4S] cluster. Both enzymes recognize substrates through conserved and specific residues, a common trait among aconitases. The aconitase superfamily, which includes four functional enzymes and one hypothetical AcnX, has evolved to encompass single and fragmented polypeptide chain versions of AcnX.
The evolutionary journey of aconitases began with an ancestor lacking an [Fe-S] cluster. Over time, these enzymes have developed similar structures and mechanisms, catalyzing stereospecific isomerization. AtAcnX and TkAcnX, like other aconitases, possess four domains. However, they exhibit unique luster. AcnX from archaea acts as a mevalonate 5-phosphate (MVA5P) dehydratase, while bacterial AcnX functions as a cis-3-hydroxy-L-proline (C3LHyp) dehydratase.
The discovery of AtAcnX and TkAcnX has expanded our understanding of the aconitase superfamily's diversity and evolution. Their unique iron-sulfur clusters and substrate-specific residues highlight the adaptability of these digestive enzymes. Further research is needed to fully understand their roles in their respective organisms and the broader implications for the evolution of the aconitase superfamily.
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