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Bacterial Molybdoenzymes: Chaperones, Assembly and Insertion

Abstract : 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
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https://hal-amu.archives-ouvertes.fr/hal-01446287
Contributor : Laure Azzopardi <>
Submitted on : Wednesday, January 25, 2017 - 5:04:40 PM
Last modification on : Thursday, January 25, 2018 - 6:26:02 PM

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Silke Leimkuhler, Olivier Lemaire, Chantal Iobbi-Nivol. Bacterial Molybdoenzymes: Chaperones, Assembly and Insertion. (Hille R. ed), Chapter IV, RSC Publishing group, Molybdenum and Tungsten Enzymes : Biochemistry, pp.117-142, 2016, Bacterial Molybdoenzymes: Chaperones, Assembly and Insertion, 978-1-78262-089-1. ⟨10.1039/9781782623915-00117⟩. ⟨hal-01446287⟩

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