Bacterial Over-Expression and Purification of the 3'phosphoadenosine 5'phosphosulfate (PAPS) Reductase Domain of Human FAD Synthase: Functional Characterization and Homology Modeling

Bacterial Over-Expression and Purification of the 3'phosphoadenosine 5'phosphosulfate (PAPS) Reductase Domain of Human FAD Synthase: Functional Characterization and Homology Modeling

FAD synthase (FADS, EC 2.7.7.2) is a key enzyme in the metabolic pathway that converts riboflavin into the redox cofactor, FAD. Human FADS is organized in two domains: -the 3'phosphoadenosine 5'phosphosulfate (PAPS) reductase domain, similar to yeast Fad1p, at the C-terminus, and -...

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Bibliographic Details
Main Authors: Maria Barile, Cesare Indiveri, Michele Galluccio, Teresa Anna Giancaspero, Angelica Miccolis
Format: Article
Language:English
Published: MDPI AG 2012-12-01
Series:International Journal of Molecular Sciences
Subjects:
FLAD1
human FAD synthase
FMN adenylyltransferase
Flavin
FAD
PAPS reductase domain
molybdopterin-binding domain
Online Access:http://www.mdpi.com/1422-0067/13/12/16880

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http://www.mdpi.com/1422-0067/13/12/16880

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