Krupa, Ananth and Sandhya, Kumaraswamy and Srinivasan, Narayanaswamy and Jonnalagadda, Sobhanaditya (2003) A conserved domain in prokaryotic bifunctional FAD synthetases can potentially catalyze nucleotide transfer. In: Trends in Biochemical Sciences, 28 (1). pp. 9-12.
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Biosynthesis of flavin adenine dinucleotides in most prokaryotes is catalyzed by a family of bifunctional flavin adenine dinucleotide (FAD) synthetases. These enzymes carry out the dual functions of phosphorylation of flavin mononucleotide (FMN) and its subsequent adenylylation to generate FAD. Using various sequence analysis methods, a new domain has been identified in the N-terminal region that is well conserved in all the bacterial FAD synthetases. We also identify remote similarity of this domain to the nucleotidyl transferases and, hence, this domain is suggested to be invloved in the adenylylation reaction of FAD synthetases.
|Item Type:||Journal Article|
|Additional Information:||The copyright belongs to Elsevier Science Ltd.|
|Department/Centre:||Division of Biological Sciences > Molecular Biophysics Unit|
|Date Deposited:||24 Oct 2007|
|Last Modified:||19 Sep 2010 04:40|
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