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The role of system specific molecular chaperones in the maturation of bacterial molybdate enzymes

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Document pages: 13 pages

Abstract: The biogenesis of prokaryotic molybdate enzyme is a complex process. The last step is to insert the mature molybdenum cofactor (Moco) into the folded deconzyme. In general, the maturation of molybdate enzymes of xanthine oxidase family in bacteria requires a specific partner of xdhc family. Xanthine oxidase family enzymes are characterized by equatorial sulfur ligands in the molybdenum center of Moco. The sulfur ligand is inserted into Moco when binding to xdhc like protein and before inserting the target enzyme. In addition, enzymes of the xanthine oxidase family bind to Moco s Molybdenum methotrexate (Mo MPT) form or modified molybdenum methotrexate cytosine dinucleotide cofactor (MCD). In both cases, only mature cofactors were inserted into B a proofreading process of XdhC. The roles of these specific XdhC-like chaperones during the biogenesis of enzymes of the xanthine oxidase family in bacteria are described.

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