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CHAPTER 4

Bacterial Molybdoenzymes: Chaperones, Assembly and Insertion

The biogenesis of molybdoenzymes is a cytoplasmic event requiring both the folded apoenzymes and the matured molybdenum cofactor. The structure and the complexity of the molybdenum cofactor varies in each molybdoenzyme family and consequently different accessory proteins are required for the maturation of the respective enzymes. Thus, for enzymes of both the DMSO reductase and xanthine oxidase families, specific chaperones exist which are dedicated to increase the stability and the folding of specific members of each family. In this review, we describe the role of these chaperones for molybdoenzyme maturation. We present a model which describes step by step the mechanism of the maturation of representative molybdoenzymes from each family.

Publication details

Print publication date
28 Sep 2016
Copyright year
2017
Print ISBN
978-1-78262-089-1
PDF eISBN
978-1-78262-391-5
ePub eISBN
978-1-78262-881-1

From the book series:
Metallobiology