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

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 fami...

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Main Authors: Meina Neumann, Silke Leimkühler
Format: Article
Language:English
Published: Wiley 2011-01-01
Series:Biochemistry Research International
Online Access:http://dx.doi.org/10.1155/2011/850924
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author Meina Neumann
Silke Leimkühler
author_facet Meina Neumann
Silke Leimkühler
author_sort Meina Neumann
collection DOAJ
description 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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spelling doaj-art-02a6360787894b8c888d1a97e6b4ae7f2025-02-03T01:26:13ZengWileyBiochemistry Research International2090-22472090-22552011-01-01201110.1155/2011/850924850924The Role of System-Specific Molecular Chaperones in the Maturation of Molybdoenzymes in BacteriaMeina Neumann0Silke Leimkühler1Department of Molecular Enzymology, Institute of Biochemistry and Biology, University of Potsdam, 14476 Potsdam, GermanyDepartment of Molecular Enzymology, Institute of Biochemistry and Biology, University of Potsdam, 14476 Potsdam, GermanyBiogenesis 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.http://dx.doi.org/10.1155/2011/850924
spellingShingle Meina Neumann
Silke Leimkühler
The Role of System-Specific Molecular Chaperones in the Maturation of Molybdoenzymes in Bacteria
Biochemistry Research International
title The Role of System-Specific Molecular Chaperones in the Maturation of Molybdoenzymes in Bacteria
title_full The Role of System-Specific Molecular Chaperones in the Maturation of Molybdoenzymes in Bacteria
title_fullStr The Role of System-Specific Molecular Chaperones in the Maturation of Molybdoenzymes in Bacteria
title_full_unstemmed The Role of System-Specific Molecular Chaperones in the Maturation of Molybdoenzymes in Bacteria
title_short The Role of System-Specific Molecular Chaperones in the Maturation of Molybdoenzymes in Bacteria
title_sort role of system specific molecular chaperones in the maturation of molybdoenzymes in bacteria
url http://dx.doi.org/10.1155/2011/850924
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