The Role of System-Specific Molecular Chaperones in the Maturation of Molybdoenzymes in Bacteria

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ID: 274981
2011
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Abstract
Biogenesis of prokaryotic molybdoenzymes is a complex process with the final step representing the insertion of a matured molybdenum cofactor (Moco) into a folded apoenzyme. Usually, specific chaperones of the XdhC family are required for the maturation of molybdoenzymes of the xanthine oxidase family in bacteria. Enzymes of the xanthine oxidase family are characterized to contain an equatorial sulfur ligand at the molybdenum center of Moco. This sulfur ligand is inserted into Moco while bound to the XdhC-like protein and before its insertion into the target enzyme. In addition, enzymes of the xanthine oxidase family bind either the molybdopterin (Mo-MPT) form of Moco or the modified molybdopterin cytosine dinucleotide cofactor (MCD). In both cases, only the matured cofactor is inserted by 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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neumann2011thebiochemistry Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors Neumann, Meina;Leimkühler, Silke;
Journal biochemistry research international
Year 2011
DOI
DOI not found
URL
http://dx.doi.org/10.1155/2011/850924
Keywords
chemistry Education Microbiology Biology (General) Medicine (General) special aspects of education biochemistry

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